CNRS Nantes University UFIP UFIP
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***  1uet  ***

elNémo ID: 2004292100249921

Job options:

ID        	=	 2004292100249921
JOBID     	=	 1uet
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1uet

HEADER    TRANSFERASE                             21-MAY-03   1UET              
TITLE     DIVERGENT EVOLUTIONS OF TRINUCLEOTIDE POLYMERIZATION REVEALED BY AN   
TITLE    2 ARCHAEAL CCA-ADDING ENZYME STRUCTURE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRNA NUCLEOTIDYLTRANSFERASE;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.7.25;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    TRANSFERASE, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,   
KEYWDS   2 STRUCTURAL GENOMICS                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.NUREKI,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)       
REVDAT   3   13-JUL-11 1UET    1       VERSN                                    
REVDAT   2   24-FEB-09 1UET    1       VERSN                                    
REVDAT   1   02-DEC-03 1UET    0                                                
JRNL        AUTH   M.OKABE,K.TOMITA,R.ISHITANI,R.ISHII,N.TAKEUCHI,F.ARISAKA,    
JRNL        AUTH 2 O.NUREKI,S.YOKOYAMA                                          
JRNL        TITL   DIVERGENT EVOLUTIONS OF TRINUCLEOTIDE POLYMERIZATION         
JRNL        TITL 2 REVEALED BY AN ARCHAEAL CCA-ADDING ENZYME STRUCTURE.         
JRNL        REF    EMBO J.                       V.  22  5918 2003              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   14592988                                                     
JRNL        DOI    10.1093/EMBOJ/CDG563                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1969248.820                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 32180                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3221                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4507                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE                    : 0.2530                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 490                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3559                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 304                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.07000                                             
REMARK   3    B22 (A**2) : 4.76000                                              
REMARK   3    B33 (A**2) : -3.70000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.95000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.16                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.97                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.860 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.730 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.560 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.160 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 53.89                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ACETATE.PARAM                                  
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ACETAET.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB005744.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.974                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32180                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, PH 7.8, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       43.67550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.27400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.67550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       38.27400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       87.35100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A    89                                                      
REMARK 465     TYR A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     ILE A    92                                                      
REMARK 465     ARG A    93                                                      
REMARK 465     TYR A    94                                                      
REMARK 465     ALA A    95                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     LYS A  121                                                       
REMARK 475     LYS A  124                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     PRO A   67   C    O                                              
REMARK 480     GLU A   68   N                                                   
REMARK 480     SER A   71   CA   C    O    CB   OG                              
REMARK 480     SER A  125   N    CA   CB   OG                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   708     O    HOH A   719              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  18      -55.94     -2.99                                   
REMARK 500    GLU A  68      170.22    -52.41                                   
REMARK 500    GLU A  77      -70.11    -63.85                                   
REMARK 500    HIS A  97      -59.29    150.26                                   
REMARK 500    CYS A 114      167.79    176.14                                   
REMARK 500    LYS A 118       55.78    -70.00                                   
REMARK 500    GLU A 119      161.68     65.00                                   
REMARK 500    PRO A 120       72.01     -2.65                                   
REMARK 500    LYS A 121       32.86   -145.97                                   
REMARK 500    LYS A 124       45.49     38.23                                   
REMARK 500    SER A 125      162.62    -31.94                                   
REMARK 500    ALA A 126      -70.83    150.97                                   
REMARK 500    ALA A 248       80.00   -154.43                                   
REMARK 500    SER A 323     -161.58   -100.19                                   
REMARK 500    TYR A 411      138.01   -172.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 681   O                                                      
REMARK 620 2 HOH A 631   O    81.9                                              
REMARK 620 3 ACT A 601   O    78.4  71.5                                        
REMARK 620 4 HOH A 865   O    83.7 143.7  73.0                                  
REMARK 620 5 ACT A 601   OXT 123.5  75.3  45.5  85.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  59   OE2                                                    
REMARK 620 2 ASP A  61   OD2  85.4                                              
REMARK 620 3 ASP A 110   OD2 166.1  98.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 719   O                                                      
REMARK 620 2 GLU A 387   OE2  82.1                                              
REMARK 620 3 HOH A 607   O   179.4  97.4                                        
REMARK 620 4 GLU A 387   OE1  94.1  48.2  85.7                                  
REMARK 620 5 THR A 383   OG1  97.9  81.9  81.7 126.3                            
REMARK 620 6 HOH A 657   O    95.2 118.1  85.3  70.6 157.5                      
REMARK 620 7 HOH A 715   O    97.5 165.0  83.0 146.3  83.3  76.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 821   O                                                      
REMARK 620 2 ACT A 601   OXT  81.9                                              
REMARK 620 3 LYS A 166   O    73.6  82.2                                        
REMARK 620 4 HOH A 785   O    76.7 154.4 104.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UEU   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH CYTIDINE-5'-TRIPHOSPHATE                       
REMARK 900 RELATED ID: 1UEV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH ADENOSINE-5'-TRIPHOSPHATE                      
REMARK 900 RELATED ID: MY_001000010.1   RELATED DB: TARGETDB                    
DBREF  1UET A    1   437  UNP    O28126   CCA_ARCFU        1    437             
SEQRES   1 A  437  MET LYS VAL GLU GLU ILE LEU GLU LYS ALA LEU GLU LEU          
SEQRES   2 A  437  VAL ILE PRO ASP GLU GLU GLU VAL ARG LYS GLY ARG GLU          
SEQRES   3 A  437  ALA GLU GLU GLU LEU ARG ARG ARG LEU ASP GLU LEU GLY          
SEQRES   4 A  437  VAL GLU TYR VAL PHE VAL GLY SER TYR ALA ARG ASN THR          
SEQRES   5 A  437  TRP LEU LYS GLY SER LEU GLU ILE ASP VAL PHE LEU LEU          
SEQRES   6 A  437  PHE PRO GLU GLU PHE SER LYS GLU GLU LEU ARG GLU ARG          
SEQRES   7 A  437  GLY LEU GLU ILE GLY LYS ALA VAL LEU ASP SER TYR GLU          
SEQRES   8 A  437  ILE ARG TYR ALA GLU HIS PRO TYR VAL HIS GLY VAL VAL          
SEQRES   9 A  437  LYS GLY VAL GLU VAL ASP VAL VAL PRO CYS TYR LYS LEU          
SEQRES  10 A  437  LYS GLU PRO LYS ASN ILE LYS SER ALA VAL ASP ARG THR          
SEQRES  11 A  437  PRO PHE HIS HIS LYS TRP LEU GLU GLY ARG ILE LYS GLY          
SEQRES  12 A  437  LYS GLU ASN GLU VAL ARG LEU LEU LYS GLY PHE LEU LYS          
SEQRES  13 A  437  ALA ASN GLY ILE TYR GLY ALA GLU TYR LYS VAL ARG GLY          
SEQRES  14 A  437  PHE SER GLY TYR LEU CYS GLU LEU LEU ILE VAL PHE TYR          
SEQRES  15 A  437  GLY SER PHE LEU GLU THR VAL LYS ASN ALA ARG ARG TRP          
SEQRES  16 A  437  THR ARG ARG THR VAL ILE ASP VAL ALA LYS GLY GLU VAL          
SEQRES  17 A  437  ARG LYS GLY GLU GLU PHE PHE VAL VAL ASP PRO VAL ASP          
SEQRES  18 A  437  GLU LYS ARG ASN VAL ALA ALA ASN LEU SER LEU ASP ASN          
SEQRES  19 A  437  LEU ALA ARG PHE VAL HIS LEU CYS ARG GLU PHE MET GLU          
SEQRES  20 A  437  ALA PRO SER LEU GLY PHE PHE LYS PRO LYS HIS PRO LEU          
SEQRES  21 A  437  GLU ILE GLU PRO GLU ARG LEU ARG LYS ILE VAL GLU GLU          
SEQRES  22 A  437  ARG GLY THR ALA VAL PHE ALA VAL LYS PHE ARG LYS PRO          
SEQRES  23 A  437  ASP ILE VAL ASP ASP ASN LEU TYR PRO GLN LEU GLU ARG          
SEQRES  24 A  437  ALA SER ARG LYS ILE PHE GLU PHE LEU GLU ARG GLU ASN          
SEQRES  25 A  437  PHE MET PRO LEU ARG SER ALA PHE LYS ALA SER GLU GLU          
SEQRES  26 A  437  PHE CYS TYR LEU LEU PHE GLU CYS GLN ILE LYS GLU ILE          
SEQRES  27 A  437  SER ARG VAL PHE ARG ARG MET GLY PRO GLN PHE GLU ASP          
SEQRES  28 A  437  GLU ARG ASN VAL LYS LYS PHE LEU SER ARG ASN ARG ALA          
SEQRES  29 A  437  PHE ARG PRO PHE ILE GLU ASN GLY ARG TRP TRP ALA PHE          
SEQRES  30 A  437  GLU MET ARG LYS PHE THR THR PRO GLU GLU GLY VAL ARG          
SEQRES  31 A  437  SER TYR ALA SER THR HIS TRP HIS THR LEU GLY LYS ASN          
SEQRES  32 A  437  VAL GLY GLU SER ILE ARG GLU TYR PHE GLU ILE ILE SER          
SEQRES  33 A  437  GLY GLU LYS LEU PHE LYS GLU PRO VAL THR ALA GLU LEU          
SEQRES  34 A  437  CYS GLU MET MET GLY VAL LYS ASP                              
HET    ACT  A 601       4                                                       
HET     CA  A 501       1                                                       
HET     MG  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  ACT    C2 H3 O2 1-                                                  
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   4   MG    MG 2+                                                        
FORMUL   7  HOH   *304(H2 O)                                                    
HELIX    1   1 LYS A    2  ILE A   15  1                                  14    
HELIX    2   2 ASP A   17  LEU A   38  1                                  22    
HELIX    3   3 SER A   71  GLY A   83  1                                  13    
HELIX    4   4 ARG A  129  LYS A  142  1                                  14    
HELIX    5   5 LYS A  144  ASN A  158  1                                  15    
HELIX    6   6 SER A  171  GLY A  183  1                                  13    
HELIX    7   7 SER A  184  ARG A  193  1                                  10    
HELIX    8   8 ALA A  204  GLY A  206  5                                   3    
HELIX    9   9 SER A  231  ALA A  248  1                                  18    
HELIX   10  10 SER A  250  LYS A  255  5                                   6    
HELIX   11  11 GLU A  263  GLY A  275  1                                  13    
HELIX   12  12 VAL A  289  GLU A  311  1                                  23    
HELIX   13  13 ASP A  351  ARG A  361  1                                  11    
HELIX   14  14 THR A  384  HIS A  396  1                                  13    
HELIX   15  15 TRP A  397  LEU A  400  5                                   4    
HELIX   16  16 GLY A  401  TYR A  411  1                                  11    
HELIX   17  17 GLY A  417  GLU A  423  1                                   7    
HELIX   18  18 VAL A  425  GLY A  434  1                                  10    
SHEET    1   A 5 TYR A  42  PHE A  44  0                                        
SHEET    2   A 5 ILE A  60  LEU A  65 -1  O  PHE A  63   N  VAL A  43           
SHEET    3   A 5 VAL A 107  CYS A 114  1  O  VAL A 112   N  LEU A  64           
SHEET    4   A 5 VAL A 100  VAL A 104 -1  N  VAL A 100   O  VAL A 111           
SHEET    5   A 5 ALA A  85  LEU A  87 -1  N  LEU A  87   O  HIS A 101           
SHEET    1   B 3 GLU A 207  LYS A 210  0                                        
SHEET    2   B 3 THR A 199  ASP A 202 -1  N  VAL A 200   O  ARG A 209           
SHEET    3   B 3 PHE A 215  VAL A 217  1  O  PHE A 215   N  ILE A 201           
SHEET    1   C 4 PRO A 315  ALA A 322  0                                        
SHEET    2   C 4 PHE A 326  CYS A 333 -1  O  LEU A 330   N  ALA A 319           
SHEET    3   C 4 ALA A 277  ARG A 284 -1  N  PHE A 283   O  CYS A 327           
SHEET    4   C 4 GLU A 413  SER A 416 -1  O  GLU A 413   N  LYS A 282           
SHEET    1   D 3 VAL A 341  GLN A 348  0                                        
SHEET    2   D 3 ARG A 373  MET A 379 -1  O  ALA A 376   N  ARG A 344           
SHEET    3   D 3 PHE A 368  GLU A 370 -1  N  GLU A 370   O  ARG A 373           
LINK        CA    CA A 501                 O   HOH A 681     1555   1555  2.80  
LINK        CA    CA A 501                 O   HOH A 631     1555   1555  2.62  
LINK        CA    CA A 501                 O   ACT A 601     1555   1555  3.00  
LINK        CA    CA A 501                 O   HOH A 865     1555   1555  3.03  
LINK        CA    CA A 501                 OXT ACT A 601     1555   1555  2.64  
LINK        MG    MG A 502                 OE2 GLU A  59     1555   1555  2.25  
LINK        MG    MG A 502                 OD2 ASP A  61     1555   1555  2.59  
LINK        MG    MG A 502                 OD2 ASP A 110     1555   1555  2.37  
LINK        CA    CA A 503                 O   HOH A 719     1555   1555  2.61  
LINK        CA    CA A 503                 OE2 GLU A 387     1555   1555  2.66  
LINK        CA    CA A 503                 O   HOH A 607     1555   1555  2.69  
LINK        CA    CA A 503                 OE1 GLU A 387     1555   1555  2.76  
LINK        CA    CA A 503                 OG1 THR A 383     1555   1555  2.65  
LINK        CA    CA A 504                 O   HOH A 821     1555   1555  2.79  
LINK        CA    CA A 504                 OXT ACT A 601     1555   1555  2.64  
LINK        CA    CA A 504                 O   LYS A 166     1555   1555  2.56  
LINK        CA    CA A 504                 O   HOH A 785     1555   1555  2.67  
LINK        CA    CA A 503                 O   HOH A 657     1555   3545  2.73  
LINK        CA    CA A 503                 O   HOH A 715     1555   3545  2.57  
SITE     1 AC1  7 LYS A 166  VAL A 167  ARG A 168  ASN A 234                    
SITE     2 AC1  7  CA A 501   CA A 504  HOH A 831                               
SITE     1 AC2  4 ACT A 601  HOH A 631  HOH A 681  HOH A 865                    
SITE     1 AC3  3 GLU A  59  ASP A  61  ASP A 110                               
SITE     1 AC4  6 THR A 383  GLU A 387  HOH A 607  HOH A 657                    
SITE     2 AC4  6 HOH A 715  HOH A 719                                          
SITE     1 AC5  4 LYS A 166  ACT A 601  HOH A 785  HOH A 821                    
CRYST1   87.351   76.548   76.771  90.00  98.33  90.00 C 1 2 1       4          
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      0.011448  0.000000  0.001676        0.00000                         
SCALE2      0.000000  0.013064  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013165        0.00000                         
ATOM      1  N   LYS A   2      -6.534  19.993   8.603  1.00 68.19           N  
ATOM      2  CA  LYS A   2      -5.940  18.838   9.332  1.00 71.71           C  
ATOM      3  C   LYS A   2      -5.046  19.320  10.471  1.00 72.23           C  
ATOM      4  O   LYS A   2      -5.104  18.796  11.585  1.00 71.66           O  
ATOM      5  CB  LYS A   2      -5.114  17.980   8.372  1.00 72.15           C  
ATOM      6  CG  LYS A   2      -4.039  18.761   7.629  1.00 75.84           C  
ATOM      7  CD  LYS A   2      -3.118  17.850   6.829  1.00 78.73           C  
ATOM      8  CE  LYS A   2      -2.147  18.669   5.983  1.00 81.91           C  
ATOM      9  NZ  LYS A   2      -1.114  17.829   5.305  1.00 82.69           N  
ATOM     10  N   VAL A   3      -4.225  20.324  10.176  1.00 70.89           N  
ATOM     11  CA  VAL A   3      -3.293  20.892  11.142  1.00 68.68           C  
ATOM     12  C   VAL A   3      -3.910  21.093  12.518  1.00 68.45           C  
ATOM     13  O   VAL A   3      -3.416  20.571  13.521  1.00 66.50           O  
ATOM     14  CB  VAL A   3      -2.756  22.251  10.652  1.00 68.06           C  
ATOM     15  CG1 VAL A   3      -1.749  22.805  11.645  1.00 67.82           C  
ATOM     16  CG2 VAL A   3      -2.125  22.091   9.285  1.00 71.53           C  
ATOM     17  N   GLU A   4      -4.994  21.855  12.558  1.00 67.97           N  
ATOM     18  CA  GLU A   4      -5.675  22.146  13.807  1.00 65.33           C  
ATOM     19  C   GLU A   4      -6.063  20.865  14.543  1.00 63.73           C  
ATOM     20  O   GLU A   4      -6.046  20.821  15.774  1.00 62.87           O  
ATOM     21  CB  GLU A   4      -6.909  23.009  13.527  1.00 70.83           C  
ATOM     22  CG  GLU A   4      -6.672  24.123  12.492  1.00 74.07           C  
ATOM     23  CD  GLU A   4      -5.538  25.076  12.866  1.00 74.35           C  
ATOM     24  OE1 GLU A   4      -4.380  24.621  12.989  1.00 75.49           O  
ATOM     25  OE2 GLU A   4      -5.804  26.287  13.032  1.00 77.59           O  
ATOM     26  N   GLU A   5      -6.406  19.820  13.797  1.00 60.43           N  
ATOM     27  CA  GLU A   5      -6.776  18.555  14.427  1.00 60.70           C  
ATOM     28  C   GLU A   5      -5.540  17.846  14.975  1.00 58.01           C  
ATOM     29  O   GLU A   5      -5.589  17.225  16.036  1.00 55.34           O  
ATOM     30  CB  GLU A   5      -7.508  17.644  13.433  1.00 65.13           C  
ATOM     31  CG  GLU A   5      -8.953  18.058  13.155  1.00 68.24           C  
ATOM     32  CD  GLU A   5      -9.845  17.954  14.389  1.00 73.86           C  
ATOM     33  OE1 GLU A   5     -10.064  16.821  14.877  1.00 71.49           O  
ATOM     34  OE2 GLU A   5     -10.323  19.006  14.874  1.00 73.44           O  
ATOM     35  N   ILE A   6      -4.429  17.948  14.256  1.00 51.82           N  
ATOM     36  CA  ILE A   6      -3.194  17.318  14.697  1.00 49.80           C  
ATOM     37  C   ILE A   6      -2.718  17.909  16.022  1.00 46.10           C  
ATOM     38  O   ILE A   6      -2.262  17.184  16.905  1.00 44.53           O  
ATOM     39  CB  ILE A   6      -2.098  17.468  13.629  1.00 54.14           C  
ATOM     40  CG1 ILE A   6      -2.485  16.639  12.402  1.00 53.22           C  
ATOM     41  CG2 ILE A   6      -0.742  17.027  14.187  1.00 54.02           C  
ATOM     42  CD1 ILE A   6      -1.567  16.813  11.229  1.00 57.42           C  
ATOM     43  N   LEU A   7      -2.838  19.224  16.168  1.00 41.93           N  
ATOM     44  CA  LEU A   7      -2.414  19.882  17.400  1.00 47.05           C  
ATOM     45  C   LEU A   7      -3.248  19.418  18.595  1.00 48.11           C  
ATOM     46  O   LEU A   7      -2.768  19.383  19.727  1.00 46.26           O  
ATOM     47  CB  LEU A   7      -2.509  21.403  17.236  1.00 46.75           C  
ATOM     48  CG  LEU A   7      -1.306  22.122  16.604  1.00 53.51           C  
ATOM     49  CD1 LEU A   7      -0.706  21.299  15.472  1.00 55.33           C  
ATOM     50  CD2 LEU A   7      -1.744  23.496  16.111  1.00 47.94           C  
ATOM     51  N   GLU A   8      -4.501  19.056  18.334  1.00 50.37           N  
ATOM     52  CA  GLU A   8      -5.400  18.585  19.379  1.00 46.13           C  
ATOM     53  C   GLU A   8      -4.899  17.243  19.913  1.00 41.16           C  
ATOM     54  O   GLU A   8      -4.902  16.996  21.118  1.00 38.93           O  
ATOM     55  CB  GLU A   8      -6.816  18.449  18.810  1.00 56.10           C  
ATOM     56  CG  GLU A   8      -7.915  18.200  19.842  1.00 61.25           C  
ATOM     57  CD  GLU A   8      -9.308  18.252  19.221  1.00 66.93           C  
ATOM     58  OE1 GLU A   8      -9.586  17.442  18.312  1.00 70.50           O  
ATOM     59  OE2 GLU A   8     -10.122  19.106  19.635  1.00 66.23           O  
ATOM     60  N   LYS A   9      -4.457  16.378  19.011  1.00 43.95           N  
ATOM     61  CA  LYS A   9      -3.944  15.076  19.412  1.00 44.94           C  
ATOM     62  C   LYS A   9      -2.576  15.230  20.078  1.00 48.47           C  
ATOM     63  O   LYS A   9      -2.230  14.482  20.998  1.00 48.70           O  
ATOM     64  CB  LYS A   9      -3.841  14.152  18.197  1.00 45.65           C  
ATOM     65  CG  LYS A   9      -5.187  13.839  17.563  1.00 54.41           C  
ATOM     66  CD  LYS A   9      -5.085  12.736  16.522  1.00 59.42           C  
ATOM     67  CE  LYS A   9      -6.466  12.286  16.069  1.00 61.45           C  
ATOM     68  NZ  LYS A   9      -6.410  11.033  15.263  1.00 68.42           N  
ATOM     69  N   ALA A  10      -1.803  16.207  19.614  1.00 42.82           N  
ATOM     70  CA  ALA A  10      -0.486  16.462  20.179  1.00 42.85           C  
ATOM     71  C   ALA A  10      -0.622  16.878  21.642  1.00 40.73           C  
ATOM     72  O   ALA A  10       0.261  16.615  22.458  1.00 41.08           O  
ATOM     73  CB  ALA A  10       0.222  17.560  19.384  1.00 43.96           C  
ATOM     74  N   LEU A  11      -1.735  17.521  21.979  1.00 42.75           N  
ATOM     75  CA  LEU A  11      -1.953  17.959  23.354  1.00 42.33           C  
ATOM     76  C   LEU A  11      -1.930  16.792  24.339  1.00 41.00           C  
ATOM     77  O   LEU A  11      -1.523  16.955  25.481  1.00 36.24           O  
ATOM     78  CB  LEU A  11      -3.283  18.698  23.477  1.00 43.71           C  
ATOM     79  CG  LEU A  11      -3.416  20.018  22.719  1.00 44.12           C  
ATOM     80  CD1 LEU A  11      -4.803  20.585  22.980  1.00 40.88           C  
ATOM     81  CD2 LEU A  11      -2.346  21.008  23.165  1.00 40.37           C  
ATOM     82  N   GLU A  12      -2.361  15.618  23.886  1.00 46.10           N  
ATOM     83  CA  GLU A  12      -2.391  14.428  24.736  1.00 50.38           C  
ATOM     84  C   GLU A  12      -0.997  13.884  25.012  1.00 48.56           C  
ATOM     85  O   GLU A  12      -0.811  13.055  25.906  1.00 47.88           O  
ATOM     86  CB  GLU A  12      -3.227  13.329  24.081  1.00 55.22           C  
ATOM     87  CG  GLU A  12      -4.729  13.539  24.135  1.00 59.09           C  
ATOM     88  CD  GLU A  12      -5.468  12.536  23.267  1.00 65.39           C  
ATOM     89  OE1 GLU A  12      -5.086  11.346  23.281  1.00 66.37           O  
ATOM     90  OE2 GLU A  12      -6.430  12.933  22.573  1.00 66.11           O  
ATOM     91  N   LEU A  13      -0.017  14.346  24.242  1.00 46.84           N  
ATOM     92  CA  LEU A  13       1.357  13.886  24.419  1.00 46.21           C  
ATOM     93  C   LEU A  13       2.197  14.853  25.232  1.00 44.97           C  
ATOM     94  O   LEU A  13       3.145  14.443  25.900  1.00 47.82           O  
ATOM     95  CB  LEU A  13       2.028  13.668  23.059  1.00 48.47           C  
ATOM     96  CG  LEU A  13       1.391  12.637  22.122  1.00 48.98           C  
ATOM     97  CD1 LEU A  13       2.119  12.659  20.786  1.00 52.26           C  
ATOM     98  CD2 LEU A  13       1.449  11.247  22.747  1.00 46.59           C  
ATOM     99  N   VAL A  14       1.837  16.133  25.184  1.00 46.19           N  
ATOM    100  CA  VAL A  14       2.584  17.173  25.884  1.00 41.74           C  
ATOM    101  C   VAL A  14       2.031  17.610  27.240  1.00 44.42           C  
ATOM    102  O   VAL A  14       2.784  18.092  28.085  1.00 47.86           O  
ATOM    103  CB  VAL A  14       2.729  18.424  24.990  1.00 39.98           C  
ATOM    104  CG1 VAL A  14       3.455  18.056  23.712  1.00 41.61           C  
ATOM    105  CG2 VAL A  14       1.360  19.007  24.667  1.00 39.90           C  
ATOM    106  N   ILE A  15       0.730  17.453  27.454  1.00 45.53           N  
ATOM    107  CA  ILE A  15       0.125  17.853  28.725  1.00 49.23           C  
ATOM    108  C   ILE A  15       0.250  16.743  29.767  1.00 47.06           C  
ATOM    109  O   ILE A  15      -0.137  15.605  29.520  1.00 48.72           O  
ATOM    110  CB  ILE A  15      -1.376  18.214  28.552  1.00 47.78           C  
ATOM    111  CG1 ILE A  15      -1.521  19.380  27.574  1.00 52.27           C  
ATOM    112  CG2 ILE A  15      -1.983  18.602  29.892  1.00 50.85           C  
ATOM    113  CD1 ILE A  15      -2.952  19.834  27.354  1.00 55.31           C  
ATOM    114  N   PRO A  16       0.802  17.065  30.949  1.00 51.29           N  
ATOM    115  CA  PRO A  16       0.978  16.090  32.035  1.00 54.94           C  
ATOM    116  C   PRO A  16      -0.350  15.443  32.436  1.00 56.14           C  
ATOM    117  O   PRO A  16      -1.394  16.091  32.396  1.00 51.30           O  
ATOM    118  CB  PRO A  16       1.559  16.936  33.165  1.00 54.92           C  
ATOM    119  CG  PRO A  16       2.296  18.011  32.438  1.00 54.54           C  
ATOM    120  CD  PRO A  16       1.332  18.381  31.345  1.00 49.00           C  
ATOM    121  N   ASP A  17      -0.313  14.173  32.825  1.00 63.43           N  
ATOM    122  CA  ASP A  17      -1.540  13.497  33.220  1.00 68.47           C  
ATOM    123  C   ASP A  17      -1.786  13.533  34.723  1.00 71.20           C  
ATOM    124  O   ASP A  17      -0.913  13.198  35.522  1.00 71.78           O  
ATOM    125  CB  ASP A  17      -1.556  12.041  32.718  1.00 69.33           C  
ATOM    126  CG  ASP A  17      -0.423  11.199  33.288  1.00 72.42           C  
ATOM    127  OD1 ASP A  17      -0.325  11.084  34.528  1.00 71.47           O  
ATOM    128  OD2 ASP A  17       0.364  10.638  32.492  1.00 73.16           O  
ATOM    129  N   GLU A  18      -2.986  13.984  35.075  1.00 74.21           N  
ATOM    130  CA  GLU A  18      -3.494  14.085  36.446  1.00 74.26           C  
ATOM    131  C   GLU A  18      -2.588  13.566  37.564  1.00 71.80           C  
ATOM    132  O   GLU A  18      -2.272  14.295  38.502  1.00 70.44           O  
ATOM    133  CB  GLU A  18      -4.834  13.355  36.493  1.00 73.88           C  
ATOM    134  CG  GLU A  18      -5.146  12.691  35.157  1.00 75.71           C  
ATOM    135  CD  GLU A  18      -6.261  11.683  35.227  1.00 77.53           C  
ATOM    136  OE1 GLU A  18      -6.290  10.887  36.189  1.00 81.87           O  
ATOM    137  OE2 GLU A  18      -7.096  11.672  34.303  1.00 79.54           O  
ATOM    138  N   GLU A  19      -2.185  12.303  37.457  1.00 73.38           N  
ATOM    139  CA  GLU A  19      -1.336  11.656  38.453  1.00 75.77           C  
ATOM    140  C   GLU A  19       0.041  12.277  38.684  1.00 76.17           C  
ATOM    141  O   GLU A  19       0.628  12.096  39.750  1.00 74.08           O  
ATOM    142  CB  GLU A  19      -1.176  10.178  38.105  1.00 78.03           C  
ATOM    143  CG  GLU A  19      -2.495   9.435  38.063  1.00 82.50           C  
ATOM    144  CD  GLU A  19      -2.337   8.006  37.607  1.00 85.63           C  
ATOM    145  OE1 GLU A  19      -1.794   7.800  36.502  1.00 87.66           O  
ATOM    146  OE2 GLU A  19      -2.756   7.091  38.349  1.00 86.60           O  
ATOM    147  N   GLU A  20       0.580  12.984  37.695  1.00 76.54           N  
ATOM    148  CA  GLU A  20       1.877  13.615  37.897  1.00 76.13           C  
ATOM    149  C   GLU A  20       1.594  15.055  38.310  1.00 73.58           C  
ATOM    150  O   GLU A  20       2.371  15.675  39.031  1.00 70.03           O  
ATOM    151  CB  GLU A  20       2.736  13.557  36.627  1.00 75.84           C  
ATOM    152  CG  GLU A  20       2.559  14.712  35.664  1.00 80.41           C  
ATOM    153  CD  GLU A  20       3.672  14.766  34.629  1.00 81.03           C  
ATOM    154  OE1 GLU A  20       3.758  13.840  33.794  1.00 79.89           O  
ATOM    155  OE2 GLU A  20       4.466  15.732  34.659  1.00 76.67           O  
ATOM    156  N   VAL A  21       0.459  15.575  37.857  1.00 73.78           N  
ATOM    157  CA  VAL A  21       0.049  16.925  38.209  1.00 75.70           C  
ATOM    158  C   VAL A  21      -0.338  16.885  39.687  1.00 79.43           C  
ATOM    159  O   VAL A  21      -0.359  17.911  40.369  1.00 78.95           O  
ATOM    160  CB  VAL A  21      -1.179  17.377  37.389  1.00 76.72           C  
ATOM    161  CG1 VAL A  21      -1.533  18.815  37.735  1.00 75.23           C  
ATOM    162  CG2 VAL A  21      -0.900  17.235  35.900  1.00 76.63           C  
ATOM    163  N   ARG A  22      -0.643  15.682  40.171  1.00 81.16           N  
ATOM    164  CA  ARG A  22      -1.025  15.481  41.565  1.00 81.42           C  
ATOM    165  C   ARG A  22       0.230  15.507  42.418  1.00 77.71           C  
ATOM    166  O   ARG A  22       0.257  16.108  43.483  1.00 78.06           O  
ATOM    167  CB  ARG A  22      -1.721  14.125  41.755  1.00 83.86           C  
ATOM    168  CG  ARG A  22      -0.750  12.964  41.959  1.00 86.88           C  
ATOM    169  CD  ARG A  22      -1.428  11.607  41.989  1.00 87.21           C  
ATOM    170  NE  ARG A  22      -0.457  10.521  41.872  1.00 87.42           N  
ATOM    171  CZ  ARG A  22      -0.777   9.241  41.707  1.00 88.21           C  
ATOM    172  NH1 ARG A  22      -2.050   8.873  41.639  1.00 88.66           N  
ATOM    173  NH2 ARG A  22       0.180   8.329  41.600  1.00 88.44           N  
ATOM    174  N   LYS A  23       1.273  14.839  41.946  1.00 76.68           N  
ATOM    175  CA  LYS A  23       2.517  14.798  42.690  1.00 75.48           C  
ATOM    176  C   LYS A  23       3.040  16.217  42.875  1.00 74.83           C  
ATOM    177  O   LYS A  23       3.496  16.588  43.951  1.00 75.02           O  
ATOM    178  CB  LYS A  23       3.534  13.929  41.951  1.00 76.28           C  
ATOM    179  CG  LYS A  23       3.074  12.486  41.798  1.00 76.97           C  
ATOM    180  CD  LYS A  23       4.142  11.591  41.190  1.00 82.29           C  
ATOM    181  CE  LYS A  23       3.649  10.146  41.086  1.00 83.88           C  
ATOM    182  NZ  LYS A  23       4.681   9.233  40.514  1.00 83.09           N  
ATOM    183  N   GLY A  24       2.944  17.018  41.822  1.00 71.58           N  
ATOM    184  CA  GLY A  24       3.410  18.386  41.902  1.00 71.04           C  
ATOM    185  C   GLY A  24       2.682  19.164  42.979  1.00 72.23           C  
ATOM    186  O   GLY A  24       3.303  19.806  43.822  1.00 68.84           O  
ATOM    187  N   ARG A  25       1.356  19.119  42.945  1.00 73.91           N  
ATOM    188  CA  ARG A  25       0.547  19.828  43.930  1.00 75.45           C  
ATOM    189  C   ARG A  25       0.909  19.397  45.346  1.00 73.35           C  
ATOM    190  O   ARG A  25       1.162  20.234  46.214  1.00 71.28           O  
ATOM    191  CB  ARG A  25      -0.945  19.572  43.680  1.00 79.87           C  
ATOM    192  CG  ARG A  25      -1.369  18.122  43.876  1.00 83.08           C  
ATOM    193  CD  ARG A  25      -2.776  17.850  43.365  1.00 86.32           C  
ATOM    194  NE  ARG A  25      -3.097  16.429  43.454  1.00 86.73           N  
ATOM    195  CZ  ARG A  25      -4.211  15.877  42.988  1.00 88.11           C  
ATOM    196  NH1 ARG A  25      -5.130  16.624  42.393  1.00 89.05           N  
ATOM    197  NH2 ARG A  25      -4.401  14.572  43.114  1.00 92.41           N  
ATOM    198  N   GLU A  26       0.933  18.087  45.575  1.00 70.74           N  
ATOM    199  CA  GLU A  26       1.255  17.546  46.891  1.00 70.63           C  
ATOM    200  C   GLU A  26       2.578  18.115  47.387  1.00 70.13           C  
ATOM    201  O   GLU A  26       2.659  18.657  48.489  1.00 71.93           O  
ATOM    202  CB  GLU A  26       1.361  16.014  46.843  1.00 72.94           C  
ATOM    203  CG  GLU A  26       0.109  15.272  46.379  1.00 74.79           C  
ATOM    204  CD  GLU A  26      -1.063  15.389  47.339  1.00 76.25           C  
ATOM    205  OE1 GLU A  26      -0.917  16.037  48.395  1.00 78.81           O  
ATOM    206  OE2 GLU A  26      -2.137  14.826  47.035  1.00 76.89           O  
ATOM    207  N   ALA A  27       3.609  17.989  46.556  1.00 67.17           N  
ATOM    208  CA  ALA A  27       4.949  18.458  46.893  1.00 64.86           C  
ATOM    209  C   ALA A  27       5.040  19.955  47.126  1.00 61.20           C  
ATOM    210  O   ALA A  27       5.776  20.405  48.002  1.00 58.02           O  
ATOM    211  CB  ALA A  27       5.931  18.052  45.803  1.00 66.27           C  
ATOM    212  N   GLU A  28       4.300  20.727  46.339  1.00 59.94           N  
ATOM    213  CA  GLU A  28       4.319  22.173  46.480  1.00 59.52           C  
ATOM    214  C   GLU A  28       3.785  22.609  47.841  1.00 59.37           C  
ATOM    215  O   GLU A  28       4.446  23.349  48.566  1.00 53.46           O  
ATOM    216  CB  GLU A  28       3.490  22.827  45.376  1.00 60.13           C  
ATOM    217  CG  GLU A  28       3.431  24.335  45.505  1.00 56.08           C  
ATOM    218  CD  GLU A  28       2.498  24.975  44.506  1.00 57.11           C  
ATOM    219  OE1 GLU A  28       2.333  26.209  44.564  1.00 59.54           O  
ATOM    220  OE2 GLU A  28       1.932  24.250  43.665  1.00 58.04           O  
ATOM    221  N   GLU A  29       2.582  22.160  48.183  1.00 60.61           N  
ATOM    222  CA  GLU A  29       1.990  22.521  49.468  1.00 61.83           C  
ATOM    223  C   GLU A  29       2.955  22.170  50.593  1.00 60.36           C  
ATOM    224  O   GLU A  29       3.286  23.013  51.429  1.00 59.62           O  
ATOM    225  CB  GLU A  29       0.660  21.784  49.677  1.00 64.17           C  
ATOM    226  CG  GLU A  29      -0.502  22.332  48.853  1.00 69.46           C  
ATOM    227  CD  GLU A  29      -1.791  21.552  49.063  1.00 73.29           C  
ATOM    228  OE1 GLU A  29      -1.858  20.381  48.626  1.00 70.68           O  
ATOM    229  OE2 GLU A  29      -2.734  22.106  49.672  1.00 75.37           O  
ATOM    230  N   GLU A  30       3.421  20.925  50.589  1.00 55.45           N  
ATOM    231  CA  GLU A  30       4.339  20.438  51.611  1.00 52.97           C  
ATOM    232  C   GLU A  30       5.613  21.273  51.706  1.00 53.35           C  
ATOM    233  O   GLU A  30       6.067  21.602  52.803  1.00 55.87           O  
ATOM    234  CB  GLU A  30       4.686  18.973  51.331  1.00 55.04           C  
ATOM    235  CG  GLU A  30       5.490  18.276  52.416  1.00 54.91           C  
ATOM    236  CD  GLU A  30       4.812  18.300  53.772  1.00 59.76           C  
ATOM    237  OE1 GLU A  30       3.579  18.080  53.832  1.00 61.49           O  
ATOM    238  OE2 GLU A  30       5.521  18.528  54.778  1.00 53.44           O  
ATOM    239  N   LEU A  31       6.186  21.618  50.559  1.00 49.59           N  
ATOM    240  CA  LEU A  31       7.407  22.411  50.531  1.00 48.60           C  
ATOM    241  C   LEU A  31       7.151  23.814  51.075  1.00 51.24           C  
ATOM    242  O   LEU A  31       8.000  24.389  51.759  1.00 52.29           O  
ATOM    243  CB  LEU A  31       7.954  22.473  49.098  1.00 48.65           C  
ATOM    244  CG  LEU A  31       9.238  23.241  48.753  1.00 48.64           C  
ATOM    245  CD1 LEU A  31      10.385  22.865  49.676  1.00 46.92           C  
ATOM    246  CD2 LEU A  31       9.602  22.929  47.310  1.00 47.73           C  
ATOM    247  N   ARG A  32       5.980  24.366  50.778  1.00 50.73           N  
ATOM    248  CA  ARG A  32       5.642  25.702  51.264  1.00 51.76           C  
ATOM    249  C   ARG A  32       5.517  25.676  52.785  1.00 50.07           C  
ATOM    250  O   ARG A  32       6.003  26.573  53.477  1.00 49.28           O  
ATOM    251  CB  ARG A  32       4.322  26.180  50.654  1.00 48.96           C  
ATOM    252  CG  ARG A  32       4.393  26.509  49.181  1.00 58.13           C  
ATOM    253  CD  ARG A  32       3.011  26.825  48.631  1.00 59.78           C  
ATOM    254  NE  ARG A  32       3.052  27.131  47.204  1.00 60.34           N  
ATOM    255  CZ  ARG A  32       3.671  28.185  46.686  1.00 58.68           C  
ATOM    256  NH1 ARG A  32       4.301  29.040  47.482  1.00 58.57           N  
ATOM    257  NH2 ARG A  32       3.664  28.381  45.373  1.00 59.08           N  
ATOM    258  N   ARG A  33       4.865  24.637  53.297  1.00 53.33           N  
ATOM    259  CA  ARG A  33       4.670  24.488  54.735  1.00 56.13           C  
ATOM    260  C   ARG A  33       6.008  24.528  55.460  1.00 55.38           C  
ATOM    261  O   ARG A  33       6.191  25.286  56.409  1.00 58.22           O  
ATOM    262  CB  ARG A  33       3.957  23.171  55.038  1.00 54.25           C  
ATOM    263  CG  ARG A  33       3.578  22.999  56.500  1.00 65.76           C  
ATOM    264  CD  ARG A  33       2.798  21.714  56.739  1.00 66.67           C  
ATOM    265  NE  ARG A  33       2.304  21.627  58.114  1.00 76.83           N  
ATOM    266  CZ  ARG A  33       1.603  20.605  58.600  1.00 75.99           C  
ATOM    267  NH1 ARG A  33       1.306  19.569  57.825  1.00 75.50           N  
ATOM    268  NH2 ARG A  33       1.195  20.619  59.862  1.00 77.60           N  
ATOM    269  N   ARG A  34       6.948  23.718  54.992  1.00 54.50           N  
ATOM    270  CA  ARG A  34       8.270  23.644  55.595  1.00 51.88           C  
ATOM    271  C   ARG A  34       9.015  24.965  55.486  1.00 51.22           C  
ATOM    272  O   ARG A  34       9.663  25.410  56.437  1.00 48.56           O  
ATOM    273  CB  ARG A  34       9.074  22.519  54.934  1.00 51.07           C  
ATOM    274  CG  ARG A  34       8.365  21.168  54.988  1.00 48.22           C  
ATOM    275  CD  ARG A  34       9.183  20.063  54.338  1.00 56.35           C  
ATOM    276  NE  ARG A  34       8.477  18.782  54.382  1.00 49.08           N  
ATOM    277  CZ  ARG A  34       8.954  17.645  53.882  1.00 51.07           C  
ATOM    278  NH1 ARG A  34      10.144  17.620  53.290  1.00 45.68           N  
ATOM    279  NH2 ARG A  34       8.243  16.526  53.986  1.00 51.70           N  
ATOM    280  N   LEU A  35       8.923  25.599  54.324  1.00 50.19           N  
ATOM    281  CA  LEU A  35       9.593  26.878  54.123  1.00 46.45           C  
ATOM    282  C   LEU A  35       8.958  27.941  55.015  1.00 40.37           C  
ATOM    283  O   LEU A  35       9.658  28.706  55.670  1.00 41.45           O  
ATOM    284  CB  LEU A  35       9.505  27.297  52.651  1.00 45.19           C  
ATOM    285  CG  LEU A  35      10.407  26.537  51.677  1.00 35.80           C  
ATOM    286  CD1 LEU A  35      10.046  26.894  50.242  1.00 33.83           C  
ATOM    287  CD2 LEU A  35      11.857  26.877  51.970  1.00 37.86           C  
ATOM    288  N   ASP A  36       7.632  27.978  55.049  1.00 43.50           N  
ATOM    289  CA  ASP A  36       6.942  28.965  55.868  1.00 47.58           C  
ATOM    290  C   ASP A  36       7.357  28.864  57.336  1.00 48.74           C  
ATOM    291  O   ASP A  36       7.742  29.866  57.944  1.00 41.59           O  
ATOM    292  CB  ASP A  36       5.425  28.815  55.725  1.00 49.07           C  
ATOM    293  CG  ASP A  36       4.920  29.260  54.352  1.00 53.97           C  
ATOM    294  OD1 ASP A  36       5.602  30.093  53.717  1.00 45.27           O  
ATOM    295  OD2 ASP A  36       3.841  28.793  53.915  1.00 47.83           O  
ATOM    296  N   GLU A  37       7.303  27.655  57.893  1.00 48.12           N  
ATOM    297  CA  GLU A  37       7.684  27.438  59.290  1.00 49.60           C  
ATOM    298  C   GLU A  37       9.040  28.046  59.646  1.00 46.70           C  
ATOM    299  O   GLU A  37       9.236  28.510  60.764  1.00 46.58           O  
ATOM    300  CB  GLU A  37       7.693  25.940  59.619  1.00 57.27           C  
ATOM    301  CG  GLU A  37       6.304  25.329  59.746  1.00 61.75           C  
ATOM    302  CD  GLU A  37       6.335  23.853  60.116  1.00 69.20           C  
ATOM    303  OE1 GLU A  37       5.245  23.253  60.267  1.00 71.36           O  
ATOM    304  OE2 GLU A  37       7.446  23.294  60.255  1.00 70.70           O  
ATOM    305  N   LEU A  38       9.970  28.044  58.699  1.00 43.31           N  
ATOM    306  CA  LEU A  38      11.296  28.608  58.928  1.00 44.20           C  
ATOM    307  C   LEU A  38      11.295  30.111  58.661  1.00 44.37           C  
ATOM    308  O   LEU A  38      12.330  30.773  58.777  1.00 40.15           O  
ATOM    309  CB  LEU A  38      12.326  27.944  58.009  1.00 41.23           C  
ATOM    310  CG  LEU A  38      12.823  26.520  58.289  1.00 54.66           C  
ATOM    311  CD1 LEU A  38      11.660  25.567  58.522  1.00 51.46           C  
ATOM    312  CD2 LEU A  38      13.655  26.058  57.106  1.00 46.55           C  
ATOM    313  N   GLY A  39      10.131  30.645  58.299  1.00 44.11           N  
ATOM    314  CA  GLY A  39      10.034  32.063  58.001  1.00 45.68           C  
ATOM    315  C   GLY A  39      10.950  32.438  56.846  1.00 45.87           C  
ATOM    316  O   GLY A  39      11.591  33.488  56.859  1.00 47.93           O  
ATOM    317  N   VAL A  40      11.018  31.574  55.841  1.00 44.77           N  
ATOM    318  CA  VAL A  40      11.870  31.821  54.681  1.00 47.09           C  
ATOM    319  C   VAL A  40      11.174  32.603  53.562  1.00 45.69           C  
ATOM    320  O   VAL A  40      10.007  32.369  53.260  1.00 48.26           O  
ATOM    321  CB  VAL A  40      12.401  30.485  54.106  1.00 48.06           C  
ATOM    322  CG1 VAL A  40      13.139  30.725  52.808  1.00 48.37           C  
ATOM    323  CG2 VAL A  40      13.329  29.824  55.116  1.00 51.38           C  
ATOM    324  N   GLU A  41      11.908  33.537  52.965  1.00 47.91           N  
ATOM    325  CA  GLU A  41      11.417  34.361  51.860  1.00 51.01           C  
ATOM    326  C   GLU A  41      11.750  33.591  50.576  1.00 46.62           C  
ATOM    327  O   GLU A  41      12.920  33.367  50.278  1.00 49.29           O  
ATOM    328  CB  GLU A  41      12.150  35.709  51.862  1.00 56.33           C  
ATOM    329  CG  GLU A  41      12.120  36.432  53.211  1.00 68.14           C  
ATOM    330  CD  GLU A  41      13.086  37.609  53.282  1.00 71.25           C  
ATOM    331  OE1 GLU A  41      12.990  38.518  52.426  1.00 67.97           O  
ATOM    332  OE2 GLU A  41      13.939  37.625  54.200  1.00 75.48           O  
ATOM    333  N   TYR A  42      10.738  33.195  49.811  1.00 47.45           N  
ATOM    334  CA  TYR A  42      10.997  32.413  48.600  1.00 48.12           C  
ATOM    335  C   TYR A  42       9.970  32.594  47.492  1.00 48.07           C  
ATOM    336  O   TYR A  42       8.898  33.164  47.700  1.00 43.58           O  
ATOM    337  CB  TYR A  42      11.044  30.931  48.964  1.00 41.45           C  
ATOM    338  CG  TYR A  42       9.730  30.431  49.517  1.00 43.41           C  
ATOM    339  CD1 TYR A  42       8.734  29.946  48.675  1.00 37.74           C  
ATOM    340  CD2 TYR A  42       9.465  30.483  50.884  1.00 40.80           C  
ATOM    341  CE1 TYR A  42       7.511  29.522  49.177  1.00 42.49           C  
ATOM    342  CE2 TYR A  42       8.239  30.065  51.397  1.00 39.38           C  
ATOM    343  CZ  TYR A  42       7.270  29.586  50.542  1.00 41.38           C  
ATOM    344  OH  TYR A  42       6.064  29.156  51.050  1.00 44.06           O  
ATOM    345  N   VAL A  43      10.305  32.073  46.315  1.00 44.28           N  
ATOM    346  CA  VAL A  43       9.412  32.143  45.168  1.00 39.11           C  
ATOM    347  C   VAL A  43       9.650  30.963  44.227  1.00 36.44           C  
ATOM    348  O   VAL A  43      10.796  30.614  43.945  1.00 36.07           O  
ATOM    349  CB  VAL A  43       9.595  33.486  44.403  1.00 38.38           C  
ATOM    350  CG1 VAL A  43      11.046  33.683  44.004  1.00 43.99           C  
ATOM    351  CG2 VAL A  43       8.692  33.516  43.188  1.00 44.71           C  
ATOM    352  N   PHE A  44       8.567  30.323  43.786  1.00 31.25           N  
ATOM    353  CA  PHE A  44       8.676  29.206  42.851  1.00 32.65           C  
ATOM    354  C   PHE A  44       8.872  29.877  41.500  1.00 34.12           C  
ATOM    355  O   PHE A  44       8.085  30.744  41.117  1.00 36.00           O  
ATOM    356  CB  PHE A  44       7.395  28.370  42.843  1.00 34.79           C  
ATOM    357  CG  PHE A  44       7.276  27.422  44.003  1.00 36.32           C  
ATOM    358  CD1 PHE A  44       7.355  27.882  45.309  1.00 40.61           C  
ATOM    359  CD2 PHE A  44       7.062  26.068  43.786  1.00 41.25           C  
ATOM    360  CE1 PHE A  44       7.225  27.008  46.386  1.00 41.54           C  
ATOM    361  CE2 PHE A  44       6.928  25.182  44.857  1.00 45.88           C  
ATOM    362  CZ  PHE A  44       7.010  25.655  46.161  1.00 41.05           C  
ATOM    363  N   VAL A  45       9.909  29.481  40.770  1.00 30.79           N  
ATOM    364  CA  VAL A  45      10.200  30.123  39.495  1.00 32.30           C  
ATOM    365  C   VAL A  45      10.329  29.197  38.303  1.00 34.32           C  
ATOM    366  O   VAL A  45      10.702  29.626  37.214  1.00 33.41           O  
ATOM    367  CB  VAL A  45      11.515  30.896  39.575  1.00 35.59           C  
ATOM    368  CG1 VAL A  45      11.483  31.865  40.734  1.00 35.05           C  
ATOM    369  CG2 VAL A  45      12.668  29.908  39.715  1.00 29.09           C  
ATOM    370  N   GLY A  46      10.044  27.925  38.500  1.00 36.65           N  
ATOM    371  CA  GLY A  46      10.188  27.018  37.390  1.00 36.03           C  
ATOM    372  C   GLY A  46       8.999  26.961  36.468  1.00 37.73           C  
ATOM    373  O   GLY A  46       8.035  27.729  36.575  1.00 35.69           O  
ATOM    374  N   SER A  47       9.101  26.022  35.542  1.00 36.28           N  
ATOM    375  CA  SER A  47       8.075  25.750  34.563  1.00 36.89           C  
ATOM    376  C   SER A  47       6.867  25.234  35.352  1.00 35.31           C  
ATOM    377  O   SER A  47       5.710  25.374  34.928  1.00 30.99           O  
ATOM    378  CB  SER A  47       8.600  24.690  33.589  1.00 37.05           C  
ATOM    379  OG  SER A  47       7.618  24.329  32.643  1.00 40.15           O  
ATOM    380  N   TYR A  48       7.136  24.648  36.515  1.00 32.92           N  
ATOM    381  CA  TYR A  48       6.053  24.139  37.350  1.00 36.40           C  
ATOM    382  C   TYR A  48       5.198  25.296  37.849  1.00 34.08           C  
ATOM    383  O   TYR A  48       3.975  25.236  37.793  1.00 39.20           O  
ATOM    384  CB  TYR A  48       6.585  23.357  38.562  1.00 36.56           C  
ATOM    385  CG  TYR A  48       5.495  23.048  39.567  1.00 39.65           C  
ATOM    386  CD1 TYR A  48       4.508  22.097  39.288  1.00 42.12           C  
ATOM    387  CD2 TYR A  48       5.391  23.776  40.759  1.00 43.70           C  
ATOM    388  CE1 TYR A  48       3.438  21.883  40.165  1.00 41.07           C  
ATOM    389  CE2 TYR A  48       4.322  23.573  41.640  1.00 42.49           C  
ATOM    390  CZ  TYR A  48       3.352  22.629  41.333  1.00 45.32           C  
ATOM    391  OH  TYR A  48       2.276  22.458  42.174  1.00 53.69           O  
ATOM    392  N   ALA A  49       5.846  26.345  38.337  1.00 32.57           N  
ATOM    393  CA  ALA A  49       5.133  27.505  38.852  1.00 36.32           C  
ATOM    394  C   ALA A  49       4.188  28.166  37.841  1.00 37.54           C  
ATOM    395  O   ALA A  49       3.182  28.758  38.235  1.00 31.64           O  
ATOM    396  CB  ALA A  49       6.127  28.535  39.375  1.00 33.02           C  
ATOM    397  N   ARG A  50       4.501  28.061  36.548  1.00 35.24           N  
ATOM    398  CA  ARG A  50       3.675  28.681  35.509  1.00 32.89           C  
ATOM    399  C   ARG A  50       2.864  27.666  34.705  1.00 35.65           C  
ATOM    400  O   ARG A  50       2.270  28.010  33.682  1.00 38.41           O  
ATOM    401  CB  ARG A  50       4.559  29.524  34.570  1.00 29.28           C  
ATOM    402  CG  ARG A  50       5.279  30.684  35.274  1.00 30.12           C  
ATOM    403  CD  ARG A  50       6.108  31.534  34.313  1.00 27.78           C  
ATOM    404  NE  ARG A  50       7.140  30.747  33.635  1.00 30.96           N  
ATOM    405  CZ  ARG A  50       8.331  30.458  34.149  1.00 33.68           C  
ATOM    406  NH1 ARG A  50       8.657  30.894  35.357  1.00 29.96           N  
ATOM    407  NH2 ARG A  50       9.200  29.727  33.451  1.00 31.94           N  
ATOM    408  N   ASN A  51       2.824  26.429  35.194  1.00 27.73           N  
ATOM    409  CA  ASN A  51       2.108  25.330  34.551  1.00 36.27           C  
ATOM    410  C   ASN A  51       2.417  25.225  33.057  1.00 35.83           C  
ATOM    411  O   ASN A  51       1.532  24.987  32.232  1.00 37.77           O  
ATOM    412  CB  ASN A  51       0.584  25.442  34.779  1.00 39.82           C  
ATOM    413  CG  ASN A  51      -0.167  24.178  34.347  1.00 53.99           C  
ATOM    414  OD1 ASN A  51       0.214  23.058  34.707  1.00 58.14           O  
ATOM    415  ND2 ASN A  51      -1.241  24.353  33.578  1.00 54.74           N  
ATOM    416  N   THR A  52       3.690  25.401  32.720  1.00 36.69           N  
ATOM    417  CA  THR A  52       4.140  25.300  31.335  1.00 35.69           C  
ATOM    418  C   THR A  52       5.067  24.096  31.150  1.00 35.60           C  
ATOM    419  O   THR A  52       5.665  23.957  30.090  1.00 36.70           O  
ATOM    420  CB  THR A  52       4.924  26.558  30.910  1.00 38.54           C  
ATOM    421  OG1 THR A  52       6.059  26.717  31.770  1.00 30.68           O  
ATOM    422  CG2 THR A  52       4.042  27.806  31.001  1.00 34.37           C  
ATOM    423  N   TRP A  53       5.181  23.226  32.160  1.00 32.84           N  
ATOM    424  CA  TRP A  53       6.086  22.069  32.070  1.00 32.79           C  
ATOM    425  C   TRP A  53       5.560  20.911  31.235  1.00 38.14           C  
ATOM    426  O   TRP A  53       4.380  20.556  31.295  1.00 37.65           O  
ATOM    427  CB  TRP A  53       6.481  21.571  33.478  1.00 34.35           C  
ATOM    428  CG  TRP A  53       5.537  20.563  34.109  1.00 37.33           C  
ATOM    429  CD1 TRP A  53       5.556  19.201  33.950  1.00 41.01           C  
ATOM    430  CD2 TRP A  53       4.436  20.846  34.980  1.00 38.92           C  
ATOM    431  NE1 TRP A  53       4.534  18.623  34.665  1.00 37.14           N  
ATOM    432  CE2 TRP A  53       3.829  19.610  35.304  1.00 43.41           C  
ATOM    433  CE3 TRP A  53       3.899  22.025  35.512  1.00 41.25           C  
ATOM    434  CZ2 TRP A  53       2.713  19.521  36.146  1.00 36.08           C  
ATOM    435  CZ3 TRP A  53       2.785  21.934  36.349  1.00 48.35           C  
ATOM    436  CH2 TRP A  53       2.206  20.690  36.652  1.00 41.11           C  
ATOM    437  N   LEU A  54       6.459  20.321  30.453  1.00 39.64           N  
ATOM    438  CA  LEU A  54       6.118  19.210  29.576  1.00 38.62           C  
ATOM    439  C   LEU A  54       5.776  17.935  30.334  1.00 36.33           C  
ATOM    440  O   LEU A  54       6.357  17.632  31.378  1.00 36.20           O  
ATOM    441  CB  LEU A  54       7.273  18.940  28.606  1.00 37.68           C  
ATOM    442  CG  LEU A  54       7.078  17.863  27.539  1.00 39.79           C  
ATOM    443  CD1 LEU A  54       6.003  18.310  26.557  1.00 37.70           C  
ATOM    444  CD2 LEU A  54       8.404  17.615  26.816  1.00 39.99           C  
ATOM    445  N   LYS A  55       4.811  17.203  29.792  1.00 40.55           N  
ATOM    446  CA  LYS A  55       4.357  15.943  30.362  1.00 40.40           C  
ATOM    447  C   LYS A  55       5.545  15.049  30.662  1.00 39.06           C  
ATOM    448  O   LYS A  55       6.377  14.797  29.785  1.00 39.14           O  
ATOM    449  CB  LYS A  55       3.428  15.232  29.377  1.00 44.41           C  
ATOM    450  CG  LYS A  55       2.963  13.851  29.825  1.00 50.96           C  
ATOM    451  CD  LYS A  55       2.094  13.194  28.758  1.00 52.02           C  
ATOM    452  CE  LYS A  55       1.572  11.847  29.211  1.00 44.82           C  
ATOM    453  NZ  LYS A  55       0.672  11.982  30.388  1.00 52.67           N  
ATOM    454  N   GLY A  56       5.618  14.584  31.909  1.00 37.18           N  
ATOM    455  CA  GLY A  56       6.694  13.706  32.328  1.00 39.18           C  
ATOM    456  C   GLY A  56       7.979  14.408  32.720  1.00 41.91           C  
ATOM    457  O   GLY A  56       8.996  13.755  32.964  1.00 43.36           O  
ATOM    458  N   SER A  57       7.935  15.734  32.803  1.00 39.34           N  
ATOM    459  CA  SER A  57       9.122  16.518  33.135  1.00 41.95           C  
ATOM    460  C   SER A  57       8.954  17.380  34.393  1.00 36.99           C  
ATOM    461  O   SER A  57       9.639  18.387  34.562  1.00 33.05           O  
ATOM    462  CB  SER A  57       9.486  17.390  31.926  1.00 44.33           C  
ATOM    463  OG  SER A  57      10.754  17.995  32.070  1.00 58.47           O  
ATOM    464  N   LEU A  58       8.051  16.965  35.280  1.00 40.61           N  
ATOM    465  CA  LEU A  58       7.783  17.683  36.530  1.00 42.68           C  
ATOM    466  C   LEU A  58       9.015  17.895  37.415  1.00 44.56           C  
ATOM    467  O   LEU A  58       9.774  16.961  37.666  1.00 45.67           O  
ATOM    468  CB  LEU A  58       6.730  16.933  37.351  1.00 45.95           C  
ATOM    469  CG  LEU A  58       6.501  17.464  38.776  1.00 42.97           C  
ATOM    470  CD1 LEU A  58       5.810  18.811  38.697  1.00 33.88           C  
ATOM    471  CD2 LEU A  58       5.667  16.478  39.592  1.00 42.63           C  
ATOM    472  N   GLU A  59       9.197  19.125  37.889  1.00 41.31           N  
ATOM    473  CA  GLU A  59      10.302  19.480  38.780  1.00 39.39           C  
ATOM    474  C   GLU A  59       9.984  20.853  39.367  1.00 37.79           C  
ATOM    475  O   GLU A  59       9.276  21.642  38.750  1.00 34.36           O  
ATOM    476  CB  GLU A  59      11.642  19.536  38.037  1.00 40.17           C  
ATOM    477  CG  GLU A  59      11.809  20.736  37.124  1.00 50.23           C  
ATOM    478  CD  GLU A  59      13.229  20.887  36.616  1.00 48.83           C  
ATOM    479  OE1 GLU A  59      13.796  19.880  36.154  1.00 56.11           O  
ATOM    480  OE2 GLU A  59      13.777  22.008  36.667  1.00 52.26           O  
ATOM    481  N   ILE A  60      10.510  21.135  40.553  1.00 34.55           N  
ATOM    482  CA  ILE A  60      10.245  22.405  41.217  1.00 33.90           C  
ATOM    483  C   ILE A  60      11.503  23.236  41.458  1.00 36.20           C  
ATOM    484  O   ILE A  60      12.508  22.733  41.968  1.00 36.05           O  
ATOM    485  CB  ILE A  60       9.542  22.152  42.571  1.00 36.49           C  
ATOM    486  CG1 ILE A  60       8.259  21.352  42.340  1.00 36.16           C  
ATOM    487  CG2 ILE A  60       9.247  23.478  43.279  1.00 31.84           C  
ATOM    488  CD1 ILE A  60       7.490  21.049  43.611  1.00 34.13           C  
ATOM    489  N   ASP A  61      11.446  24.509  41.081  1.00 33.48           N  
ATOM    490  CA  ASP A  61      12.572  25.413  41.283  1.00 32.82           C  
ATOM    491  C   ASP A  61      12.177  26.468  42.306  1.00 35.45           C  
ATOM    492  O   ASP A  61      11.377  27.356  42.003  1.00 30.04           O  
ATOM    493  CB  ASP A  61      12.953  26.112  39.975  1.00 30.46           C  
ATOM    494  CG  ASP A  61      13.585  25.164  38.955  1.00 38.23           C  
ATOM    495  OD1 ASP A  61      13.824  25.601  37.816  1.00 44.44           O  
ATOM    496  OD2 ASP A  61      13.842  23.992  39.288  1.00 33.16           O  
ATOM    497  N   VAL A  62      12.723  26.368  43.517  1.00 35.14           N  
ATOM    498  CA  VAL A  62      12.421  27.348  44.562  1.00 32.96           C  
ATOM    499  C   VAL A  62      13.655  28.166  44.855  1.00 35.29           C  
ATOM    500  O   VAL A  62      14.690  27.631  45.251  1.00 33.50           O  
ATOM    501  CB  VAL A  62      11.977  26.697  45.884  1.00 35.83           C  
ATOM    502  CG1 VAL A  62      11.752  27.778  46.935  1.00 39.70           C  
ATOM    503  CG2 VAL A  62      10.696  25.902  45.675  1.00 44.07           C  
ATOM    504  N   PHE A  63      13.542  29.469  44.656  1.00 34.08           N  
ATOM    505  CA  PHE A  63      14.648  30.370  44.903  1.00 35.17           C  
ATOM    506  C   PHE A  63      14.434  31.073  46.236  1.00 36.98           C  
ATOM    507  O   PHE A  63      13.321  31.472  46.558  1.00 39.20           O  
ATOM    508  CB  PHE A  63      14.765  31.381  43.757  1.00 33.09           C  
ATOM    509  CG  PHE A  63      15.541  30.869  42.567  1.00 35.38           C  
ATOM    510  CD1 PHE A  63      15.289  29.603  42.045  1.00 31.85           C  
ATOM    511  CD2 PHE A  63      16.527  31.655  41.968  1.00 30.51           C  
ATOM    512  CE1 PHE A  63      16.000  29.132  40.947  1.00 28.36           C  
ATOM    513  CE2 PHE A  63      17.243  31.193  40.866  1.00 32.46           C  
ATOM    514  CZ  PHE A  63      16.983  29.926  40.357  1.00 30.65           C  
ATOM    515  N   LEU A  64      15.506  31.192  47.013  1.00 44.74           N  
ATOM    516  CA  LEU A  64      15.459  31.833  48.320  1.00 46.26           C  
ATOM    517  C   LEU A  64      16.023  33.251  48.202  1.00 44.47           C  
ATOM    518  O   LEU A  64      17.163  33.435  47.793  1.00 44.43           O  
ATOM    519  CB  LEU A  64      16.284  31.019  49.326  1.00 44.35           C  
ATOM    520  CG  LEU A  64      15.998  29.516  49.422  1.00 41.57           C  
ATOM    521  CD1 LEU A  64      16.859  28.913  50.521  1.00 48.02           C  
ATOM    522  CD2 LEU A  64      14.543  29.270  49.720  1.00 40.03           C  
ATOM    523  N   LEU A  65      15.230  34.247  48.584  1.00 51.21           N  
ATOM    524  CA  LEU A  65      15.630  35.665  48.488  1.00 57.11           C  
ATOM    525  C   LEU A  65      16.530  36.181  49.633  1.00 59.13           C  
ATOM    526  O   LEU A  65      16.096  36.195  50.775  1.00 60.75           O  
ATOM    527  CB  LEU A  65      14.350  36.495  48.408  1.00 56.88           C  
ATOM    528  CG  LEU A  65      13.316  35.960  47.409  1.00 55.62           C  
ATOM    529  CD1 LEU A  65      12.051  36.777  47.495  1.00 58.66           C  
ATOM    530  CD2 LEU A  65      13.888  36.007  46.002  1.00 57.83           C  
ATOM    531  N   PHE A  66      17.747  36.650  49.321  1.00 64.63           N  
ATOM    532  CA  PHE A  66      18.709  37.121  50.344  1.00 68.80           C  
ATOM    533  C   PHE A  66      19.459  38.444  50.073  1.00 72.73           C  
ATOM    534  O   PHE A  66      19.692  38.811  48.940  1.00 71.05           O  
ATOM    535  CB  PHE A  66      19.772  36.049  50.564  1.00 68.91           C  
ATOM    536  CG  PHE A  66      19.263  34.790  51.188  1.00 71.56           C  
ATOM    537  CD1 PHE A  66      19.915  33.591  50.945  1.00 72.45           C  
ATOM    538  CD2 PHE A  66      18.171  34.800  52.049  1.00 70.67           C  
ATOM    539  CE1 PHE A  66      19.504  32.420  51.552  1.00 67.50           C  
ATOM    540  CE2 PHE A  66      17.747  33.634  52.666  1.00 71.30           C  
ATOM    541  CZ  PHE A  66      18.418  32.432  52.411  1.00 69.79           C  
ATOM    542  N   PRO A  67      19.846  39.172  51.126  1.00 74.68           N  
ATOM    543  CA  PRO A  67      20.568  40.431  50.876  1.00 76.57           C  
ATOM    544  C   PRO A  67      22.108  40.316  51.044  0.00 79.54           C  
ATOM    545  O   PRO A  67      22.873  40.773  50.188  0.00 79.85           O  
ATOM    546  CB  PRO A  67      19.929  41.393  51.875  1.00 77.16           C  
ATOM    547  CG  PRO A  67      18.631  40.609  52.407  1.00 74.78           C  
ATOM    548  CD  PRO A  67      19.099  39.210  52.397  1.00 76.99           C  
ATOM    549  N   GLU A  68      22.548  39.695  52.139  0.00 82.60           N  
ATOM    550  CA  GLU A  68      23.975  39.511  52.458  1.00 85.61           C  
ATOM    551  C   GLU A  68      24.830  38.879  51.359  1.00 88.69           C  
ATOM    552  O   GLU A  68      24.305  38.379  50.371  1.00 92.77           O  
ATOM    553  CB  GLU A  68      24.111  38.668  53.727  1.00 86.69           C  
ATOM    554  CG  GLU A  68      23.081  37.550  53.870  1.00 84.18           C  
ATOM    555  CD  GLU A  68      22.036  37.859  54.931  1.00 85.01           C  
ATOM    556  OE1 GLU A  68      21.484  38.979  54.930  1.00 85.80           O  
ATOM    557  OE2 GLU A  68      21.745  36.981  55.765  1.00 84.62           O  
ATOM    558  N   GLU A  69      26.152  38.885  51.541  1.00 89.66           N  
ATOM    559  CA  GLU A  69      27.057  38.307  50.539  1.00 91.99           C  
ATOM    560  C   GLU A  69      27.217  36.788  50.594  1.00 92.39           C  
ATOM    561  O   GLU A  69      26.966  36.094  49.602  1.00 93.31           O  
ATOM    562  CB  GLU A  69      28.451  38.921  50.627  1.00 93.01           C  
ATOM    563  CG  GLU A  69      29.367  38.420  49.508  1.00 94.94           C  
ATOM    564  CD  GLU A  69      30.815  38.840  49.658  1.00 97.48           C  
ATOM    565  OE1 GLU A  69      31.477  38.406  50.624  1.00 99.62           O  
ATOM    566  OE2 GLU A  69      31.306  39.598  48.798  1.00100.94           O  
ATOM    567  N   PHE A  70      27.678  36.270  51.728  1.00 94.90           N  
ATOM    568  CA  PHE A  70      27.838  34.828  51.849  1.00 96.05           C  
ATOM    569  C   PHE A  70      26.748  34.198  52.703  1.00 97.21           C  
ATOM    570  O   PHE A  70      26.693  34.383  53.920  1.00 96.54           O  
ATOM    571  CB  PHE A  70      29.213  34.464  52.423  1.00 97.09           C  
ATOM    572  CG  PHE A  70      29.825  33.249  51.780  1.00 98.98           C  
ATOM    573  CD1 PHE A  70      30.365  33.329  50.498  1.00 99.99           C  
ATOM    574  CD2 PHE A  70      29.852  32.022  52.443  1.00100.87           C  
ATOM    575  CE1 PHE A  70      30.921  32.204  49.880  1.00100.93           C  
ATOM    576  CE2 PHE A  70      30.407  30.888  51.831  1.00100.16           C  
ATOM    577  CZ  PHE A  70      30.944  30.984  50.549  1.00100.19           C  
ATOM    578  N   SER A  71      25.876  33.454  52.036  1.00 98.44           N  
ATOM    579  CA  SER A  71      24.770  32.762  52.681  0.00 97.93           C  
ATOM    580  C   SER A  71      24.695  31.414  51.990  0.00 97.74           C  
ATOM    581  O   SER A  71      23.728  30.662  52.134  0.00 97.75           O  
ATOM    582  CB  SER A  71      23.468  33.534  52.479  0.00 98.11           C  
ATOM    583  OG  SER A  71      22.366  32.842  53.035  0.00 98.22           O  
ATOM    584  N   LYS A  72      25.747  31.133  51.227  1.00 97.12           N  
ATOM    585  CA  LYS A  72      25.887  29.882  50.500  1.00 96.92           C  
ATOM    586  C   LYS A  72      25.538  28.763  51.461  1.00 97.13           C  
ATOM    587  O   LYS A  72      25.056  27.711  51.052  1.00 97.10           O  
ATOM    588  CB  LYS A  72      27.333  29.710  50.019  1.00 95.95           C  
ATOM    589  CG  LYS A  72      27.623  28.360  49.370  1.00 97.78           C  
ATOM    590  CD  LYS A  72      29.114  28.161  49.105  1.00 97.83           C  
ATOM    591  CE  LYS A  72      29.400  26.777  48.527  1.00 99.19           C  
ATOM    592  NZ  LYS A  72      30.859  26.514  48.377  1.00 98.21           N  
ATOM    593  N   GLU A  73      25.779  29.012  52.746  1.00 97.05           N  
ATOM    594  CA  GLU A  73      25.507  28.034  53.788  1.00 96.68           C  
ATOM    595  C   GLU A  73      24.114  28.167  54.394  1.00 95.83           C  
ATOM    596  O   GLU A  73      23.521  27.172  54.812  1.00 93.52           O  
ATOM    597  CB  GLU A  73      26.575  28.136  54.880  1.00 99.19           C  
ATOM    598  CG  GLU A  73      26.829  29.549  55.382  1.00100.40           C  
ATOM    599  CD  GLU A  73      28.036  29.634  56.304  1.00104.29           C  
ATOM    600  OE1 GLU A  73      28.048  28.937  57.344  1.00102.96           O  
ATOM    601  OE2 GLU A  73      28.975  30.399  55.988  1.00103.82           O  
ATOM    602  N   GLU A  74      23.589  29.388  54.450  1.00 95.63           N  
ATOM    603  CA  GLU A  74      22.254  29.579  55.001  1.00 95.19           C  
ATOM    604  C   GLU A  74      21.259  28.847  54.111  1.00 94.97           C  
ATOM    605  O   GLU A  74      20.201  28.414  54.570  1.00 92.50           O  
ATOM    606  CB  GLU A  74      21.892  31.059  55.074  1.00 95.12           C  
ATOM    607  CG  GLU A  74      20.458  31.300  55.513  1.00 97.52           C  
ATOM    608  CD  GLU A  74      20.092  32.767  55.539  1.00 98.61           C  
ATOM    609  OE1 GLU A  74      20.290  33.447  54.510  1.00101.12           O  
ATOM    610  OE2 GLU A  74      19.601  33.239  56.587  1.00 97.52           O  
ATOM    611  N   LEU A  75      21.599  28.724  52.831  1.00 94.61           N  
ATOM    612  CA  LEU A  75      20.743  28.006  51.901  1.00 95.99           C  
ATOM    613  C   LEU A  75      21.022  26.527  52.090  1.00 95.41           C  
ATOM    614  O   LEU A  75      20.115  25.699  51.998  1.00 95.12           O  
ATOM    615  CB  LEU A  75      21.041  28.377  50.452  1.00100.29           C  
ATOM    616  CG  LEU A  75      20.302  27.433  49.488  1.00104.48           C  
ATOM    617  CD1 LEU A  75      19.291  28.211  48.665  1.00102.42           C  
ATOM    618  CD2 LEU A  75      21.302  26.708  48.595  1.00102.91           C  
ATOM    619  N   ARG A  76      22.288  26.201  52.337  1.00 94.45           N  
ATOM    620  CA  ARG A  76      22.676  24.817  52.559  1.00 94.34           C  
ATOM    621  C   ARG A  76      21.759  24.280  53.642  1.00 93.58           C  
ATOM    622  O   ARG A  76      21.246  23.167  53.539  1.00 94.91           O  
ATOM    623  CB  ARG A  76      24.126  24.713  53.042  1.00 97.40           C  
ATOM    624  CG  ARG A  76      25.184  25.161  52.048  1.00 99.74           C  
ATOM    625  CD  ARG A  76      25.068  24.450  50.712  1.00101.33           C  
ATOM    626  NE  ARG A  76      26.282  24.611  49.915  1.00104.71           N  
ATOM    627  CZ  ARG A  76      26.419  24.195  48.660  1.00108.44           C  
ATOM    628  NH1 ARG A  76      25.410  23.592  48.044  1.00111.50           N  
ATOM    629  NH2 ARG A  76      27.571  24.368  48.024  1.00109.25           N  
ATOM    630  N   GLU A  77      21.552  25.089  54.678  1.00 90.45           N  
ATOM    631  CA  GLU A  77      20.694  24.700  55.785  1.00 88.68           C  
ATOM    632  C   GLU A  77      19.260  24.520  55.301  1.00 86.39           C  
ATOM    633  O   GLU A  77      18.761  23.400  55.232  1.00 87.41           O  
ATOM    634  CB  GLU A  77      20.723  25.757  56.894  1.00 92.00           C  
ATOM    635  CG  GLU A  77      22.107  26.108  57.437  1.00 95.01           C  
ATOM    636  CD  GLU A  77      22.895  24.901  57.914  1.00 96.29           C  
ATOM    637  OE1 GLU A  77      22.273  23.902  58.337  1.00 97.49           O  
ATOM    638  OE2 GLU A  77      24.143  24.960  57.880  1.00 96.65           O  
ATOM    639  N   ARG A  78      18.612  25.630  54.955  1.00 83.34           N  
ATOM    640  CA  ARG A  78      17.227  25.619  54.489  1.00 80.32           C  
ATOM    641  C   ARG A  78      16.896  24.477  53.539  1.00 76.64           C  
ATOM    642  O   ARG A  78      15.953  23.722  53.777  1.00 74.09           O  
ATOM    643  CB  ARG A  78      16.886  26.945  53.810  1.00 83.31           C  
ATOM    644  CG  ARG A  78      17.032  28.147  54.714  1.00 88.54           C  
ATOM    645  CD  ARG A  78      16.518  29.401  54.041  1.00 92.61           C  
ATOM    646  NE  ARG A  78      16.646  30.567  54.909  1.00 97.34           N  
ATOM    647  CZ  ARG A  78      16.170  31.775  54.618  1.00101.56           C  
ATOM    648  NH1 ARG A  78      15.528  31.983  53.476  1.00102.66           N  
ATOM    649  NH2 ARG A  78      16.342  32.781  55.467  1.00103.54           N  
ATOM    650  N   GLY A  79      17.662  24.360  52.460  1.00 72.77           N  
ATOM    651  CA  GLY A  79      17.414  23.301  51.499  1.00 70.81           C  
ATOM    652  C   GLY A  79      17.500  21.933  52.144  1.00 68.23           C  
ATOM    653  O   GLY A  79      16.607  21.096  52.000  1.00 66.68           O  
ATOM    654  N   LEU A  80      18.589  21.716  52.868  1.00 68.90           N  
ATOM    655  CA  LEU A  80      18.830  20.456  53.556  1.00 67.83           C  
ATOM    656  C   LEU A  80      17.734  20.158  54.578  1.00 63.79           C  
ATOM    657  O   LEU A  80      17.417  18.999  54.836  1.00 59.54           O  
ATOM    658  CB  LEU A  80      20.205  20.515  54.233  1.00 72.50           C  
ATOM    659  CG  LEU A  80      20.751  19.372  55.093  1.00 79.40           C  
ATOM    660  CD1 LEU A  80      20.615  18.040  54.376  1.00 82.35           C  
ATOM    661  CD2 LEU A  80      22.219  19.664  55.415  1.00 77.06           C  
ATOM    662  N   GLU A  81      17.142  21.206  55.141  1.00 60.44           N  
ATOM    663  CA  GLU A  81      16.092  21.038  56.140  1.00 61.16           C  
ATOM    664  C   GLU A  81      14.699  20.827  55.543  1.00 61.16           C  
ATOM    665  O   GLU A  81      13.866  20.143  56.137  1.00 58.30           O  
ATOM    666  CB  GLU A  81      16.059  22.246  57.081  1.00 63.32           C  
ATOM    667  CG  GLU A  81      17.437  22.749  57.515  1.00 72.08           C  
ATOM    668  CD  GLU A  81      18.316  21.671  58.143  1.00 76.47           C  
ATOM    669  OE1 GLU A  81      19.513  21.947  58.388  1.00 75.94           O  
ATOM    670  OE2 GLU A  81      17.819  20.552  58.397  1.00 79.97           O  
ATOM    671  N   ILE A  82      14.441  21.413  54.375  1.00 57.26           N  
ATOM    672  CA  ILE A  82      13.132  21.272  53.739  1.00 58.56           C  
ATOM    673  C   ILE A  82      13.058  20.098  52.767  1.00 54.78           C  
ATOM    674  O   ILE A  82      11.968  19.674  52.387  1.00 54.09           O  
ATOM    675  CB  ILE A  82      12.727  22.560  52.976  1.00 59.25           C  
ATOM    676  CG1 ILE A  82      13.776  22.881  51.912  1.00 60.76           C  
ATOM    677  CG2 ILE A  82      12.567  23.720  53.951  1.00 60.34           C  
ATOM    678  CD1 ILE A  82      13.464  24.104  51.091  1.00 69.66           C  
ATOM    679  N   GLY A  83      14.212  19.575  52.363  1.00 57.00           N  
ATOM    680  CA  GLY A  83      14.218  18.450  51.439  1.00 53.72           C  
ATOM    681  C   GLY A  83      14.279  17.096  52.126  1.00 50.71           C  
ATOM    682  O   GLY A  83      15.095  16.893  53.021  1.00 48.01           O  
ATOM    683  N   LYS A  84      13.417  16.170  51.709  1.00 51.78           N  
ATOM    684  CA  LYS A  84      13.388  14.823  52.283  1.00 51.21           C  
ATOM    685  C   LYS A  84      14.724  14.113  52.075  1.00 52.06           C  
ATOM    686  O   LYS A  84      15.199  13.375  52.943  1.00 48.62           O  
ATOM    687  CB  LYS A  84      12.271  13.999  51.645  1.00 49.14           C  
ATOM    688  CG  LYS A  84      10.887  14.507  51.972  1.00 53.88           C  
ATOM    689  CD  LYS A  84       9.813  13.531  51.544  1.00 51.17           C  
ATOM    690  CE  LYS A  84       8.449  14.009  52.027  1.00 62.86           C  
ATOM    691  NZ  LYS A  84       7.405  12.944  51.999  1.00 60.66           N  
ATOM    692  N   ALA A  85      15.308  14.335  50.903  1.00 52.22           N  
ATOM    693  CA  ALA A  85      16.600  13.772  50.535  1.00 54.05           C  
ATOM    694  C   ALA A  85      17.345  14.928  49.874  1.00 53.80           C  
ATOM    695  O   ALA A  85      16.718  15.794  49.268  1.00 55.92           O  
ATOM    696  CB  ALA A  85      16.416  12.616  49.555  1.00 49.22           C  
ATOM    697  N   VAL A  86      18.668  14.956  49.985  1.00 51.26           N  
ATOM    698  CA  VAL A  86      19.435  16.054  49.400  1.00 55.53           C  
ATOM    699  C   VAL A  86      20.778  15.675  48.790  1.00 55.65           C  
ATOM    700  O   VAL A  86      21.399  14.691  49.193  1.00 55.74           O  
ATOM    701  CB  VAL A  86      19.708  17.158  50.450  1.00 57.35           C  
ATOM    702  CG1 VAL A  86      20.505  16.588  51.612  1.00 58.23           C  
ATOM    703  CG2 VAL A  86      20.490  18.290  49.817  1.00 64.88           C  
ATOM    704  N   LEU A  87      21.215  16.478  47.823  1.00 58.01           N  
ATOM    705  CA  LEU A  87      22.492  16.285  47.154  1.00 61.08           C  
ATOM    706  C   LEU A  87      22.913  17.651  46.633  1.00 63.85           C  
ATOM    707  O   LEU A  87      22.151  18.621  46.717  1.00 65.64           O  
ATOM    708  CB  LEU A  87      22.365  15.329  45.965  1.00 63.61           C  
ATOM    709  CG  LEU A  87      21.840  13.913  46.228  1.00 73.43           C  
ATOM    710  CD1 LEU A  87      21.549  13.196  44.909  1.00 75.34           C  
ATOM    711  CD2 LEU A  87      22.849  13.128  47.054  1.00 68.33           C  
ATOM    712  N   ASP A  88      24.122  17.730  46.093  1.00 68.30           N  
ATOM    713  CA  ASP A  88      24.633  18.983  45.548  1.00 70.29           C  
ATOM    714  C   ASP A  88      25.253  18.741  44.180  1.00 74.75           C  
ATOM    715  O   ASP A  88      26.486  18.905  44.034  1.00 79.82           O  
ATOM    716  CB  ASP A  88      25.661  19.587  46.509  1.00 69.12           C  
ATOM    717  CG  ASP A  88      25.023  20.116  47.789  1.00 70.31           C  
ATOM    718  OD1 ASP A  88      24.094  19.467  48.311  1.00 70.75           O  
ATOM    719  OD2 ASP A  88      25.453  21.181  48.274  1.00 66.35           O  
ATOM    720  N   GLU A  96      26.582  32.367  43.320  1.00 77.69           N  
ATOM    721  CA  GLU A  96      27.994  31.915  43.168  1.00 80.00           C  
ATOM    722  C   GLU A  96      28.065  30.666  42.293  1.00 81.37           C  
ATOM    723  O   GLU A  96      29.011  30.516  41.519  1.00 81.69           O  
ATOM    724  CB  GLU A  96      28.604  31.619  44.540  1.00 81.59           C  
ATOM    725  CG  GLU A  96      28.214  32.622  45.616  1.00 84.55           C  
ATOM    726  CD  GLU A  96      28.944  32.385  46.925  1.00 88.13           C  
ATOM    727  OE1 GLU A  96      28.951  31.228  47.400  1.00 87.97           O  
ATOM    728  OE2 GLU A  96      29.504  33.357  47.480  1.00 88.10           O  
ATOM    729  N   HIS A  97      27.065  29.787  42.438  1.00 81.09           N  
ATOM    730  CA  HIS A  97      26.920  28.530  41.681  1.00 80.07           C  
ATOM    731  C   HIS A  97      26.194  27.422  42.459  1.00 80.82           C  
ATOM    732  O   HIS A  97      25.149  26.935  42.024  1.00 84.23           O  
ATOM    733  CB  HIS A  97      28.276  27.990  41.197  1.00 79.47           C  
ATOM    734  CG  HIS A  97      28.697  28.514  39.861  1.00 80.81           C  
ATOM    735  ND1 HIS A  97      28.051  29.557  39.232  1.00 81.59           N  
ATOM    736  CD2 HIS A  97      29.725  28.165  39.050  1.00 82.90           C  
ATOM    737  CE1 HIS A  97      28.663  29.829  38.093  1.00 82.49           C  
ATOM    738  NE2 HIS A  97      29.683  28.998  37.960  1.00 85.22           N  
ATOM    739  N   PRO A  98      26.734  27.016  43.625  1.00 78.71           N  
ATOM    740  CA  PRO A  98      26.152  25.960  44.471  1.00 75.69           C  
ATOM    741  C   PRO A  98      24.693  26.131  44.917  1.00 71.16           C  
ATOM    742  O   PRO A  98      24.277  27.212  45.331  1.00 69.02           O  
ATOM    743  CB  PRO A  98      27.106  25.913  45.665  1.00 74.72           C  
ATOM    744  CG  PRO A  98      28.414  26.352  45.080  1.00 75.09           C  
ATOM    745  CD  PRO A  98      27.996  27.507  44.208  1.00 78.61           C  
ATOM    746  N   TYR A  99      23.936  25.037  44.841  1.00 68.06           N  
ATOM    747  CA  TYR A  99      22.527  25.018  45.235  1.00 63.68           C  
ATOM    748  C   TYR A  99      22.186  23.624  45.764  1.00 62.65           C  
ATOM    749  O   TYR A  99      22.987  22.699  45.640  1.00 60.46           O  
ATOM    750  CB  TYR A  99      21.634  25.367  44.035  1.00 63.25           C  
ATOM    751  CG  TYR A  99      21.668  24.350  42.916  1.00 63.28           C  
ATOM    752  CD1 TYR A  99      20.665  23.390  42.789  1.00 63.27           C  
ATOM    753  CD2 TYR A  99      22.719  24.329  42.002  1.00 65.53           C  
ATOM    754  CE1 TYR A  99      20.707  22.434  41.779  1.00 63.61           C  
ATOM    755  CE2 TYR A  99      22.774  23.376  40.990  1.00 66.26           C  
ATOM    756  CZ  TYR A  99      21.766  22.431  40.886  1.00 66.39           C  
ATOM    757  OH  TYR A  99      21.824  21.476  39.898  1.00 70.97           O  
ATOM    758  N   VAL A 100      20.999  23.474  46.345  1.00 60.81           N  
ATOM    759  CA  VAL A 100      20.577  22.193  46.905  1.00 56.87           C  
ATOM    760  C   VAL A 100      19.495  21.487  46.091  1.00 56.25           C  
ATOM    761  O   VAL A 100      18.428  22.050  45.846  1.00 50.98           O  
ATOM    762  CB  VAL A 100      20.053  22.383  48.337  1.00 59.73           C  
ATOM    763  CG1 VAL A 100      19.509  21.080  48.872  1.00 55.82           C  
ATOM    764  CG2 VAL A 100      21.164  22.912  49.225  1.00 63.17           C  
ATOM    765  N   HIS A 101      19.771  20.252  45.681  1.00 50.54           N  
ATOM    766  CA  HIS A 101      18.806  19.473  44.910  1.00 51.69           C  
ATOM    767  C   HIS A 101      18.335  18.250  45.683  1.00 47.94           C  
ATOM    768  O   HIS A 101      19.130  17.566  46.319  1.00 50.05           O  
ATOM    769  CB  HIS A 101      19.405  19.012  43.586  1.00 57.24           C  
ATOM    770  CG  HIS A 101      18.528  18.053  42.843  1.00 63.00           C  
ATOM    771  ND1 HIS A 101      17.280  18.403  42.372  1.00 58.20           N  
ATOM    772  CD2 HIS A 101      18.692  16.744  42.538  1.00 64.74           C  
ATOM    773  CE1 HIS A 101      16.713  17.351  41.810  1.00 63.71           C  
ATOM    774  NE2 HIS A 101      17.548  16.331  41.897  1.00 66.72           N  
ATOM    775  N   GLY A 102      17.041  17.964  45.613  1.00 44.70           N  
ATOM    776  CA  GLY A 102      16.522  16.819  46.330  1.00 41.17           C  
ATOM    777  C   GLY A 102      15.113  16.436  45.941  1.00 45.97           C  
ATOM    778  O   GLY A 102      14.681  16.656  44.805  1.00 45.52           O  
ATOM    779  N   VAL A 103      14.387  15.866  46.898  1.00 44.62           N  
ATOM    780  CA  VAL A 103      13.027  15.421  46.656  1.00 48.63           C  
ATOM    781  C   VAL A 103      12.094  15.744  47.819  1.00 51.76           C  
ATOM    782  O   VAL A 103      12.506  15.766  48.982  1.00 50.46           O  
ATOM    783  CB  VAL A 103      12.994  13.885  46.402  1.00 52.31           C  
ATOM    784  CG1 VAL A 103      11.573  13.424  46.135  1.00 53.92           C  
ATOM    785  CG2 VAL A 103      13.885  13.534  45.220  1.00 53.80           C  
ATOM    786  N   VAL A 104      10.833  15.999  47.489  1.00 49.22           N  
ATOM    787  CA  VAL A 104       9.816  16.297  48.485  1.00 50.28           C  
ATOM    788  C   VAL A 104       8.508  15.700  47.981  1.00 51.05           C  
ATOM    789  O   VAL A 104       7.980  16.134  46.961  1.00 50.13           O  
ATOM    790  CB  VAL A 104       9.640  17.828  48.687  1.00 51.06           C  
ATOM    791  CG1 VAL A 104       8.486  18.096  49.632  1.00 47.67           C  
ATOM    792  CG2 VAL A 104      10.923  18.438  49.247  1.00 51.43           C  
ATOM    793  N   LYS A 105       7.989  14.704  48.696  1.00 50.50           N  
ATOM    794  CA  LYS A 105       6.749  14.050  48.298  1.00 53.03           C  
ATOM    795  C   LYS A 105       6.956  13.400  46.933  1.00 55.70           C  
ATOM    796  O   LYS A 105       6.044  13.364  46.102  1.00 55.26           O  
ATOM    797  CB  LYS A 105       5.607  15.068  48.207  1.00 61.20           C  
ATOM    798  CG  LYS A 105       5.197  15.719  49.527  1.00 65.20           C  
ATOM    799  CD  LYS A 105       4.178  14.886  50.279  1.00 64.47           C  
ATOM    800  CE  LYS A 105       3.581  15.683  51.430  1.00 68.81           C  
ATOM    801  NZ  LYS A 105       2.542  14.928  52.187  1.00 64.10           N  
ATOM    802  N   GLY A 106       8.174  12.914  46.701  1.00 56.16           N  
ATOM    803  CA  GLY A 106       8.493  12.257  45.446  1.00 56.07           C  
ATOM    804  C   GLY A 106       8.781  13.151  44.250  1.00 54.89           C  
ATOM    805  O   GLY A 106       8.933  12.654  43.134  1.00 55.05           O  
ATOM    806  N   VAL A 107       8.870  14.460  44.470  1.00 48.22           N  
ATOM    807  CA  VAL A 107       9.132  15.393  43.377  1.00 45.16           C  
ATOM    808  C   VAL A 107      10.510  16.049  43.464  1.00 44.65           C  
ATOM    809  O   VAL A 107      10.937  16.480  44.538  1.00 45.96           O  
ATOM    810  CB  VAL A 107       8.055  16.500  43.337  1.00 45.73           C  
ATOM    811  CG1 VAL A 107       8.375  17.510  42.253  1.00 44.52           C  
ATOM    812  CG2 VAL A 107       6.687  15.875  43.099  1.00 45.82           C  
ATOM    813  N   GLU A 108      11.199  16.116  42.327  1.00 39.08           N  
ATOM    814  CA  GLU A 108      12.513  16.733  42.261  1.00 40.09           C  
ATOM    815  C   GLU A 108      12.373  18.214  42.561  1.00 40.75           C  
ATOM    816  O   GLU A 108      11.467  18.885  42.059  1.00 40.69           O  
ATOM    817  CB  GLU A 108      13.137  16.549  40.878  1.00 45.70           C  
ATOM    818  CG  GLU A 108      13.525  15.116  40.550  1.00 55.15           C  
ATOM    819  CD  GLU A 108      14.251  15.003  39.224  1.00 56.92           C  
ATOM    820  OE1 GLU A 108      13.638  15.310  38.178  1.00 65.76           O  
ATOM    821  OE2 GLU A 108      15.439  14.610  39.227  1.00 66.73           O  
ATOM    822  N   VAL A 109      13.286  18.722  43.373  1.00 39.28           N  
ATOM    823  CA  VAL A 109      13.257  20.114  43.779  1.00 38.07           C  
ATOM    824  C   VAL A 109      14.644  20.722  43.797  1.00 36.98           C  
ATOM    825  O   VAL A 109      15.598  20.091  44.247  1.00 40.95           O  
ATOM    826  CB  VAL A 109      12.660  20.242  45.209  1.00 35.93           C  
ATOM    827  CG1 VAL A 109      12.765  21.665  45.706  1.00 43.28           C  
ATOM    828  CG2 VAL A 109      11.216  19.777  45.214  1.00 34.04           C  
ATOM    829  N   ASP A 110      14.764  21.937  43.285  1.00 30.44           N  
ATOM    830  CA  ASP A 110      16.033  22.642  43.338  1.00 30.67           C  
ATOM    831  C   ASP A 110      15.799  23.823  44.290  1.00 38.56           C  
ATOM    832  O   ASP A 110      14.768  24.501  44.217  1.00 37.93           O  
ATOM    833  CB  ASP A 110      16.475  23.138  41.953  1.00 28.25           C  
ATOM    834  CG  ASP A 110      17.040  22.013  41.076  1.00 35.55           C  
ATOM    835  OD1 ASP A 110      17.469  20.974  41.618  1.00 38.17           O  
ATOM    836  OD2 ASP A 110      17.076  22.171  39.845  1.00 37.08           O  
ATOM    837  N   VAL A 111      16.733  24.026  45.215  1.00 39.69           N  
ATOM    838  CA  VAL A 111      16.655  25.115  46.186  1.00 39.81           C  
ATOM    839  C   VAL A 111      17.874  25.992  45.955  1.00 41.46           C  
ATOM    840  O   VAL A 111      18.995  25.639  46.328  1.00 45.51           O  
ATOM    841  CB  VAL A 111      16.676  24.585  47.634  1.00 40.75           C  
ATOM    842  CG1 VAL A 111      16.634  25.744  48.608  1.00 39.30           C  
ATOM    843  CG2 VAL A 111      15.500  23.659  47.864  1.00 44.65           C  
ATOM    844  N   VAL A 112      17.650  27.145  45.344  1.00 34.98           N  
ATOM    845  CA  VAL A 112      18.743  28.044  45.011  1.00 42.75           C  
ATOM    846  C   VAL A 112      18.732  29.374  45.766  1.00 46.11           C  
ATOM    847  O   VAL A 112      17.668  29.934  46.033  1.00 40.76           O  
ATOM    848  CB  VAL A 112      18.716  28.349  43.495  1.00 41.30           C  
ATOM    849  CG1 VAL A 112      19.957  29.107  43.085  1.00 43.30           C  
ATOM    850  CG2 VAL A 112      18.587  27.049  42.709  1.00 42.66           C  
ATOM    851  N   PRO A 113      19.923  29.880  46.140  1.00 51.44           N  
ATOM    852  CA  PRO A 113      20.038  31.155  46.854  1.00 56.21           C  
ATOM    853  C   PRO A 113      20.087  32.253  45.805  1.00 54.92           C  
ATOM    854  O   PRO A 113      20.391  31.988  44.647  1.00 62.27           O  
ATOM    855  CB  PRO A 113      21.386  31.055  47.576  1.00 56.21           C  
ATOM    856  CG  PRO A 113      21.769  29.621  47.497  1.00 56.31           C  
ATOM    857  CD  PRO A 113      21.201  29.153  46.187  1.00 59.41           C  
ATOM    858  N   CYS A 114      19.795  33.479  46.216  1.00 59.23           N  
ATOM    859  CA  CYS A 114      19.826  34.632  45.322  1.00 59.26           C  
ATOM    860  C   CYS A 114      19.341  35.814  46.143  1.00 60.35           C  
ATOM    861  O   CYS A 114      18.810  35.626  47.235  1.00 59.24           O  
ATOM    862  CB  CYS A 114      18.913  34.418  44.106  1.00 53.07           C  
ATOM    863  SG  CYS A 114      17.161  34.780  44.373  1.00 50.89           S  
ATOM    864  N   TYR A 115      19.514  37.025  45.625  1.00 64.21           N  
ATOM    865  CA  TYR A 115      19.095  38.215  46.357  1.00 66.54           C  
ATOM    866  C   TYR A 115      17.689  38.685  46.029  1.00 66.85           C  
ATOM    867  O   TYR A 115      17.335  38.810  44.858  1.00 68.60           O  
ATOM    868  CB  TYR A 115      20.059  39.380  46.099  1.00 67.47           C  
ATOM    869  CG  TYR A 115      21.515  39.092  46.399  1.00 70.13           C  
ATOM    870  CD1 TYR A 115      22.333  38.465  45.461  1.00 73.19           C  
ATOM    871  CD2 TYR A 115      22.077  39.449  47.621  1.00 72.29           C  
ATOM    872  CE1 TYR A 115      23.674  38.200  45.732  1.00 69.91           C  
ATOM    873  CE2 TYR A 115      23.414  39.186  47.903  1.00 72.17           C  
ATOM    874  CZ  TYR A 115      24.205  38.562  46.957  1.00 73.41           C  
ATOM    875  OH  TYR A 115      25.520  38.293  47.251  1.00 73.41           O  
ATOM    876  N   LYS A 116      16.882  38.926  47.062  1.00 70.29           N  
ATOM    877  CA  LYS A 116      15.541  39.441  46.833  1.00 75.31           C  
ATOM    878  C   LYS A 116      15.911  40.801  46.329  1.00 78.74           C  
ATOM    879  O   LYS A 116      16.484  41.603  47.065  1.00 81.98           O  
ATOM    880  CB  LYS A 116      14.741  39.607  48.121  1.00 74.64           C  
ATOM    881  CG  LYS A 116      13.380  40.251  47.878  1.00 77.77           C  
ATOM    882  CD  LYS A 116      12.728  40.715  49.169  1.00 79.69           C  
ATOM    883  CE  LYS A 116      11.428  41.452  48.883  1.00 77.84           C  
ATOM    884  NZ  LYS A 116      10.798  42.015  50.110  1.00 81.42           N  
ATOM    885  N   LEU A 117      15.615  41.087  45.077  1.00 81.06           N  
ATOM    886  CA  LEU A 117      16.025  42.381  44.618  1.00 83.86           C  
ATOM    887  C   LEU A 117      14.991  43.400  44.331  1.00 86.74           C  
ATOM    888  O   LEU A 117      13.922  43.122  43.773  1.00 83.42           O  
ATOM    889  CB  LEU A 117      16.952  42.257  43.424  1.00 83.01           C  
ATOM    890  CG  LEU A 117      18.396  42.202  43.918  1.00 82.47           C  
ATOM    891  CD1 LEU A 117      19.345  42.095  42.750  1.00 81.56           C  
ATOM    892  CD2 LEU A 117      18.681  43.456  44.738  1.00 83.17           C  
ATOM    893  N   LYS A 118      15.340  44.610  44.738  1.00 90.97           N  
ATOM    894  CA  LYS A 118      14.504  45.765  44.522  1.00 93.51           C  
ATOM    895  C   LYS A 118      14.606  45.963  42.999  1.00 94.45           C  
ATOM    896  O   LYS A 118      15.006  47.038  42.556  1.00 97.21           O  
ATOM    897  CB  LYS A 118      15.124  46.950  45.278  1.00 93.66           C  
ATOM    898  CG  LYS A 118      16.626  46.800  45.692  1.00 95.14           C  
ATOM    899  CD  LYS A 118      16.887  45.942  46.980  1.00 96.09           C  
ATOM    900  CE  LYS A 118      16.822  46.754  48.301  1.00 96.21           C  
ATOM    901  NZ  LYS A 118      17.450  46.063  49.492  1.00 95.25           N  
ATOM    902  N   GLU A 119      14.280  44.939  42.201  1.00 94.29           N  
ATOM    903  CA  GLU A 119      14.389  45.058  40.741  1.00 93.65           C  
ATOM    904  C   GLU A 119      15.792  45.243  40.166  1.00 94.34           C  
ATOM    905  O   GLU A 119      16.676  45.623  40.890  1.00 95.93           O  
ATOM    906  CB  GLU A 119      13.467  46.195  40.283  1.00 92.59           C  
ATOM    907  CG  GLU A 119      12.044  45.972  40.694  1.00 95.24           C  
ATOM    908  CD  GLU A 119      11.648  44.501  40.560  1.00 96.29           C  
ATOM    909  OE1 GLU A 119      12.022  43.647  41.406  1.00 97.85           O  
ATOM    910  OE2 GLU A 119      10.945  44.185  39.587  1.00 96.79           O  
ATOM    911  N   PRO A 120      15.984  44.982  38.853  1.00 94.49           N  
ATOM    912  CA  PRO A 120      17.260  45.107  38.136  1.00 94.15           C  
ATOM    913  C   PRO A 120      18.516  45.624  38.851  1.00 94.90           C  
ATOM    914  O   PRO A 120      18.995  46.722  38.591  1.00 95.84           O  
ATOM    915  CB  PRO A 120      16.852  45.942  36.926  1.00 94.21           C  
ATOM    916  CG  PRO A 120      15.542  45.242  36.574  1.00 94.05           C  
ATOM    917  CD  PRO A 120      14.861  44.950  37.886  1.00 94.91           C  
ATOM    918  N   LYS A 121      19.066  44.799  39.724  0.00 94.74           N  
ATOM    919  CA  LYS A 121      20.277  45.160  40.420  0.00 94.70           C  
ATOM    920  C   LYS A 121      21.037  43.859  40.597  0.00 94.49           C  
ATOM    921  O   LYS A 121      21.723  43.665  41.590  0.00 94.52           O  
ATOM    922  CB  LYS A 121      19.972  45.791  41.779  0.00 94.91           C  
ATOM    923  CG  LYS A 121      19.401  47.195  41.677  0.00 95.33           C  
ATOM    924  CD  LYS A 121      19.261  47.784  43.062  0.00 95.62           C  
ATOM    925  CE  LYS A 121      18.842  49.242  43.044  0.00 95.82           C  
ATOM    926  NZ  LYS A 121      18.705  49.851  44.411  0.00 96.10           N  
ATOM    927  N   ASN A 122      20.890  42.959  39.625  1.00 94.48           N  
ATOM    928  CA  ASN A 122      21.533  41.633  39.645  1.00 93.86           C  
ATOM    929  C   ASN A 122      23.024  41.685  40.018  1.00 93.69           C  
ATOM    930  O   ASN A 122      23.870  42.154  39.250  1.00 92.85           O  
ATOM    931  CB  ASN A 122      21.361  40.969  38.280  1.00 93.94           C  
ATOM    932  CG  ASN A 122      19.916  40.978  37.814  1.00 95.14           C  
ATOM    933  OD1 ASN A 122      19.301  42.038  37.697  1.00 95.90           O  
ATOM    934  ND2 ASN A 122      19.370  39.802  37.539  1.00 98.50           N  
ATOM    935  N   ILE A 123      23.339  41.180  41.204  1.00 93.40           N  
ATOM    936  CA  ILE A 123      24.708  41.166  41.705  1.00 93.01           C  
ATOM    937  C   ILE A 123      25.461  39.964  41.129  1.00 91.94           C  
ATOM    938  O   ILE A 123      25.036  38.822  41.311  1.00 92.30           O  
ATOM    939  CB  ILE A 123      24.697  41.108  43.239  1.00 93.06           C  
ATOM    940  CG1 ILE A 123      23.824  42.249  43.768  1.00 92.33           C  
ATOM    941  CG2 ILE A 123      26.109  41.233  43.775  1.00 94.28           C  
ATOM    942  CD1 ILE A 123      23.560  42.211  45.253  1.00 92.22           C  
ATOM    943  N   LYS A 124      26.575  40.224  40.441  0.00 90.16           N  
ATOM    944  CA  LYS A 124      27.358  39.160  39.807  0.00 88.42           C  
ATOM    945  C   LYS A 124      26.326  38.183  39.268  0.00 86.83           C  
ATOM    946  O   LYS A 124      26.435  36.963  39.427  0.00 86.76           O  
ATOM    947  CB  LYS A 124      28.281  38.471  40.820  0.00 89.10           C  
ATOM    948  CG  LYS A 124      29.295  37.519  40.177  0.00 89.99           C  
ATOM    949  CD  LYS A 124      29.991  38.181  38.996  0.00 90.74           C  
ATOM    950  CE  LYS A 124      30.838  37.204  38.203  0.00 91.21           C  
ATOM    951  NZ  LYS A 124      31.389  37.926  37.026  0.00 91.63           N  
ATOM    952  N   SER A 125      25.318  38.772  38.628  0.00 84.98           N  
ATOM    953  CA  SER A 125      24.181  38.069  38.064  0.00 83.40           C  
ATOM    954  C   SER A 125      24.394  36.677  37.536  1.00 82.41           C  
ATOM    955  O   SER A 125      25.515  36.253  37.264  1.00 86.10           O  
ATOM    956  CB  SER A 125      23.502  38.921  36.970  0.00 83.26           C  
ATOM    957  OG  SER A 125      24.369  39.197  35.892  0.00 83.68           O  
ATOM    958  N   ALA A 126      23.257  35.999  37.389  1.00 77.92           N  
ATOM    959  CA  ALA A 126      23.134  34.638  36.879  1.00 72.50           C  
ATOM    960  C   ALA A 126      21.906  34.052  37.533  1.00 71.23           C  
ATOM    961  O   ALA A 126      20.881  33.830  36.889  1.00 69.99           O  
ATOM    962  CB  ALA A 126      24.337  33.823  37.250  1.00 74.03           C  
ATOM    963  N   VAL A 127      22.027  33.793  38.828  1.00 66.32           N  
ATOM    964  CA  VAL A 127      20.919  33.240  39.579  1.00 61.36           C  
ATOM    965  C   VAL A 127      19.965  34.375  39.973  1.00 59.46           C  
ATOM    966  O   VAL A 127      18.760  34.160  40.108  1.00 52.99           O  
ATOM    967  CB  VAL A 127      21.405  32.494  40.854  1.00 61.12           C  
ATOM    968  CG1 VAL A 127      20.218  31.946  41.605  1.00 67.72           C  
ATOM    969  CG2 VAL A 127      22.338  31.355  40.481  1.00 59.51           C  
ATOM    970  N   ASP A 128      20.498  35.583  40.143  1.00 55.86           N  
ATOM    971  CA  ASP A 128      19.664  36.716  40.517  1.00 54.28           C  
ATOM    972  C   ASP A 128      18.651  37.104  39.438  1.00 49.51           C  
ATOM    973  O   ASP A 128      17.648  37.755  39.750  1.00 52.06           O  
ATOM    974  CB  ASP A 128      20.513  37.947  40.848  1.00 55.46           C  
ATOM    975  CG  ASP A 128      21.483  37.705  41.994  1.00 65.58           C  
ATOM    976  OD1 ASP A 128      22.695  37.544  41.722  1.00 63.53           O  
ATOM    977  OD2 ASP A 128      21.033  37.656  43.157  1.00 61.41           O  
ATOM    978  N   ARG A 129      18.899  36.708  38.187  1.00 43.63           N  
ATOM    979  CA  ARG A 129      17.992  37.032  37.076  1.00 41.65           C  
ATOM    980  C   ARG A 129      16.723  36.193  37.036  1.00 37.40           C  
ATOM    981  O   ARG A 129      15.643  36.685  36.697  1.00 37.12           O  
ATOM    982  CB  ARG A 129      18.680  36.831  35.725  1.00 46.75           C  
ATOM    983  CG  ARG A 129      19.819  37.754  35.405  1.00 54.07           C  
ATOM    984  CD  ARG A 129      19.989  37.849  33.897  1.00 49.21           C  
ATOM    985  NE  ARG A 129      21.351  38.215  33.541  1.00 55.44           N  
ATOM    986  CZ  ARG A 129      22.370  37.363  33.556  1.00 56.76           C  
ATOM    987  NH1 ARG A 129      22.166  36.099  33.905  1.00 50.75           N  
ATOM    988  NH2 ARG A 129      23.590  37.774  33.229  1.00 63.51           N  
ATOM    989  N   THR A 130      16.880  34.913  37.344  1.00 33.43           N  
ATOM    990  CA  THR A 130      15.781  33.973  37.316  1.00 34.32           C  
ATOM    991  C   THR A 130      14.470  34.513  37.881  1.00 39.15           C  
ATOM    992  O   THR A 130      13.423  34.363  37.255  1.00 39.13           O  
ATOM    993  CB  THR A 130      16.187  32.668  38.023  1.00 32.47           C  
ATOM    994  OG1 THR A 130      17.287  32.085  37.315  1.00 36.97           O  
ATOM    995  CG2 THR A 130      15.045  31.673  38.042  1.00 35.32           C  
ATOM    996  N   PRO A 131      14.498  35.152  39.064  1.00 39.49           N  
ATOM    997  CA  PRO A 131      13.214  35.656  39.564  1.00 38.09           C  
ATOM    998  C   PRO A 131      12.555  36.655  38.603  1.00 34.31           C  
ATOM    999  O   PRO A 131      11.337  36.650  38.442  1.00 34.13           O  
ATOM   1000  CB  PRO A 131      13.586  36.284  40.912  1.00 44.86           C  
ATOM   1001  CG  PRO A 131      15.019  36.701  40.716  1.00 49.04           C  
ATOM   1002  CD  PRO A 131      15.602  35.515  39.973  1.00 39.81           C  
ATOM   1003  N   PHE A 132      13.362  37.497  37.962  1.00 32.68           N  
ATOM   1004  CA  PHE A 132      12.842  38.484  37.016  1.00 35.32           C  
ATOM   1005  C   PHE A 132      12.303  37.800  35.770  1.00 34.81           C  
ATOM   1006  O   PHE A 132      11.288  38.217  35.205  1.00 25.81           O  
ATOM   1007  CB  PHE A 132      13.928  39.475  36.612  1.00 36.92           C  
ATOM   1008  CG  PHE A 132      14.459  40.278  37.748  1.00 42.93           C  
ATOM   1009  CD1 PHE A 132      15.535  39.820  38.493  1.00 45.75           C  
ATOM   1010  CD2 PHE A 132      13.866  41.483  38.095  1.00 51.49           C  
ATOM   1011  CE1 PHE A 132      16.021  40.552  39.571  1.00 50.80           C  
ATOM   1012  CE2 PHE A 132      14.343  42.225  39.174  1.00 51.42           C  
ATOM   1013  CZ  PHE A 132      15.421  41.759  39.912  1.00 50.45           C  
ATOM   1014  N   HIS A 133      13.004  36.754  35.338  1.00 35.33           N  
ATOM   1015  CA  HIS A 133      12.582  35.985  34.184  1.00 34.33           C  
ATOM   1016  C   HIS A 133      11.183  35.485  34.483  1.00 31.92           C  
ATOM   1017  O   HIS A 133      10.284  35.592  33.659  1.00 35.85           O  
ATOM   1018  CB  HIS A 133      13.526  34.800  33.960  1.00 32.03           C  
ATOM   1019  CG  HIS A 133      14.824  35.181  33.323  1.00 32.99           C  
ATOM   1020  ND1 HIS A 133      15.909  34.329  33.269  1.00 34.14           N  
ATOM   1021  CD2 HIS A 133      15.203  36.315  32.687  1.00 23.98           C  
ATOM   1022  CE1 HIS A 133      16.899  34.922  32.626  1.00 33.48           C  
ATOM   1023  NE2 HIS A 133      16.495  36.129  32.263  1.00 31.22           N  
ATOM   1024  N   HIS A 134      10.993  34.958  35.683  1.00 32.22           N  
ATOM   1025  CA  HIS A 134       9.686  34.454  36.070  1.00 35.20           C  
ATOM   1026  C   HIS A 134       8.648  35.581  36.152  1.00 34.93           C  
ATOM   1027  O   HIS A 134       7.515  35.416  35.706  1.00 40.76           O  
ATOM   1028  CB  HIS A 134       9.776  33.735  37.423  1.00 33.82           C  
ATOM   1029  CG  HIS A 134       8.447  33.428  38.026  1.00 25.84           C  
ATOM   1030  ND1 HIS A 134       7.553  32.552  37.456  1.00 28.14           N  
ATOM   1031  CD2 HIS A 134       7.847  33.896  39.152  1.00 30.83           C  
ATOM   1032  CE1 HIS A 134       6.460  32.487  38.200  1.00 32.05           C  
ATOM   1033  NE2 HIS A 134       6.618  33.297  39.233  1.00 27.59           N  
ATOM   1034  N   LYS A 135       9.030  36.722  36.712  1.00 39.35           N  
ATOM   1035  CA  LYS A 135       8.088  37.838  36.843  1.00 42.16           C  
ATOM   1036  C   LYS A 135       7.572  38.335  35.489  1.00 42.27           C  
ATOM   1037  O   LYS A 135       6.368  38.537  35.301  1.00 37.46           O  
ATOM   1038  CB  LYS A 135       8.739  38.995  37.616  1.00 46.64           C  
ATOM   1039  CG  LYS A 135       9.027  38.663  39.082  1.00 57.18           C  
ATOM   1040  CD  LYS A 135       9.639  39.840  39.860  1.00 62.63           C  
ATOM   1041  CE  LYS A 135       9.959  39.439  41.307  1.00 62.45           C  
ATOM   1042  NZ  LYS A 135      10.623  40.518  42.101  1.00 63.71           N  
ATOM   1043  N   TRP A 136       8.493  38.517  34.552  1.00 41.03           N  
ATOM   1044  CA  TRP A 136       8.174  38.987  33.211  1.00 34.81           C  
ATOM   1045  C   TRP A 136       7.229  38.015  32.511  1.00 37.62           C  
ATOM   1046  O   TRP A 136       6.235  38.427  31.904  1.00 38.99           O  
ATOM   1047  CB  TRP A 136       9.471  39.135  32.411  1.00 35.22           C  
ATOM   1048  CG  TRP A 136       9.328  39.948  31.186  1.00 32.37           C  
ATOM   1049  CD1 TRP A 136       9.535  41.294  31.058  1.00 33.47           C  
ATOM   1050  CD2 TRP A 136       8.891  39.484  29.914  1.00 28.53           C  
ATOM   1051  NE1 TRP A 136       9.247  41.695  29.774  1.00 32.59           N  
ATOM   1052  CE2 TRP A 136       8.850  40.602  29.051  1.00 30.88           C  
ATOM   1053  CE3 TRP A 136       8.527  38.229  29.415  1.00 30.29           C  
ATOM   1054  CZ2 TRP A 136       8.459  40.500  27.714  1.00 33.00           C  
ATOM   1055  CZ3 TRP A 136       8.139  38.129  28.087  1.00 29.42           C  
ATOM   1056  CH2 TRP A 136       8.109  39.259  27.252  1.00 25.55           C  
ATOM   1057  N   LEU A 137       7.532  36.723  32.612  1.00 34.61           N  
ATOM   1058  CA  LEU A 137       6.725  35.675  31.983  1.00 35.41           C  
ATOM   1059  C   LEU A 137       5.376  35.379  32.629  1.00 37.62           C  
ATOM   1060  O   LEU A 137       4.397  35.105  31.934  1.00 34.49           O  
ATOM   1061  CB  LEU A 137       7.503  34.349  31.944  1.00 36.73           C  
ATOM   1062  CG  LEU A 137       8.709  34.131  31.021  1.00 37.96           C  
ATOM   1063  CD1 LEU A 137       9.319  32.766  31.315  1.00 38.75           C  
ATOM   1064  CD2 LEU A 137       8.273  34.216  29.563  1.00 40.67           C  
ATOM   1065  N   GLU A 138       5.334  35.406  33.958  1.00 38.45           N  
ATOM   1066  CA  GLU A 138       4.119  35.067  34.687  1.00 38.14           C  
ATOM   1067  C   GLU A 138       2.828  35.716  34.184  1.00 37.39           C  
ATOM   1068  O   GLU A 138       1.838  35.030  33.969  1.00 35.35           O  
ATOM   1069  CB  GLU A 138       4.301  35.358  36.180  1.00 38.32           C  
ATOM   1070  CG  GLU A 138       3.105  34.933  37.024  1.00 48.18           C  
ATOM   1071  CD  GLU A 138       3.379  34.995  38.518  1.00 50.44           C  
ATOM   1072  OE1 GLU A 138       3.930  36.011  38.994  1.00 49.01           O  
ATOM   1073  OE2 GLU A 138       3.031  34.024  39.220  1.00 63.50           O  
ATOM   1074  N   GLY A 139       2.838  37.028  33.984  1.00 40.43           N  
ATOM   1075  CA  GLY A 139       1.627  37.690  33.527  1.00 43.98           C  
ATOM   1076  C   GLY A 139       1.431  37.718  32.024  1.00 44.16           C  
ATOM   1077  O   GLY A 139       0.395  38.177  31.539  1.00 49.94           O  
ATOM   1078  N   ARG A 140       2.408  37.227  31.275  1.00 36.32           N  
ATOM   1079  CA  ARG A 140       2.305  37.237  29.822  1.00 33.06           C  
ATOM   1080  C   ARG A 140       2.059  35.863  29.207  1.00 37.39           C  
ATOM   1081  O   ARG A 140       1.543  35.764  28.091  1.00 40.44           O  
ATOM   1082  CB  ARG A 140       3.567  37.851  29.219  1.00 29.28           C  
ATOM   1083  CG  ARG A 140       3.871  39.258  29.705  1.00 30.28           C  
ATOM   1084  CD  ARG A 140       5.167  39.755  29.090  1.00 35.01           C  
ATOM   1085  NE  ARG A 140       5.351  41.203  29.200  1.00 34.54           N  
ATOM   1086  CZ  ARG A 140       5.683  41.838  30.318  1.00 40.53           C  
ATOM   1087  NH1 ARG A 140       5.871  41.158  31.441  1.00 36.03           N  
ATOM   1088  NH2 ARG A 140       5.836  43.155  30.309  1.00 38.77           N  
ATOM   1089  N   ILE A 141       2.412  34.802  29.930  1.00 34.76           N  
ATOM   1090  CA  ILE A 141       2.229  33.460  29.415  1.00 32.42           C  
ATOM   1091  C   ILE A 141       0.871  32.875  29.771  1.00 33.59           C  
ATOM   1092  O   ILE A 141       0.442  31.893  29.178  1.00 37.83           O  
ATOM   1093  CB  ILE A 141       3.342  32.491  29.924  1.00 33.42           C  
ATOM   1094  CG1 ILE A 141       3.319  31.193  29.110  1.00 31.46           C  
ATOM   1095  CG2 ILE A 141       3.101  32.128  31.375  1.00 33.86           C  
ATOM   1096  CD1 ILE A 141       3.606  31.383  27.626  1.00 38.74           C  
ATOM   1097  N   LYS A 142       0.193  33.465  30.745  1.00 36.94           N  
ATOM   1098  CA  LYS A 142      -1.122  32.961  31.147  1.00 38.73           C  
ATOM   1099  C   LYS A 142      -2.052  32.737  29.951  1.00 33.50           C  
ATOM   1100  O   LYS A 142      -2.199  33.609  29.092  1.00 34.00           O  
ATOM   1101  CB  LYS A 142      -1.786  33.940  32.122  1.00 46.35           C  
ATOM   1102  CG  LYS A 142      -1.144  34.010  33.498  1.00 54.52           C  
ATOM   1103  CD  LYS A 142      -1.416  32.748  34.321  1.00 59.93           C  
ATOM   1104  CE  LYS A 142      -0.915  32.901  35.762  1.00 57.62           C  
ATOM   1105  NZ  LYS A 142      -0.917  31.610  36.500  1.00 60.25           N  
ATOM   1106  N   GLY A 143      -2.675  31.565  29.914  1.00 31.41           N  
ATOM   1107  CA  GLY A 143      -3.586  31.219  28.837  1.00 34.75           C  
ATOM   1108  C   GLY A 143      -2.923  30.531  27.656  1.00 38.76           C  
ATOM   1109  O   GLY A 143      -3.599  29.936  26.816  1.00 44.63           O  
ATOM   1110  N   LYS A 144      -1.596  30.596  27.591  1.00 39.09           N  
ATOM   1111  CA  LYS A 144      -0.854  29.997  26.487  1.00 33.15           C  
ATOM   1112  C   LYS A 144       0.055  28.858  26.943  1.00 35.88           C  
ATOM   1113  O   LYS A 144       0.941  28.411  26.201  1.00 34.14           O  
ATOM   1114  CB  LYS A 144      -0.036  31.081  25.799  1.00 33.56           C  
ATOM   1115  CG  LYS A 144      -0.894  32.265  25.396  1.00 42.72           C  
ATOM   1116  CD  LYS A 144      -0.136  33.290  24.598  1.00 43.30           C  
ATOM   1117  CE  LYS A 144      -1.111  34.285  23.994  1.00 52.19           C  
ATOM   1118  NZ  LYS A 144      -0.420  35.239  23.087  1.00 67.25           N  
ATOM   1119  N   GLU A 145      -0.181  28.382  28.158  1.00 32.94           N  
ATOM   1120  CA  GLU A 145       0.617  27.305  28.716  1.00 35.04           C  
ATOM   1121  C   GLU A 145       0.730  26.123  27.766  1.00 32.72           C  
ATOM   1122  O   GLU A 145       1.830  25.631  27.517  1.00 35.11           O  
ATOM   1123  CB  GLU A 145       0.032  26.829  30.055  1.00 36.12           C  
ATOM   1124  CG  GLU A 145      -0.092  27.907  31.130  1.00 34.42           C  
ATOM   1125  CD  GLU A 145      -1.292  28.822  30.913  1.00 43.93           C  
ATOM   1126  OE1 GLU A 145      -2.183  28.440  30.127  1.00 44.28           O  
ATOM   1127  OE2 GLU A 145      -1.355  29.914  31.537  1.00 41.98           O  
ATOM   1128  N   ASN A 146      -0.394  25.659  27.230  1.00 32.40           N  
ATOM   1129  CA  ASN A 146      -0.342  24.510  26.330  1.00 34.97           C  
ATOM   1130  C   ASN A 146       0.371  24.830  25.017  1.00 30.15           C  
ATOM   1131  O   ASN A 146       0.875  23.929  24.358  1.00 31.15           O  
ATOM   1132  CB  ASN A 146      -1.747  23.952  26.055  1.00 39.09           C  
ATOM   1133  CG  ASN A 146      -2.354  23.263  27.276  1.00 49.52           C  
ATOM   1134  OD1 ASN A 146      -1.644  22.640  28.078  1.00 55.18           O  
ATOM   1135  ND2 ASN A 146      -3.674  23.356  27.412  1.00 46.22           N  
ATOM   1136  N   GLU A 147       0.407  26.105  24.636  1.00 29.97           N  
ATOM   1137  CA  GLU A 147       1.112  26.496  23.417  1.00 26.54           C  
ATOM   1138  C   GLU A 147       2.591  26.188  23.682  1.00 26.00           C  
ATOM   1139  O   GLU A 147       3.275  25.602  22.848  1.00 28.68           O  
ATOM   1140  CB  GLU A 147       0.937  27.992  23.134  1.00 26.93           C  
ATOM   1141  CG  GLU A 147      -0.491  28.447  22.840  1.00 25.74           C  
ATOM   1142  CD  GLU A 147      -1.091  27.804  21.595  1.00 30.28           C  
ATOM   1143  OE1 GLU A 147      -0.344  27.256  20.743  1.00 34.06           O  
ATOM   1144  OE2 GLU A 147      -2.329  27.856  21.462  1.00 36.42           O  
ATOM   1145  N   VAL A 148       3.065  26.584  24.859  1.00 28.96           N  
ATOM   1146  CA  VAL A 148       4.445  26.338  25.272  1.00 27.57           C  
ATOM   1147  C   VAL A 148       4.721  24.833  25.265  1.00 31.49           C  
ATOM   1148  O   VAL A 148       5.777  24.382  24.811  1.00 30.16           O  
ATOM   1149  CB  VAL A 148       4.702  26.859  26.700  1.00 26.86           C  
ATOM   1150  CG1 VAL A 148       6.095  26.453  27.162  1.00 31.17           C  
ATOM   1151  CG2 VAL A 148       4.557  28.362  26.743  1.00 30.51           C  
ATOM   1152  N   ARG A 149       3.769  24.058  25.776  1.00 27.37           N  
ATOM   1153  CA  ARG A 149       3.938  22.618  25.824  1.00 26.36           C  
ATOM   1154  C   ARG A 149       4.057  21.987  24.459  1.00 29.45           C  
ATOM   1155  O   ARG A 149       4.844  21.050  24.274  1.00 29.86           O  
ATOM   1156  CB  ARG A 149       2.801  21.981  26.614  1.00 25.27           C  
ATOM   1157  CG  ARG A 149       2.968  22.226  28.099  1.00 27.81           C  
ATOM   1158  CD  ARG A 149       1.741  21.852  28.905  1.00 34.85           C  
ATOM   1159  NE  ARG A 149       2.070  21.821  30.327  1.00 34.85           N  
ATOM   1160  CZ  ARG A 149       1.213  22.093  31.305  1.00 44.78           C  
ATOM   1161  NH1 ARG A 149      -0.039  22.427  31.018  1.00 42.78           N  
ATOM   1162  NH2 ARG A 149       1.608  22.029  32.571  1.00 44.20           N  
ATOM   1163  N   LEU A 150       3.288  22.490  23.495  1.00 29.60           N  
ATOM   1164  CA  LEU A 150       3.354  21.948  22.147  1.00 29.06           C  
ATOM   1165  C   LEU A 150       4.739  22.245  21.582  1.00 27.01           C  
ATOM   1166  O   LEU A 150       5.339  21.408  20.907  1.00 26.32           O  
ATOM   1167  CB  LEU A 150       2.278  22.573  21.248  1.00 27.69           C  
ATOM   1168  CG  LEU A 150       0.832  22.086  21.423  1.00 30.25           C  
ATOM   1169  CD1 LEU A 150      -0.088  22.905  20.528  1.00 25.08           C  
ATOM   1170  CD2 LEU A 150       0.735  20.612  21.063  1.00 30.42           C  
ATOM   1171  N   LEU A 151       5.243  23.441  21.866  1.00 28.00           N  
ATOM   1172  CA  LEU A 151       6.560  23.827  21.378  1.00 27.35           C  
ATOM   1173  C   LEU A 151       7.625  22.893  21.947  1.00 27.89           C  
ATOM   1174  O   LEU A 151       8.443  22.358  21.210  1.00 27.94           O  
ATOM   1175  CB  LEU A 151       6.899  25.255  21.794  1.00 26.43           C  
ATOM   1176  CG  LEU A 151       7.659  26.118  20.778  1.00 30.81           C  
ATOM   1177  CD1 LEU A 151       8.603  27.046  21.511  1.00 23.48           C  
ATOM   1178  CD2 LEU A 151       8.408  25.266  19.780  1.00 25.22           C  
ATOM   1179  N   LYS A 152       7.615  22.731  23.268  1.00 29.72           N  
ATOM   1180  CA  LYS A 152       8.571  21.879  23.959  1.00 28.55           C  
ATOM   1181  C   LYS A 152       8.480  20.433  23.467  1.00 27.97           C  
ATOM   1182  O   LYS A 152       9.500  19.783  23.200  1.00 25.98           O  
ATOM   1183  CB  LYS A 152       8.319  21.939  25.472  1.00 29.54           C  
ATOM   1184  CG  LYS A 152       8.678  23.255  26.140  1.00 24.34           C  
ATOM   1185  CD  LYS A 152       8.393  23.210  27.657  1.00 27.52           C  
ATOM   1186  CE  LYS A 152       8.859  24.471  28.378  1.00 26.69           C  
ATOM   1187  NZ  LYS A 152       8.565  24.436  29.857  1.00 26.93           N  
ATOM   1188  N   GLY A 153       7.255  19.928  23.349  1.00 27.93           N  
ATOM   1189  CA  GLY A 153       7.061  18.562  22.880  1.00 25.73           C  
ATOM   1190  C   GLY A 153       7.595  18.377  21.470  1.00 25.84           C  
ATOM   1191  O   GLY A 153       8.206  17.358  21.160  1.00 24.94           O  
ATOM   1192  N   PHE A 154       7.360  19.372  20.616  1.00 26.23           N  
ATOM   1193  CA  PHE A 154       7.820  19.368  19.218  1.00 26.31           C  
ATOM   1194  C   PHE A 154       9.348  19.304  19.211  1.00 26.44           C  
ATOM   1195  O   PHE A 154       9.950  18.487  18.508  1.00 26.67           O  
ATOM   1196  CB  PHE A 154       7.344  20.661  18.532  1.00 26.64           C  
ATOM   1197  CG  PHE A 154       7.670  20.759  17.058  1.00 28.43           C  
ATOM   1198  CD1 PHE A 154       6.848  20.168  16.104  1.00 26.80           C  
ATOM   1199  CD2 PHE A 154       8.748  21.531  16.623  1.00 27.60           C  
ATOM   1200  CE1 PHE A 154       7.080  20.357  14.739  1.00 26.12           C  
ATOM   1201  CE2 PHE A 154       8.993  21.728  15.262  1.00 28.35           C  
ATOM   1202  CZ  PHE A 154       8.157  21.142  14.316  1.00 28.06           C  
ATOM   1203  N   LEU A 155       9.969  20.164  20.012  1.00 25.93           N  
ATOM   1204  CA  LEU A 155      11.428  20.216  20.111  1.00 24.49           C  
ATOM   1205  C   LEU A 155      11.997  18.918  20.700  1.00 25.75           C  
ATOM   1206  O   LEU A 155      12.948  18.346  20.172  1.00 27.94           O  
ATOM   1207  CB  LEU A 155      11.843  21.424  20.971  1.00 21.11           C  
ATOM   1208  CG  LEU A 155      11.512  22.792  20.346  1.00 21.94           C  
ATOM   1209  CD1 LEU A 155      11.532  23.865  21.414  1.00 24.16           C  
ATOM   1210  CD2 LEU A 155      12.513  23.123  19.224  1.00 20.99           C  
ATOM   1211  N   LYS A 156      11.397  18.438  21.776  1.00 27.50           N  
ATOM   1212  CA  LYS A 156      11.885  17.222  22.419  1.00 27.92           C  
ATOM   1213  C   LYS A 156      11.809  16.003  21.506  1.00 30.31           C  
ATOM   1214  O   LYS A 156      12.761  15.230  21.412  1.00 26.90           O  
ATOM   1215  CB  LYS A 156      11.101  16.953  23.712  1.00 29.19           C  
ATOM   1216  CG  LYS A 156      11.788  15.958  24.648  1.00 33.52           C  
ATOM   1217  CD  LYS A 156      11.327  16.164  26.075  1.00 50.24           C  
ATOM   1218  CE  LYS A 156      12.284  15.544  27.088  1.00 52.79           C  
ATOM   1219  NZ  LYS A 156      12.119  16.226  28.415  1.00 54.26           N  
ATOM   1220  N   ALA A 157      10.682  15.834  20.828  1.00 27.45           N  
ATOM   1221  CA  ALA A 157      10.508  14.696  19.939  1.00 27.24           C  
ATOM   1222  C   ALA A 157      11.557  14.704  18.847  1.00 27.99           C  
ATOM   1223  O   ALA A 157      11.817  13.672  18.222  1.00 28.76           O  
ATOM   1224  CB  ALA A 157       9.113  14.714  19.320  1.00 28.13           C  
ATOM   1225  N   ASN A 158      12.161  15.866  18.615  1.00 24.28           N  
ATOM   1226  CA  ASN A 158      13.175  15.997  17.576  1.00 27.51           C  
ATOM   1227  C   ASN A 158      14.573  16.228  18.141  1.00 27.65           C  
ATOM   1228  O   ASN A 158      15.477  16.706  17.438  1.00 25.85           O  
ATOM   1229  CB  ASN A 158      12.774  17.115  16.601  1.00 29.86           C  
ATOM   1230  CG  ASN A 158      11.578  16.723  15.738  1.00 32.93           C  
ATOM   1231  OD1 ASN A 158      11.683  15.854  14.869  1.00 26.60           O  
ATOM   1232  ND2 ASN A 158      10.434  17.348  15.986  1.00 29.87           N  
ATOM   1233  N   GLY A 159      14.722  15.898  19.425  1.00 25.97           N  
ATOM   1234  CA  GLY A 159      15.997  15.999  20.113  1.00 27.62           C  
ATOM   1235  C   GLY A 159      16.601  17.378  20.283  1.00 27.13           C  
ATOM   1236  O   GLY A 159      17.817  17.493  20.454  1.00 20.73           O  
ATOM   1237  N   ILE A 160      15.778  18.424  20.261  1.00 18.59           N  
ATOM   1238  CA  ILE A 160      16.337  19.759  20.398  1.00 23.09           C  
ATOM   1239  C   ILE A 160      15.745  20.614  21.502  1.00 25.27           C  
ATOM   1240  O   ILE A 160      15.759  21.850  21.431  1.00 26.34           O  
ATOM   1241  CB  ILE A 160      16.310  20.546  19.053  1.00 25.22           C  
ATOM   1242  CG1 ILE A 160      14.943  20.430  18.378  1.00 20.33           C  
ATOM   1243  CG2 ILE A 160      17.398  20.010  18.116  1.00 23.25           C  
ATOM   1244  CD1 ILE A 160      14.867  21.245  17.083  1.00 23.24           C  
ATOM   1245  N   TYR A 161      15.219  19.961  22.531  1.00 21.18           N  
ATOM   1246  CA  TYR A 161      14.724  20.712  23.657  1.00 22.55           C  
ATOM   1247  C   TYR A 161      15.784  20.575  24.744  1.00 27.46           C  
ATOM   1248  O   TYR A 161      16.202  19.464  25.095  1.00 23.63           O  
ATOM   1249  CB  TYR A 161      13.384  20.191  24.168  1.00 24.15           C  
ATOM   1250  CG  TYR A 161      12.955  20.907  25.426  1.00 28.45           C  
ATOM   1251  CD1 TYR A 161      12.835  22.296  25.447  1.00 31.09           C  
ATOM   1252  CD2 TYR A 161      12.667  20.204  26.589  1.00 38.86           C  
ATOM   1253  CE1 TYR A 161      12.441  22.970  26.593  1.00 32.20           C  
ATOM   1254  CE2 TYR A 161      12.264  20.868  27.754  1.00 42.36           C  
ATOM   1255  CZ  TYR A 161      12.152  22.253  27.746  1.00 39.42           C  
ATOM   1256  OH  TYR A 161      11.755  22.915  28.885  1.00 36.09           O  
ATOM   1257  N   GLY A 162      16.232  21.716  25.248  1.00 24.10           N  
ATOM   1258  CA  GLY A 162      17.243  21.730  26.285  1.00 25.66           C  
ATOM   1259  C   GLY A 162      18.446  22.547  25.862  1.00 22.71           C  
ATOM   1260  O   GLY A 162      18.993  22.354  24.782  1.00 23.06           O  
ATOM   1261  N   ALA A 163      18.858  23.470  26.716  1.00 20.44           N  
ATOM   1262  CA  ALA A 163      19.996  24.311  26.404  1.00 22.92           C  
ATOM   1263  C   ALA A 163      21.304  23.754  26.975  1.00 23.88           C  
ATOM   1264  O   ALA A 163      22.343  24.369  26.790  1.00 23.32           O  
ATOM   1265  CB  ALA A 163      19.753  25.722  26.916  1.00 24.57           C  
ATOM   1266  N   GLU A 164      21.261  22.597  27.643  1.00 23.60           N  
ATOM   1267  CA  GLU A 164      22.495  22.015  28.193  1.00 28.17           C  
ATOM   1268  C   GLU A 164      23.428  21.642  27.038  1.00 25.31           C  
ATOM   1269  O   GLU A 164      22.976  21.326  25.938  1.00 25.42           O  
ATOM   1270  CB  GLU A 164      22.214  20.781  29.074  1.00 22.33           C  
ATOM   1271  CG  GLU A 164      21.547  19.585  28.390  1.00 32.36           C  
ATOM   1272  CD  GLU A 164      20.027  19.689  28.412  1.00 43.64           C  
ATOM   1273  OE1 GLU A 164      19.341  18.639  28.339  1.00 35.42           O  
ATOM   1274  OE2 GLU A 164      19.525  20.837  28.498  1.00 38.38           O  
ATOM   1275  N   TYR A 165      24.731  21.681  27.286  1.00 25.73           N  
ATOM   1276  CA  TYR A 165      25.696  21.413  26.226  1.00 25.31           C  
ATOM   1277  C   TYR A 165      25.517  20.085  25.532  1.00 20.47           C  
ATOM   1278  O   TYR A 165      25.877  19.950  24.375  1.00 22.52           O  
ATOM   1279  CB  TYR A 165      27.112  21.563  26.767  1.00 26.53           C  
ATOM   1280  CG  TYR A 165      27.424  22.985  27.177  1.00 33.82           C  
ATOM   1281  CD1 TYR A 165      28.283  23.255  28.248  1.00 37.65           C  
ATOM   1282  CD2 TYR A 165      26.857  24.066  26.503  1.00 42.73           C  
ATOM   1283  CE1 TYR A 165      28.566  24.566  28.639  1.00 39.79           C  
ATOM   1284  CE2 TYR A 165      27.135  25.387  26.886  1.00 46.82           C  
ATOM   1285  CZ  TYR A 165      27.989  25.625  27.955  1.00 46.13           C  
ATOM   1286  OH  TYR A 165      28.258  26.921  28.341  1.00 47.78           O  
ATOM   1287  N   LYS A 166      24.952  19.102  26.220  1.00 25.07           N  
ATOM   1288  CA  LYS A 166      24.740  17.819  25.579  1.00 23.16           C  
ATOM   1289  C   LYS A 166      23.736  17.962  24.440  1.00 27.01           C  
ATOM   1290  O   LYS A 166      23.793  17.233  23.469  1.00 20.91           O  
ATOM   1291  CB  LYS A 166      24.207  16.788  26.582  1.00 28.67           C  
ATOM   1292  CG  LYS A 166      23.785  15.478  25.921  1.00 29.15           C  
ATOM   1293  CD  LYS A 166      23.523  14.380  26.940  1.00 33.93           C  
ATOM   1294  CE  LYS A 166      23.128  13.082  26.252  1.00 39.11           C  
ATOM   1295  NZ  LYS A 166      22.848  12.016  27.251  1.00 47.25           N  
ATOM   1296  N   VAL A 167      22.817  18.915  24.557  1.00 26.06           N  
ATOM   1297  CA  VAL A 167      21.788  19.087  23.540  1.00 23.74           C  
ATOM   1298  C   VAL A 167      22.014  20.304  22.634  1.00 23.87           C  
ATOM   1299  O   VAL A 167      21.875  20.207  21.414  1.00 23.81           O  
ATOM   1300  CB  VAL A 167      20.392  19.191  24.222  1.00 27.74           C  
ATOM   1301  CG1 VAL A 167      19.280  19.225  23.179  1.00 22.23           C  
ATOM   1302  CG2 VAL A 167      20.191  18.009  25.180  1.00 26.71           C  
ATOM   1303  N   ARG A 168      22.373  21.436  23.240  1.00 22.86           N  
ATOM   1304  CA  ARG A 168      22.593  22.688  22.521  1.00 22.78           C  
ATOM   1305  C   ARG A 168      21.317  23.031  21.744  1.00 19.94           C  
ATOM   1306  O   ARG A 168      21.348  23.383  20.564  1.00 18.50           O  
ATOM   1307  CB  ARG A 168      23.807  22.575  21.576  1.00 23.48           C  
ATOM   1308  CG  ARG A 168      25.156  22.462  22.306  1.00 21.21           C  
ATOM   1309  CD  ARG A 168      26.357  22.684  21.355  1.00 25.29           C  
ATOM   1310  NE  ARG A 168      27.635  22.522  22.046  1.00 31.20           N  
ATOM   1311  CZ  ARG A 168      28.193  23.436  22.842  1.00 40.18           C  
ATOM   1312  NH1 ARG A 168      27.587  24.602  23.053  1.00 34.76           N  
ATOM   1313  NH2 ARG A 168      29.361  23.186  23.430  1.00 33.00           N  
ATOM   1314  N   GLY A 169      20.193  22.919  22.437  1.00 21.47           N  
ATOM   1315  CA  GLY A 169      18.907  23.196  21.822  1.00 25.32           C  
ATOM   1316  C   GLY A 169      18.214  24.406  22.412  1.00 23.20           C  
ATOM   1317  O   GLY A 169      18.872  25.392  22.762  1.00 22.92           O  
ATOM   1318  N   PHE A 170      16.891  24.320  22.534  1.00 23.29           N  
ATOM   1319  CA  PHE A 170      16.060  25.418  23.049  1.00 23.75           C  
ATOM   1320  C   PHE A 170      15.759  25.306  24.539  1.00 26.12           C  
ATOM   1321  O   PHE A 170      15.161  24.320  24.981  1.00 27.55           O  
ATOM   1322  CB  PHE A 170      14.697  25.457  22.326  1.00 23.01           C  
ATOM   1323  CG  PHE A 170      14.768  25.843  20.877  1.00 28.07           C  
ATOM   1324  CD1 PHE A 170      15.471  25.064  19.957  1.00 26.85           C  
ATOM   1325  CD2 PHE A 170      14.060  26.956  20.413  1.00 27.46           C  
ATOM   1326  CE1 PHE A 170      15.469  25.386  18.607  1.00 23.73           C  
ATOM   1327  CE2 PHE A 170      14.052  27.290  19.058  1.00 27.15           C  
ATOM   1328  CZ  PHE A 170      14.750  26.505  18.153  1.00 29.28           C  
ATOM   1329  N   SER A 171      16.135  26.316  25.315  1.00 22.93           N  
ATOM   1330  CA  SER A 171      15.839  26.284  26.746  1.00 25.23           C  
ATOM   1331  C   SER A 171      14.335  26.499  26.940  1.00 27.75           C  
ATOM   1332  O   SER A 171      13.633  26.981  26.033  1.00 22.64           O  
ATOM   1333  CB  SER A 171      16.609  27.385  27.488  1.00 25.71           C  
ATOM   1334  OG  SER A 171      16.112  28.671  27.143  1.00 22.81           O  
ATOM   1335  N   GLY A 172      13.841  26.109  28.111  1.00 28.53           N  
ATOM   1336  CA  GLY A 172      12.436  26.291  28.415  1.00 25.29           C  
ATOM   1337  C   GLY A 172      12.132  27.774  28.369  1.00 25.78           C  
ATOM   1338  O   GLY A 172      11.095  28.180  27.855  1.00 27.21           O  
ATOM   1339  N   TYR A 173      13.041  28.590  28.897  1.00 24.73           N  
ATOM   1340  CA  TYR A 173      12.842  30.038  28.893  1.00 29.16           C  
ATOM   1341  C   TYR A 173      12.648  30.521  27.455  1.00 31.73           C  
ATOM   1342  O   TYR A 173      11.726  31.294  27.161  1.00 26.17           O  
ATOM   1343  CB  TYR A 173      14.042  30.757  29.545  1.00 24.66           C  
ATOM   1344  CG  TYR A 173      13.890  32.273  29.685  1.00 27.39           C  
ATOM   1345  CD1 TYR A 173      12.658  32.851  29.985  1.00 32.52           C  
ATOM   1346  CD2 TYR A 173      14.981  33.123  29.513  1.00 27.63           C  
ATOM   1347  CE1 TYR A 173      12.514  34.243  30.106  1.00 28.30           C  
ATOM   1348  CE2 TYR A 173      14.854  34.514  29.631  1.00 27.29           C  
ATOM   1349  CZ  TYR A 173      13.609  35.063  29.925  1.00 29.60           C  
ATOM   1350  OH  TYR A 173      13.464  36.432  29.996  1.00 26.44           O  
ATOM   1351  N   LEU A 174      13.517  30.064  26.553  1.00 26.66           N  
ATOM   1352  CA  LEU A 174      13.418  30.462  25.156  1.00 26.24           C  
ATOM   1353  C   LEU A 174      12.060  30.086  24.563  1.00 23.73           C  
ATOM   1354  O   LEU A 174      11.482  30.856  23.797  1.00 25.14           O  
ATOM   1355  CB  LEU A 174      14.559  29.834  24.325  1.00 25.56           C  
ATOM   1356  CG  LEU A 174      14.559  30.036  22.800  1.00 31.77           C  
ATOM   1357  CD1 LEU A 174      14.492  31.529  22.449  1.00 26.03           C  
ATOM   1358  CD2 LEU A 174      15.841  29.407  22.204  1.00 24.86           C  
ATOM   1359  N   CYS A 175      11.545  28.913  24.917  1.00 25.05           N  
ATOM   1360  CA  CYS A 175      10.243  28.475  24.397  1.00 24.56           C  
ATOM   1361  C   CYS A 175       9.106  29.402  24.841  1.00 30.36           C  
ATOM   1362  O   CYS A 175       8.214  29.730  24.048  1.00 25.76           O  
ATOM   1363  CB  CYS A 175       9.936  27.046  24.852  1.00 27.19           C  
ATOM   1364  SG  CYS A 175      11.065  25.795  24.164  1.00 28.19           S  
ATOM   1365  N   GLU A 176       9.129  29.803  26.109  1.00 22.82           N  
ATOM   1366  CA  GLU A 176       8.102  30.692  26.628  1.00 30.41           C  
ATOM   1367  C   GLU A 176       8.210  32.065  25.989  1.00 26.75           C  
ATOM   1368  O   GLU A 176       7.188  32.658  25.664  1.00 32.32           O  
ATOM   1369  CB  GLU A 176       8.172  30.775  28.165  1.00 32.00           C  
ATOM   1370  CG  GLU A 176       7.757  29.448  28.836  1.00 32.65           C  
ATOM   1371  CD  GLU A 176       7.412  29.585  30.310  1.00 36.05           C  
ATOM   1372  OE1 GLU A 176       6.781  30.599  30.683  1.00 34.97           O  
ATOM   1373  OE2 GLU A 176       7.749  28.665  31.094  1.00 37.34           O  
ATOM   1374  N   LEU A 177       9.424  32.580  25.800  1.00 26.39           N  
ATOM   1375  CA  LEU A 177       9.576  33.888  25.149  1.00 27.73           C  
ATOM   1376  C   LEU A 177       9.044  33.833  23.718  1.00 28.36           C  
ATOM   1377  O   LEU A 177       8.411  34.781  23.246  1.00 25.16           O  
ATOM   1378  CB  LEU A 177      11.042  34.348  25.105  1.00 26.85           C  
ATOM   1379  CG  LEU A 177      11.687  34.867  26.390  1.00 31.60           C  
ATOM   1380  CD1 LEU A 177      13.071  35.441  26.067  1.00 27.91           C  
ATOM   1381  CD2 LEU A 177      10.801  35.938  27.024  1.00 32.11           C  
ATOM   1382  N   LEU A 178       9.302  32.725  23.024  1.00 24.74           N  
ATOM   1383  CA  LEU A 178       8.829  32.581  21.648  1.00 27.05           C  
ATOM   1384  C   LEU A 178       7.300  32.576  21.573  1.00 27.50           C  
ATOM   1385  O   LEU A 178       6.703  33.215  20.707  1.00 26.58           O  
ATOM   1386  CB  LEU A 178       9.384  31.296  21.022  1.00 24.46           C  
ATOM   1387  CG  LEU A 178      10.874  31.356  20.663  1.00 28.68           C  
ATOM   1388  CD1 LEU A 178      11.374  29.983  20.211  1.00 23.18           C  
ATOM   1389  CD2 LEU A 178      11.084  32.391  19.566  1.00 26.53           C  
ATOM   1390  N   ILE A 179       6.671  31.860  22.492  1.00 27.27           N  
ATOM   1391  CA  ILE A 179       5.225  31.765  22.513  1.00 33.56           C  
ATOM   1392  C   ILE A 179       4.600  33.127  22.815  1.00 38.29           C  
ATOM   1393  O   ILE A 179       3.539  33.465  22.287  1.00 33.54           O  
ATOM   1394  CB  ILE A 179       4.768  30.730  23.556  1.00 32.17           C  
ATOM   1395  CG1 ILE A 179       5.166  29.324  23.087  1.00 25.99           C  
ATOM   1396  CG2 ILE A 179       3.276  30.847  23.792  1.00 32.57           C  
ATOM   1397  CD1 ILE A 179       4.596  28.928  21.732  1.00 26.69           C  
ATOM   1398  N   VAL A 180       5.273  33.907  23.652  1.00 34.69           N  
ATOM   1399  CA  VAL A 180       4.790  35.224  24.005  1.00 34.17           C  
ATOM   1400  C   VAL A 180       4.962  36.185  22.838  1.00 39.31           C  
ATOM   1401  O   VAL A 180       4.135  37.083  22.621  1.00 36.14           O  
ATOM   1402  CB  VAL A 180       5.550  35.779  25.219  1.00 33.16           C  
ATOM   1403  CG1 VAL A 180       5.274  37.285  25.377  1.00 29.62           C  
ATOM   1404  CG2 VAL A 180       5.131  35.031  26.464  1.00 27.83           C  
ATOM   1405  N   PHE A 181       6.037  35.991  22.083  1.00 32.81           N  
ATOM   1406  CA  PHE A 181       6.323  36.847  20.946  1.00 33.54           C  
ATOM   1407  C   PHE A 181       5.397  36.569  19.764  1.00 30.18           C  
ATOM   1408  O   PHE A 181       4.920  37.504  19.115  1.00 28.51           O  
ATOM   1409  CB  PHE A 181       7.768  36.662  20.497  1.00 27.79           C  
ATOM   1410  CG  PHE A 181       8.252  37.721  19.543  1.00 27.76           C  
ATOM   1411  CD1 PHE A 181       8.703  38.951  20.015  1.00 24.83           C  
ATOM   1412  CD2 PHE A 181       8.299  37.474  18.181  1.00 27.05           C  
ATOM   1413  CE1 PHE A 181       9.204  39.919  19.137  1.00 27.22           C  
ATOM   1414  CE2 PHE A 181       8.799  38.439  17.294  1.00 32.31           C  
ATOM   1415  CZ  PHE A 181       9.252  39.660  17.773  1.00 22.30           C  
ATOM   1416  N   TYR A 182       5.133  35.295  19.488  1.00 27.13           N  
ATOM   1417  CA  TYR A 182       4.289  34.950  18.353  1.00 31.95           C  
ATOM   1418  C   TYR A 182       2.841  34.641  18.689  1.00 31.97           C  
ATOM   1419  O   TYR A 182       1.999  34.578  17.796  1.00 31.66           O  
ATOM   1420  CB  TYR A 182       4.899  33.788  17.561  1.00 27.65           C  
ATOM   1421  CG  TYR A 182       6.215  34.140  16.908  1.00 29.20           C  
ATOM   1422  CD1 TYR A 182       7.404  33.544  17.336  1.00 27.26           C  
ATOM   1423  CD2 TYR A 182       6.274  35.054  15.850  1.00 21.98           C  
ATOM   1424  CE1 TYR A 182       8.610  33.842  16.724  1.00 26.37           C  
ATOM   1425  CE2 TYR A 182       7.467  35.359  15.240  1.00 22.85           C  
ATOM   1426  CZ  TYR A 182       8.641  34.743  15.681  1.00 23.63           C  
ATOM   1427  OH  TYR A 182       9.841  35.020  15.071  1.00 27.19           O  
ATOM   1428  N   GLY A 183       2.555  34.434  19.969  1.00 30.86           N  
ATOM   1429  CA  GLY A 183       1.191  34.167  20.376  1.00 24.57           C  
ATOM   1430  C   GLY A 183       0.786  32.719  20.515  1.00 28.91           C  
ATOM   1431  O   GLY A 183      -0.056  32.401  21.341  1.00 28.72           O  
ATOM   1432  N   SER A 184       1.373  31.829  19.727  1.00 28.59           N  
ATOM   1433  CA  SER A 184       0.984  30.423  19.803  1.00 30.14           C  
ATOM   1434  C   SER A 184       2.047  29.532  19.174  1.00 25.35           C  
ATOM   1435  O   SER A 184       2.992  30.020  18.566  1.00 24.22           O  
ATOM   1436  CB  SER A 184      -0.328  30.212  19.039  1.00 32.82           C  
ATOM   1437  OG  SER A 184      -0.108  30.427  17.646  1.00 28.30           O  
ATOM   1438  N   PHE A 185       1.880  28.224  19.316  1.00 24.38           N  
ATOM   1439  CA  PHE A 185       2.825  27.282  18.723  1.00 27.18           C  
ATOM   1440  C   PHE A 185       2.783  27.402  17.202  1.00 30.16           C  
ATOM   1441  O   PHE A 185       3.809  27.615  16.553  1.00 27.72           O  
ATOM   1442  CB  PHE A 185       2.465  25.848  19.088  1.00 25.12           C  
ATOM   1443  CG  PHE A 185       3.276  24.822  18.352  1.00 24.75           C  
ATOM   1444  CD1 PHE A 185       4.607  24.601  18.682  1.00 24.07           C  
ATOM   1445  CD2 PHE A 185       2.711  24.086  17.316  1.00 27.98           C  
ATOM   1446  CE1 PHE A 185       5.366  23.659  17.988  1.00 28.43           C  
ATOM   1447  CE2 PHE A 185       3.459  23.146  16.616  1.00 33.40           C  
ATOM   1448  CZ  PHE A 185       4.788  22.928  16.951  1.00 28.27           C  
ATOM   1449  N   LEU A 186       1.582  27.285  16.639  1.00 27.39           N  
ATOM   1450  CA  LEU A 186       1.413  27.335  15.193  1.00 26.77           C  
ATOM   1451  C   LEU A 186       2.055  28.573  14.581  1.00 25.56           C  
ATOM   1452  O   LEU A 186       2.747  28.474  13.572  1.00 25.74           O  
ATOM   1453  CB  LEU A 186      -0.080  27.289  14.826  1.00 35.56           C  
ATOM   1454  CG  LEU A 186      -0.499  26.595  13.520  1.00 42.51           C  
ATOM   1455  CD1 LEU A 186      -1.975  26.851  13.261  1.00 44.53           C  
ATOM   1456  CD2 LEU A 186       0.313  27.098  12.357  1.00 46.51           C  
ATOM   1457  N   GLU A 187       1.842  29.736  15.192  1.00 24.57           N  
ATOM   1458  CA  GLU A 187       2.397  30.977  14.649  1.00 27.53           C  
ATOM   1459  C   GLU A 187       3.925  30.980  14.794  1.00 21.04           C  
ATOM   1460  O   GLU A 187       4.634  31.515  13.955  1.00 23.31           O  
ATOM   1461  CB  GLU A 187       1.754  32.183  15.358  1.00 28.61           C  
ATOM   1462  CG  GLU A 187       1.865  33.535  14.637  1.00 35.22           C  
ATOM   1463  CD  GLU A 187       1.326  33.512  13.206  1.00 37.71           C  
ATOM   1464  OE1 GLU A 187       0.327  32.811  12.935  1.00 32.57           O  
ATOM   1465  OE2 GLU A 187       1.910  34.209  12.347  1.00 41.69           O  
ATOM   1466  N   THR A 188       4.428  30.367  15.857  1.00 26.68           N  
ATOM   1467  CA  THR A 188       5.877  30.298  16.049  1.00 25.88           C  
ATOM   1468  C   THR A 188       6.497  29.510  14.895  1.00 24.11           C  
ATOM   1469  O   THR A 188       7.447  29.968  14.261  1.00 24.78           O  
ATOM   1470  CB  THR A 188       6.242  29.606  17.379  1.00 26.42           C  
ATOM   1471  OG1 THR A 188       5.816  30.431  18.469  1.00 25.43           O  
ATOM   1472  CG2 THR A 188       7.766  29.387  17.481  1.00 27.61           C  
ATOM   1473  N   VAL A 189       5.954  28.333  14.606  1.00 22.06           N  
ATOM   1474  CA  VAL A 189       6.502  27.533  13.528  1.00 23.98           C  
ATOM   1475  C   VAL A 189       6.326  28.188  12.156  1.00 23.26           C  
ATOM   1476  O   VAL A 189       7.222  28.130  11.326  1.00 26.06           O  
ATOM   1477  CB  VAL A 189       5.910  26.096  13.518  1.00 29.98           C  
ATOM   1478  CG1 VAL A 189       5.929  25.526  14.916  1.00 24.45           C  
ATOM   1479  CG2 VAL A 189       4.519  26.091  12.943  1.00 40.70           C  
ATOM   1480  N   LYS A 190       5.191  28.831  11.911  1.00 25.37           N  
ATOM   1481  CA  LYS A 190       4.985  29.469  10.614  1.00 27.70           C  
ATOM   1482  C   LYS A 190       6.058  30.525  10.342  1.00 26.18           C  
ATOM   1483  O   LYS A 190       6.619  30.578   9.243  1.00 27.21           O  
ATOM   1484  CB  LYS A 190       3.590  30.107  10.544  1.00 28.51           C  
ATOM   1485  CG  LYS A 190       2.452  29.099  10.446  1.00 33.26           C  
ATOM   1486  CD  LYS A 190       1.091  29.763  10.656  1.00 41.11           C  
ATOM   1487  CE  LYS A 190       0.812  30.848   9.617  1.00 44.80           C  
ATOM   1488  NZ  LYS A 190      -0.471  31.567   9.893  1.00 47.06           N  
ATOM   1489  N   ASN A 191       6.361  31.348  11.347  1.00 27.07           N  
ATOM   1490  CA  ASN A 191       7.362  32.400  11.193  1.00 25.09           C  
ATOM   1491  C   ASN A 191       8.809  31.900  11.246  1.00 28.48           C  
ATOM   1492  O   ASN A 191       9.699  32.481  10.602  1.00 28.64           O  
ATOM   1493  CB  ASN A 191       7.152  33.492  12.256  1.00 23.94           C  
ATOM   1494  CG  ASN A 191       5.877  34.325  12.010  1.00 26.42           C  
ATOM   1495  OD1 ASN A 191       4.782  34.005  12.501  1.00 26.13           O  
ATOM   1496  ND2 ASN A 191       6.023  35.381  11.230  1.00 29.83           N  
ATOM   1497  N   ALA A 192       9.049  30.831  12.006  1.00 26.41           N  
ATOM   1498  CA  ALA A 192      10.398  30.277  12.119  1.00 24.56           C  
ATOM   1499  C   ALA A 192      10.881  29.756  10.765  1.00 27.44           C  
ATOM   1500  O   ALA A 192      12.085  29.594  10.535  1.00 29.73           O  
ATOM   1501  CB  ALA A 192      10.424  29.153  13.162  1.00 23.38           C  
ATOM   1502  N   ARG A 193       9.946  29.502   9.861  1.00 24.85           N  
ATOM   1503  CA  ARG A 193      10.320  29.023   8.541  1.00 29.79           C  
ATOM   1504  C   ARG A 193      11.172  30.068   7.841  1.00 28.56           C  
ATOM   1505  O   ARG A 193      11.889  29.759   6.896  1.00 26.99           O  
ATOM   1506  CB  ARG A 193       9.076  28.739   7.698  1.00 34.55           C  
ATOM   1507  CG  ARG A 193       8.174  27.652   8.256  1.00 33.06           C  
ATOM   1508  CD  ARG A 193       6.987  27.451   7.343  1.00 35.75           C  
ATOM   1509  NE  ARG A 193       6.074  28.596   7.357  1.00 33.47           N  
ATOM   1510  CZ  ARG A 193       4.980  28.674   6.604  1.00 37.24           C  
ATOM   1511  NH1 ARG A 193       4.674  27.675   5.777  1.00 29.76           N  
ATOM   1512  NH2 ARG A 193       4.188  29.741   6.681  1.00 36.77           N  
ATOM   1513  N   ARG A 194      11.098  31.312   8.309  1.00 25.68           N  
ATOM   1514  CA  ARG A 194      11.867  32.378   7.691  1.00 28.72           C  
ATOM   1515  C   ARG A 194      13.035  32.890   8.536  1.00 27.31           C  
ATOM   1516  O   ARG A 194      13.668  33.886   8.183  1.00 28.57           O  
ATOM   1517  CB  ARG A 194      10.925  33.535   7.296  1.00 33.36           C  
ATOM   1518  CG  ARG A 194       9.989  33.165   6.125  1.00 35.79           C  
ATOM   1519  CD  ARG A 194       9.057  34.315   5.704  1.00 40.24           C  
ATOM   1520  NE  ARG A 194       8.089  34.662   6.746  1.00 39.06           N  
ATOM   1521  CZ  ARG A 194       7.040  33.915   7.084  1.00 40.32           C  
ATOM   1522  NH1 ARG A 194       6.800  32.761   6.463  1.00 45.87           N  
ATOM   1523  NH2 ARG A 194       6.228  34.321   8.049  1.00 39.64           N  
ATOM   1524  N   TRP A 195      13.338  32.212   9.641  1.00 24.98           N  
ATOM   1525  CA  TRP A 195      14.466  32.638  10.470  1.00 23.75           C  
ATOM   1526  C   TRP A 195      15.770  32.384   9.727  1.00 24.44           C  
ATOM   1527  O   TRP A 195      15.863  31.447   8.937  1.00 26.85           O  
ATOM   1528  CB  TRP A 195      14.537  31.855  11.777  1.00 22.48           C  
ATOM   1529  CG  TRP A 195      13.497  32.134  12.798  1.00 22.77           C  
ATOM   1530  CD1 TRP A 195      12.595  33.172  12.824  1.00 26.47           C  
ATOM   1531  CD2 TRP A 195      13.280  31.382  13.993  1.00 23.62           C  
ATOM   1532  NE1 TRP A 195      11.832  33.100  13.970  1.00 25.18           N  
ATOM   1533  CE2 TRP A 195      12.234  32.013  14.703  1.00 23.80           C  
ATOM   1534  CE3 TRP A 195      13.874  30.230  14.538  1.00 25.70           C  
ATOM   1535  CZ2 TRP A 195      11.773  31.533  15.931  1.00 28.63           C  
ATOM   1536  CZ3 TRP A 195      13.411  29.750  15.766  1.00 19.90           C  
ATOM   1537  CH2 TRP A 195      12.373  30.402  16.445  1.00 27.21           C  
ATOM   1538  N   THR A 196      16.781  33.206   9.994  1.00 23.99           N  
ATOM   1539  CA  THR A 196      18.093  33.044   9.376  1.00 20.46           C  
ATOM   1540  C   THR A 196      19.118  33.036  10.490  1.00 26.24           C  
ATOM   1541  O   THR A 196      18.784  33.310  11.639  1.00 25.83           O  
ATOM   1542  CB  THR A 196      18.442  34.212   8.447  1.00 23.94           C  
ATOM   1543  OG1 THR A 196      18.820  35.353   9.242  1.00 27.33           O  
ATOM   1544  CG2 THR A 196      17.240  34.564   7.576  1.00 25.87           C  
ATOM   1545  N   ARG A 197      20.366  32.723  10.140  1.00 24.84           N  
ATOM   1546  CA  ARG A 197      21.448  32.679  11.099  1.00 24.35           C  
ATOM   1547  C   ARG A 197      21.801  34.080  11.607  1.00 27.97           C  
ATOM   1548  O   ARG A 197      22.651  34.226  12.484  1.00 25.39           O  
ATOM   1549  CB  ARG A 197      22.689  32.014  10.473  1.00 24.95           C  
ATOM   1550  CG  ARG A 197      23.390  32.823   9.388  1.00 26.96           C  
ATOM   1551  CD  ARG A 197      24.459  31.987   8.698  1.00 24.99           C  
ATOM   1552  NE  ARG A 197      23.822  30.879   7.998  1.00 21.76           N  
ATOM   1553  CZ  ARG A 197      24.454  29.808   7.525  1.00 23.93           C  
ATOM   1554  NH1 ARG A 197      25.765  29.672   7.671  1.00 23.90           N  
ATOM   1555  NH2 ARG A 197      23.768  28.886   6.877  1.00 23.40           N  
ATOM   1556  N   ARG A 198      21.152  35.106  11.061  1.00 28.14           N  
ATOM   1557  CA  ARG A 198      21.407  36.480  11.494  1.00 29.30           C  
ATOM   1558  C   ARG A 198      20.153  37.116  12.096  1.00 30.60           C  
ATOM   1559  O   ARG A 198      20.115  38.324  12.341  1.00 24.75           O  
ATOM   1560  CB  ARG A 198      21.889  37.326  10.312  1.00 30.68           C  
ATOM   1561  CG  ARG A 198      23.187  36.809   9.700  1.00 42.71           C  
ATOM   1562  CD  ARG A 198      23.566  37.546   8.431  1.00 50.74           C  
ATOM   1563  NE  ARG A 198      24.648  36.855   7.728  1.00 64.58           N  
ATOM   1564  CZ  ARG A 198      25.844  36.608   8.256  1.00 60.06           C  
ATOM   1565  NH1 ARG A 198      26.116  36.999   9.494  1.00 65.27           N  
ATOM   1566  NH2 ARG A 198      26.764  35.961   7.555  1.00 56.93           N  
ATOM   1567  N   THR A 199      19.138  36.295  12.351  1.00 28.45           N  
ATOM   1568  CA  THR A 199      17.885  36.788  12.899  1.00 26.23           C  
ATOM   1569  C   THR A 199      17.951  37.184  14.370  1.00 29.20           C  
ATOM   1570  O   THR A 199      18.385  36.403  15.220  1.00 27.38           O  
ATOM   1571  CB  THR A 199      16.760  35.741  12.706  1.00 23.43           C  
ATOM   1572  OG1 THR A 199      16.545  35.537  11.304  1.00 24.91           O  
ATOM   1573  CG2 THR A 199      15.446  36.215  13.363  1.00 23.22           C  
ATOM   1574  N   VAL A 200      17.509  38.407  14.661  1.00 27.49           N  
ATOM   1575  CA  VAL A 200      17.484  38.919  16.026  1.00 25.26           C  
ATOM   1576  C   VAL A 200      16.026  39.112  16.430  1.00 29.13           C  
ATOM   1577  O   VAL A 200      15.303  39.909  15.816  1.00 27.11           O  
ATOM   1578  CB  VAL A 200      18.205  40.294  16.149  1.00 30.92           C  
ATOM   1579  CG1 VAL A 200      18.021  40.868  17.566  1.00 25.15           C  
ATOM   1580  CG2 VAL A 200      19.682  40.143  15.841  1.00 26.08           C  
ATOM   1581  N   ILE A 201      15.590  38.353  17.432  1.00 22.82           N  
ATOM   1582  CA  ILE A 201      14.233  38.455  17.941  1.00 22.78           C  
ATOM   1583  C   ILE A 201      14.281  39.256  19.238  1.00 26.01           C  
ATOM   1584  O   ILE A 201      14.681  38.750  20.288  1.00 24.42           O  
ATOM   1585  CB  ILE A 201      13.611  37.063  18.193  1.00 23.50           C  
ATOM   1586  CG1 ILE A 201      13.579  36.262  16.888  1.00 20.33           C  
ATOM   1587  CG2 ILE A 201      12.160  37.216  18.711  1.00 26.84           C  
ATOM   1588  CD1 ILE A 201      12.961  34.878  17.013  1.00 18.46           C  
ATOM   1589  N   ASP A 202      13.888  40.525  19.153  1.00 26.48           N  
ATOM   1590  CA  ASP A 202      13.916  41.407  20.314  1.00 28.59           C  
ATOM   1591  C   ASP A 202      12.515  41.486  20.895  1.00 26.38           C  
ATOM   1592  O   ASP A 202      11.711  42.327  20.500  1.00 27.37           O  
ATOM   1593  CB  ASP A 202      14.428  42.789  19.880  1.00 29.53           C  
ATOM   1594  CG  ASP A 202      14.699  43.721  21.050  1.00 28.05           C  
ATOM   1595  OD1 ASP A 202      15.385  44.740  20.833  1.00 32.26           O  
ATOM   1596  OD2 ASP A 202      14.224  43.459  22.174  1.00 29.53           O  
ATOM   1597  N   VAL A 203      12.252  40.585  21.835  1.00 24.37           N  
ATOM   1598  CA  VAL A 203      10.975  40.431  22.518  1.00 24.40           C  
ATOM   1599  C   VAL A 203      10.445  41.699  23.171  1.00 27.92           C  
ATOM   1600  O   VAL A 203       9.289  42.072  22.968  1.00 28.56           O  
ATOM   1601  CB  VAL A 203      11.089  39.346  23.603  1.00 29.83           C  
ATOM   1602  CG1 VAL A 203       9.725  39.008  24.140  1.00 31.21           C  
ATOM   1603  CG2 VAL A 203      11.781  38.096  23.015  1.00 36.28           C  
ATOM   1604  N   ALA A 204      11.295  42.351  23.958  1.00 26.62           N  
ATOM   1605  CA  ALA A 204      10.911  43.568  24.651  1.00 27.51           C  
ATOM   1606  C   ALA A 204      10.460  44.680  23.699  1.00 28.13           C  
ATOM   1607  O   ALA A 204       9.610  45.485  24.064  1.00 29.98           O  
ATOM   1608  CB  ALA A 204      12.073  44.059  25.526  1.00 29.43           C  
ATOM   1609  N   LYS A 205      11.023  44.735  22.492  1.00 27.69           N  
ATOM   1610  CA  LYS A 205      10.644  45.780  21.532  1.00 28.07           C  
ATOM   1611  C   LYS A 205       9.676  45.283  20.467  1.00 25.61           C  
ATOM   1612  O   LYS A 205       9.355  46.002  19.509  1.00 23.89           O  
ATOM   1613  CB  LYS A 205      11.879  46.361  20.849  1.00 31.95           C  
ATOM   1614  CG  LYS A 205      12.890  46.961  21.816  1.00 34.07           C  
ATOM   1615  CD  LYS A 205      13.972  47.734  21.084  1.00 36.31           C  
ATOM   1616  CE  LYS A 205      14.868  48.457  22.081  1.00 43.52           C  
ATOM   1617  NZ  LYS A 205      15.975  49.187  21.415  1.00 49.61           N  
ATOM   1618  N   GLY A 206       9.225  44.046  20.635  1.00 22.16           N  
ATOM   1619  CA  GLY A 206       8.291  43.459  19.695  1.00 23.64           C  
ATOM   1620  C   GLY A 206       8.739  43.493  18.244  1.00 27.54           C  
ATOM   1621  O   GLY A 206       7.899  43.572  17.339  1.00 26.35           O  
ATOM   1622  N   GLU A 207      10.049  43.412  18.013  1.00 27.11           N  
ATOM   1623  CA  GLU A 207      10.562  43.454  16.655  1.00 30.35           C  
ATOM   1624  C   GLU A 207      11.579  42.380  16.268  1.00 28.55           C  
ATOM   1625  O   GLU A 207      12.189  41.739  17.115  1.00 28.85           O  
ATOM   1626  CB  GLU A 207      11.159  44.838  16.363  1.00 40.03           C  
ATOM   1627  CG  GLU A 207      12.612  45.052  16.783  1.00 36.23           C  
ATOM   1628  CD  GLU A 207      13.133  46.448  16.400  1.00 40.90           C  
ATOM   1629  OE1 GLU A 207      14.364  46.666  16.455  1.00 36.44           O  
ATOM   1630  OE2 GLU A 207      12.310  47.329  16.054  1.00 34.70           O  
ATOM   1631  N   VAL A 208      11.731  42.187  14.962  1.00 28.75           N  
ATOM   1632  CA  VAL A 208      12.699  41.237  14.429  1.00 31.23           C  
ATOM   1633  C   VAL A 208      13.594  42.075  13.532  1.00 30.83           C  
ATOM   1634  O   VAL A 208      13.117  42.951  12.820  1.00 33.69           O  
ATOM   1635  CB  VAL A 208      12.042  40.146  13.565  1.00 30.75           C  
ATOM   1636  CG1 VAL A 208      13.100  39.070  13.189  1.00 33.45           C  
ATOM   1637  CG2 VAL A 208      10.886  39.514  14.310  1.00 23.56           C  
ATOM   1638  N   ARG A 209      14.892  41.844  13.594  1.00 29.80           N  
ATOM   1639  CA  ARG A 209      15.810  42.580  12.746  1.00 32.35           C  
ATOM   1640  C   ARG A 209      16.993  41.693  12.424  1.00 32.19           C  
ATOM   1641  O   ARG A 209      17.064  40.549  12.880  1.00 33.44           O  
ATOM   1642  CB  ARG A 209      16.283  43.874  13.425  1.00 30.06           C  
ATOM   1643  CG  ARG A 209      16.855  43.701  14.806  1.00 31.45           C  
ATOM   1644  CD  ARG A 209      17.383  45.031  15.356  1.00 33.18           C  
ATOM   1645  NE  ARG A 209      18.097  44.839  16.615  1.00 30.22           N  
ATOM   1646  CZ  ARG A 209      17.519  44.821  17.809  1.00 33.90           C  
ATOM   1647  NH1 ARG A 209      16.207  44.998  17.921  1.00 39.21           N  
ATOM   1648  NH2 ARG A 209      18.251  44.592  18.896  1.00 39.52           N  
ATOM   1649  N   LYS A 210      17.912  42.217  11.624  1.00 30.28           N  
ATOM   1650  CA  LYS A 210      19.085  41.460  11.242  1.00 35.83           C  
ATOM   1651  C   LYS A 210      20.237  41.810  12.171  1.00 35.50           C  
ATOM   1652  O   LYS A 210      20.384  42.959  12.593  1.00 35.19           O  
ATOM   1653  CB  LYS A 210      19.446  41.760   9.781  1.00 38.39           C  
ATOM   1654  CG  LYS A 210      20.544  40.866   9.210  1.00 52.11           C  
ATOM   1655  CD  LYS A 210      20.706  41.065   7.699  1.00 55.15           C  
ATOM   1656  CE  LYS A 210      21.908  40.307   7.147  1.00 54.31           C  
ATOM   1657  NZ  LYS A 210      23.188  40.808   7.745  1.00 60.07           N  
ATOM   1658  N   GLY A 211      21.036  40.805  12.515  1.00 33.85           N  
ATOM   1659  CA  GLY A 211      22.171  41.030  13.388  1.00 33.15           C  
ATOM   1660  C   GLY A 211      23.372  40.215  12.952  1.00 31.06           C  
ATOM   1661  O   GLY A 211      23.446  39.774  11.809  1.00 31.14           O  
ATOM   1662  N   GLU A 212      24.305  40.012  13.876  1.00 35.03           N  
ATOM   1663  CA  GLU A 212      25.521  39.243  13.619  1.00 40.60           C  
ATOM   1664  C   GLU A 212      25.257  37.743  13.705  1.00 38.71           C  
ATOM   1665  O   GLU A 212      25.868  36.948  12.991  1.00 42.80           O  
ATOM   1666  CB  GLU A 212      26.588  39.603  14.654  1.00 44.41           C  
ATOM   1667  CG  GLU A 212      26.943  41.069  14.696  1.00 48.88           C  
ATOM   1668  CD  GLU A 212      27.738  41.492  13.487  1.00 59.20           C  
ATOM   1669  OE1 GLU A 212      27.245  41.305  12.351  1.00 60.68           O  
ATOM   1670  OE2 GLU A 212      28.862  42.012  13.673  1.00 68.17           O  
ATOM   1671  N   GLU A 213      24.344  37.364  14.587  1.00 34.91           N  
ATOM   1672  CA  GLU A 213      24.032  35.960  14.801  1.00 31.16           C  
ATOM   1673  C   GLU A 213      22.607  35.838  15.303  1.00 34.26           C  
ATOM   1674  O   GLU A 213      21.964  36.848  15.611  1.00 32.75           O  
ATOM   1675  CB  GLU A 213      24.974  35.394  15.858  1.00 27.95           C  
ATOM   1676  CG  GLU A 213      24.745  36.004  17.233  1.00 35.65           C  
ATOM   1677  CD  GLU A 213      25.582  35.358  18.316  1.00 41.05           C  
ATOM   1678  OE1 GLU A 213      25.621  34.111  18.379  1.00 51.11           O  
ATOM   1679  OE2 GLU A 213      26.194  36.100  19.110  1.00 54.13           O  
ATOM   1680  N   PHE A 214      22.125  34.601  15.401  1.00 30.86           N  
ATOM   1681  CA  PHE A 214      20.778  34.354  15.883  1.00 29.36           C  
ATOM   1682  C   PHE A 214      20.761  34.783  17.333  1.00 30.45           C  
ATOM   1683  O   PHE A 214      21.442  34.204  18.190  1.00 29.88           O  
ATOM   1684  CB  PHE A 214      20.397  32.880  15.770  1.00 26.43           C  
ATOM   1685  CG  PHE A 214      18.959  32.628  16.066  1.00 24.47           C  
ATOM   1686  CD1 PHE A 214      17.975  32.933  15.116  1.00 24.15           C  
ATOM   1687  CD2 PHE A 214      18.567  32.151  17.310  1.00 26.91           C  
ATOM   1688  CE1 PHE A 214      16.621  32.762  15.412  1.00 21.52           C  
ATOM   1689  CE2 PHE A 214      17.210  31.977  17.617  1.00 25.51           C  
ATOM   1690  CZ  PHE A 214      16.237  32.285  16.663  1.00 23.90           C  
ATOM   1691  N   PHE A 215      19.947  35.788  17.614  1.00 27.38           N  
ATOM   1692  CA  PHE A 215      19.911  36.364  18.942  1.00 27.25           C  
ATOM   1693  C   PHE A 215      18.486  36.606  19.404  1.00 24.94           C  
ATOM   1694  O   PHE A 215      17.697  37.225  18.694  1.00 26.31           O  
ATOM   1695  CB  PHE A 215      20.674  37.687  18.860  1.00 23.52           C  
ATOM   1696  CG  PHE A 215      21.204  38.188  20.160  1.00 23.72           C  
ATOM   1697  CD1 PHE A 215      22.580  38.257  20.368  1.00 27.06           C  
ATOM   1698  CD2 PHE A 215      20.349  38.704  21.129  1.00 25.27           C  
ATOM   1699  CE1 PHE A 215      23.099  38.837  21.519  1.00 31.94           C  
ATOM   1700  CE2 PHE A 215      20.858  39.290  22.286  1.00 31.06           C  
ATOM   1701  CZ  PHE A 215      22.238  39.362  22.484  1.00 28.06           C  
ATOM   1702  N   VAL A 216      18.148  36.096  20.583  1.00 23.48           N  
ATOM   1703  CA  VAL A 216      16.825  36.316  21.153  1.00 22.88           C  
ATOM   1704  C   VAL A 216      17.091  37.173  22.390  1.00 26.02           C  
ATOM   1705  O   VAL A 216      17.615  36.702  23.409  1.00 25.90           O  
ATOM   1706  CB  VAL A 216      16.130  34.986  21.522  1.00 17.97           C  
ATOM   1707  CG1 VAL A 216      14.796  35.268  22.257  1.00 20.25           C  
ATOM   1708  CG2 VAL A 216      15.874  34.190  20.241  1.00 20.85           C  
ATOM   1709  N   VAL A 217      16.770  38.456  22.272  1.00 26.91           N  
ATOM   1710  CA  VAL A 217      17.022  39.399  23.351  1.00 25.71           C  
ATOM   1711  C   VAL A 217      16.181  39.146  24.596  1.00 26.15           C  
ATOM   1712  O   VAL A 217      14.958  39.117  24.538  1.00 29.44           O  
ATOM   1713  CB  VAL A 217      16.801  40.855  22.870  1.00 28.16           C  
ATOM   1714  CG1 VAL A 217      17.420  41.844  23.873  1.00 29.26           C  
ATOM   1715  CG2 VAL A 217      17.428  41.048  21.496  1.00 23.15           C  
ATOM   1716  N   ASP A 218      16.860  38.939  25.716  1.00 21.86           N  
ATOM   1717  CA  ASP A 218      16.215  38.712  26.993  1.00 25.83           C  
ATOM   1718  C   ASP A 218      15.524  40.033  27.351  1.00 26.19           C  
ATOM   1719  O   ASP A 218      16.167  41.083  27.384  1.00 28.58           O  
ATOM   1720  CB  ASP A 218      17.279  38.372  28.042  1.00 25.99           C  
ATOM   1721  CG  ASP A 218      16.685  37.947  29.369  1.00 30.55           C  
ATOM   1722  OD1 ASP A 218      17.472  37.518  30.239  1.00 39.31           O  
ATOM   1723  OD2 ASP A 218      15.449  38.034  29.550  1.00 30.89           O  
ATOM   1724  N   PRO A 219      14.210  40.002  27.591  1.00 28.15           N  
ATOM   1725  CA  PRO A 219      13.516  41.251  27.936  1.00 35.17           C  
ATOM   1726  C   PRO A 219      13.964  41.821  29.278  1.00 36.47           C  
ATOM   1727  O   PRO A 219      13.790  43.013  29.555  1.00 37.29           O  
ATOM   1728  CB  PRO A 219      12.038  40.848  27.915  1.00 30.35           C  
ATOM   1729  CG  PRO A 219      12.068  39.393  28.249  1.00 31.25           C  
ATOM   1730  CD  PRO A 219      13.258  38.884  27.467  1.00 26.21           C  
ATOM   1731  N   VAL A 220      14.558  40.964  30.101  1.00 38.22           N  
ATOM   1732  CA  VAL A 220      15.044  41.381  31.406  1.00 38.43           C  
ATOM   1733  C   VAL A 220      16.439  42.001  31.317  1.00 39.41           C  
ATOM   1734  O   VAL A 220      16.800  42.820  32.152  1.00 43.31           O  
ATOM   1735  CB  VAL A 220      15.076  40.189  32.401  1.00 38.20           C  
ATOM   1736  CG1 VAL A 220      15.524  40.662  33.761  1.00 39.03           C  
ATOM   1737  CG2 VAL A 220      13.701  39.566  32.505  1.00 30.74           C  
ATOM   1738  N   ASP A 221      17.219  41.615  30.308  1.00 39.26           N  
ATOM   1739  CA  ASP A 221      18.576  42.148  30.122  1.00 40.73           C  
ATOM   1740  C   ASP A 221      18.915  42.138  28.626  1.00 41.37           C  
ATOM   1741  O   ASP A 221      19.198  41.080  28.055  1.00 37.49           O  
ATOM   1742  CB  ASP A 221      19.592  41.289  30.890  1.00 40.77           C  
ATOM   1743  CG  ASP A 221      20.996  41.869  30.863  1.00 43.25           C  
ATOM   1744  OD1 ASP A 221      21.252  42.798  30.067  1.00 40.13           O  
ATOM   1745  OD2 ASP A 221      21.856  41.384  31.636  1.00 45.05           O  
ATOM   1746  N   GLU A 222      18.897  43.322  28.012  1.00 38.10           N  
ATOM   1747  CA  GLU A 222      19.158  43.489  26.582  1.00 41.65           C  
ATOM   1748  C   GLU A 222      20.436  42.891  26.022  1.00 40.14           C  
ATOM   1749  O   GLU A 222      20.488  42.529  24.852  1.00 40.53           O  
ATOM   1750  CB  GLU A 222      19.168  44.972  26.200  1.00 46.65           C  
ATOM   1751  CG  GLU A 222      17.853  45.710  26.326  1.00 61.23           C  
ATOM   1752  CD  GLU A 222      17.918  47.091  25.673  1.00 67.52           C  
ATOM   1753  OE1 GLU A 222      18.893  47.835  25.942  1.00 64.78           O  
ATOM   1754  OE2 GLU A 222      16.998  47.428  24.892  1.00 70.75           O  
ATOM   1755  N   LYS A 223      21.479  42.808  26.830  1.00 42.22           N  
ATOM   1756  CA  LYS A 223      22.735  42.288  26.315  1.00 45.33           C  
ATOM   1757  C   LYS A 223      22.853  40.768  26.343  1.00 43.64           C  
ATOM   1758  O   LYS A 223      23.864  40.206  25.916  1.00 43.22           O  
ATOM   1759  CB  LYS A 223      23.890  42.943  27.076  1.00 49.12           C  
ATOM   1760  CG  LYS A 223      23.888  44.469  26.935  1.00 50.46           C  
ATOM   1761  CD  LYS A 223      23.947  44.874  25.456  1.00 55.58           C  
ATOM   1762  CE  LYS A 223      23.742  46.372  25.260  1.00 60.47           C  
ATOM   1763  NZ  LYS A 223      24.690  47.197  26.079  1.00 60.08           N  
ATOM   1764  N   ARG A 224      21.798  40.107  26.806  1.00 36.85           N  
ATOM   1765  CA  ARG A 224      21.797  38.658  26.924  1.00 35.00           C  
ATOM   1766  C   ARG A 224      21.000  37.947  25.835  1.00 32.57           C  
ATOM   1767  O   ARG A 224      19.842  38.268  25.580  1.00 28.29           O  
ATOM   1768  CB  ARG A 224      21.268  38.289  28.305  1.00 35.84           C  
ATOM   1769  CG  ARG A 224      21.269  36.812  28.651  1.00 49.32           C  
ATOM   1770  CD  ARG A 224      21.485  36.679  30.155  1.00 53.43           C  
ATOM   1771  NE  ARG A 224      20.903  35.478  30.741  1.00 56.91           N  
ATOM   1772  CZ  ARG A 224      21.145  34.237  30.333  1.00 60.19           C  
ATOM   1773  NH1 ARG A 224      21.963  34.013  29.311  1.00 66.17           N  
ATOM   1774  NH2 ARG A 224      20.589  33.215  30.973  1.00 54.12           N  
ATOM   1775  N   ASN A 225      21.642  36.974  25.198  1.00 28.86           N  
ATOM   1776  CA  ASN A 225      21.025  36.187  24.133  1.00 27.32           C  
ATOM   1777  C   ASN A 225      20.426  34.949  24.784  1.00 30.90           C  
ATOM   1778  O   ASN A 225      21.158  34.044  25.197  1.00 30.34           O  
ATOM   1779  CB  ASN A 225      22.096  35.792  23.105  1.00 22.85           C  
ATOM   1780  CG  ASN A 225      21.548  34.951  21.950  1.00 27.83           C  
ATOM   1781  OD1 ASN A 225      22.287  34.615  21.018  1.00 32.90           O  
ATOM   1782  ND2 ASN A 225      20.270  34.605  22.005  1.00 23.51           N  
ATOM   1783  N   VAL A 226      19.101  34.907  24.886  1.00 27.30           N  
ATOM   1784  CA  VAL A 226      18.429  33.765  25.499  1.00 27.69           C  
ATOM   1785  C   VAL A 226      18.707  32.456  24.731  1.00 25.07           C  
ATOM   1786  O   VAL A 226      18.598  31.361  25.285  1.00 24.43           O  
ATOM   1787  CB  VAL A 226      16.899  34.004  25.590  1.00 26.80           C  
ATOM   1788  CG1 VAL A 226      16.219  32.799  26.206  1.00 27.34           C  
ATOM   1789  CG2 VAL A 226      16.614  35.255  26.428  1.00 23.63           C  
ATOM   1790  N   ALA A 227      19.077  32.577  23.463  1.00 24.64           N  
ATOM   1791  CA  ALA A 227      19.367  31.395  22.643  1.00 26.89           C  
ATOM   1792  C   ALA A 227      20.875  31.180  22.501  1.00 26.41           C  
ATOM   1793  O   ALA A 227      21.335  30.529  21.552  1.00 24.96           O  
ATOM   1794  CB  ALA A 227      18.717  31.548  21.247  1.00 17.90           C  
ATOM   1795  N   ALA A 228      21.642  31.738  23.439  1.00 26.55           N  
ATOM   1796  CA  ALA A 228      23.095  31.621  23.408  1.00 27.54           C  
ATOM   1797  C   ALA A 228      23.583  30.194  23.136  1.00 22.56           C  
ATOM   1798  O   ALA A 228      24.509  30.002  22.355  1.00 27.32           O  
ATOM   1799  CB  ALA A 228      23.692  32.132  24.731  1.00 26.41           C  
ATOM   1800  N   ASN A 229      22.963  29.199  23.767  1.00 24.05           N  
ATOM   1801  CA  ASN A 229      23.387  27.806  23.594  1.00 27.29           C  
ATOM   1802  C   ASN A 229      22.747  27.024  22.442  1.00 28.97           C  
ATOM   1803  O   ASN A 229      23.085  25.859  22.229  1.00 24.91           O  
ATOM   1804  CB  ASN A 229      23.172  27.017  24.890  1.00 28.67           C  
ATOM   1805  CG  ASN A 229      23.860  27.651  26.083  1.00 40.98           C  
ATOM   1806  OD1 ASN A 229      24.578  28.653  25.954  1.00 38.91           O  
ATOM   1807  ND2 ASN A 229      23.643  27.068  27.262  1.00 39.46           N  
ATOM   1808  N   LEU A 230      21.805  27.630  21.726  1.00 22.08           N  
ATOM   1809  CA  LEU A 230      21.199  26.951  20.589  1.00 23.88           C  
ATOM   1810  C   LEU A 230      22.263  26.936  19.499  1.00 28.26           C  
ATOM   1811  O   LEU A 230      22.682  27.992  19.024  1.00 25.40           O  
ATOM   1812  CB  LEU A 230      19.982  27.721  20.076  1.00 25.13           C  
ATOM   1813  CG  LEU A 230      19.409  27.209  18.750  1.00 20.68           C  
ATOM   1814  CD1 LEU A 230      18.933  25.770  18.926  1.00 20.50           C  
ATOM   1815  CD2 LEU A 230      18.248  28.098  18.304  1.00 21.59           C  
ATOM   1816  N   SER A 231      22.706  25.751  19.093  1.00 25.81           N  
ATOM   1817  CA  SER A 231      23.732  25.682  18.058  1.00 25.22           C  
ATOM   1818  C   SER A 231      23.167  26.108  16.707  1.00 25.12           C  
ATOM   1819  O   SER A 231      21.960  26.015  16.476  1.00 25.16           O  
ATOM   1820  CB  SER A 231      24.274  24.264  17.929  1.00 23.41           C  
ATOM   1821  OG  SER A 231      23.300  23.420  17.347  1.00 23.34           O  
ATOM   1822  N   LEU A 232      24.056  26.556  15.821  1.00 22.16           N  
ATOM   1823  CA  LEU A 232      23.672  26.962  14.480  1.00 26.49           C  
ATOM   1824  C   LEU A 232      22.931  25.819  13.798  1.00 25.73           C  
ATOM   1825  O   LEU A 232      21.902  26.016  13.168  1.00 25.97           O  
ATOM   1826  CB  LEU A 232      24.915  27.327  13.651  1.00 28.57           C  
ATOM   1827  CG  LEU A 232      24.755  27.497  12.122  1.00 32.90           C  
ATOM   1828  CD1 LEU A 232      23.764  28.648  11.800  1.00 27.98           C  
ATOM   1829  CD2 LEU A 232      26.121  27.812  11.504  1.00 26.15           C  
ATOM   1830  N   ASP A 233      23.451  24.610  13.943  1.00 25.63           N  
ATOM   1831  CA  ASP A 233      22.834  23.467  13.293  1.00 23.93           C  
ATOM   1832  C   ASP A 233      21.476  23.059  13.833  1.00 23.40           C  
ATOM   1833  O   ASP A 233      20.652  22.558  13.074  1.00 22.74           O  
ATOM   1834  CB  ASP A 233      23.816  22.297  13.294  1.00 23.68           C  
ATOM   1835  CG  ASP A 233      24.972  22.536  12.339  1.00 29.84           C  
ATOM   1836  OD1 ASP A 233      26.029  21.875  12.464  1.00 29.18           O  
ATOM   1837  OD2 ASP A 233      24.806  23.405  11.448  1.00 29.34           O  
ATOM   1838  N   ASN A 234      21.229  23.261  15.126  1.00 20.38           N  
ATOM   1839  CA  ASN A 234      19.918  22.916  15.667  1.00 20.73           C  
ATOM   1840  C   ASN A 234      18.889  23.995  15.295  1.00 24.82           C  
ATOM   1841  O   ASN A 234      17.704  23.709  15.188  1.00 21.98           O  
ATOM   1842  CB  ASN A 234      20.000  22.680  17.180  1.00 19.20           C  
ATOM   1843  CG  ASN A 234      20.614  21.313  17.503  1.00 21.50           C  
ATOM   1844  OD1 ASN A 234      20.576  20.410  16.666  1.00 18.60           O  
ATOM   1845  ND2 ASN A 234      21.173  21.161  18.702  1.00 21.46           N  
ATOM   1846  N   LEU A 235      19.364  25.225  15.104  1.00 21.99           N  
ATOM   1847  CA  LEU A 235      18.516  26.322  14.652  1.00 24.36           C  
ATOM   1848  C   LEU A 235      18.114  25.905  13.237  1.00 22.99           C  
ATOM   1849  O   LEU A 235      16.931  25.935  12.876  1.00 22.44           O  
ATOM   1850  CB  LEU A 235      19.316  27.631  14.572  1.00 22.64           C  
ATOM   1851  CG  LEU A 235      18.706  28.713  13.670  1.00 23.28           C  
ATOM   1852  CD1 LEU A 235      17.366  29.170  14.225  1.00 23.98           C  
ATOM   1853  CD2 LEU A 235      19.675  29.882  13.549  1.00 19.95           C  
ATOM   1854  N   ALA A 236      19.109  25.499  12.441  1.00 24.57           N  
ATOM   1855  CA  ALA A 236      18.845  25.064  11.065  1.00 24.61           C  
ATOM   1856  C   ALA A 236      17.856  23.913  11.037  1.00 25.62           C  
ATOM   1857  O   ALA A 236      16.893  23.928  10.247  1.00 23.62           O  
ATOM   1858  CB  ALA A 236      20.152  24.645  10.359  1.00 24.31           C  
ATOM   1859  N   ARG A 237      18.079  22.919  11.896  1.00 20.17           N  
ATOM   1860  CA  ARG A 237      17.177  21.763  11.954  1.00 22.42           C  
ATOM   1861  C   ARG A 237      15.753  22.198  12.324  1.00 23.84           C  
ATOM   1862  O   ARG A 237      14.783  21.710  11.746  1.00 21.98           O  
ATOM   1863  CB  ARG A 237      17.687  20.722  12.964  1.00 27.60           C  
ATOM   1864  CG  ARG A 237      19.049  20.162  12.579  1.00 25.21           C  
ATOM   1865  CD  ARG A 237      19.521  18.981  13.448  1.00 31.32           C  
ATOM   1866  NE  ARG A 237      20.786  18.482  12.913  1.00 28.51           N  
ATOM   1867  CZ  ARG A 237      21.989  18.786  13.392  1.00 27.65           C  
ATOM   1868  NH1 ARG A 237      22.115  19.577  14.445  1.00 28.65           N  
ATOM   1869  NH2 ARG A 237      23.080  18.335  12.781  1.00 30.45           N  
ATOM   1870  N   PHE A 238      15.626  23.118  13.278  1.00 21.96           N  
ATOM   1871  CA  PHE A 238      14.301  23.584  13.674  1.00 22.05           C  
ATOM   1872  C   PHE A 238      13.591  24.295  12.510  1.00 20.41           C  
ATOM   1873  O   PHE A 238      12.411  24.065  12.271  1.00 22.25           O  
ATOM   1874  CB  PHE A 238      14.393  24.535  14.869  1.00 20.21           C  
ATOM   1875  CG  PHE A 238      13.055  25.047  15.335  1.00 24.34           C  
ATOM   1876  CD1 PHE A 238      12.106  24.173  15.847  1.00 21.76           C  
ATOM   1877  CD2 PHE A 238      12.730  26.402  15.232  1.00 27.61           C  
ATOM   1878  CE1 PHE A 238      10.853  24.631  16.250  1.00 26.57           C  
ATOM   1879  CE2 PHE A 238      11.479  26.864  15.631  1.00 22.88           C  
ATOM   1880  CZ  PHE A 238      10.542  25.973  16.142  1.00 27.19           C  
ATOM   1881  N   VAL A 239      14.315  25.164  11.805  1.00 22.98           N  
ATOM   1882  CA  VAL A 239      13.741  25.900  10.684  1.00 22.21           C  
ATOM   1883  C   VAL A 239      13.237  24.925   9.624  1.00 24.63           C  
ATOM   1884  O   VAL A 239      12.144  25.101   9.075  1.00 23.15           O  
ATOM   1885  CB  VAL A 239      14.776  26.873  10.079  1.00 23.40           C  
ATOM   1886  CG1 VAL A 239      14.272  27.441   8.759  1.00 24.18           C  
ATOM   1887  CG2 VAL A 239      15.044  28.003  11.053  1.00 24.63           C  
ATOM   1888  N   HIS A 240      14.020  23.881   9.365  1.00 21.45           N  
ATOM   1889  CA  HIS A 240      13.654  22.873   8.380  1.00 23.97           C  
ATOM   1890  C   HIS A 240      12.425  22.108   8.857  1.00 24.34           C  
ATOM   1891  O   HIS A 240      11.460  21.942   8.104  1.00 25.62           O  
ATOM   1892  CB  HIS A 240      14.822  21.897   8.139  1.00 24.41           C  
ATOM   1893  CG  HIS A 240      14.546  20.889   7.072  1.00 25.39           C  
ATOM   1894  ND1 HIS A 240      14.385  21.236   5.749  1.00 27.77           N  
ATOM   1895  CD2 HIS A 240      14.354  19.552   7.140  1.00 28.05           C  
ATOM   1896  CE1 HIS A 240      14.103  20.154   5.046  1.00 29.89           C  
ATOM   1897  NE2 HIS A 240      14.078  19.119   5.866  1.00 29.97           N  
ATOM   1898  N   LEU A 241      12.458  21.629  10.103  1.00 26.31           N  
ATOM   1899  CA  LEU A 241      11.320  20.903  10.673  1.00 24.68           C  
ATOM   1900  C   LEU A 241      10.047  21.749  10.588  1.00 25.74           C  
ATOM   1901  O   LEU A 241       8.959  21.238  10.333  1.00 24.00           O  
ATOM   1902  CB  LEU A 241      11.583  20.566  12.146  1.00 27.12           C  
ATOM   1903  CG  LEU A 241      12.622  19.486  12.434  1.00 34.40           C  
ATOM   1904  CD1 LEU A 241      12.912  19.450  13.928  1.00 38.87           C  
ATOM   1905  CD2 LEU A 241      12.104  18.136  11.953  1.00 29.89           C  
ATOM   1906  N   CYS A 242      10.181  23.046  10.833  1.00 23.45           N  
ATOM   1907  CA  CYS A 242       9.019  23.911  10.771  1.00 25.79           C  
ATOM   1908  C   CYS A 242       8.461  23.940   9.361  1.00 25.60           C  
ATOM   1909  O   CYS A 242       7.249  23.847   9.185  1.00 27.26           O  
ATOM   1910  CB  CYS A 242       9.365  25.327  11.249  1.00 24.75           C  
ATOM   1911  SG  CYS A 242       9.501  25.430  13.062  1.00 28.81           S  
ATOM   1912  N   ARG A 243       9.349  24.055   8.372  1.00 26.52           N  
ATOM   1913  CA  ARG A 243       8.959  24.079   6.969  1.00 28.89           C  
ATOM   1914  C   ARG A 243       8.282  22.761   6.593  1.00 32.52           C  
ATOM   1915  O   ARG A 243       7.246  22.749   5.911  1.00 28.73           O  
ATOM   1916  CB  ARG A 243      10.185  24.293   6.076  1.00 25.32           C  
ATOM   1917  CG  ARG A 243      10.730  25.704   6.079  1.00 22.46           C  
ATOM   1918  CD  ARG A 243      12.034  25.804   5.335  1.00 23.06           C  
ATOM   1919  NE  ARG A 243      12.579  27.148   5.433  1.00 21.64           N  
ATOM   1920  CZ  ARG A 243      13.812  27.494   5.084  1.00 27.35           C  
ATOM   1921  NH1 ARG A 243      14.664  26.589   4.603  1.00 24.66           N  
ATOM   1922  NH2 ARG A 243      14.197  28.754   5.227  1.00 27.11           N  
ATOM   1923  N   GLU A 244       8.874  21.653   7.040  1.00 25.83           N  
ATOM   1924  CA  GLU A 244       8.333  20.327   6.754  1.00 30.87           C  
ATOM   1925  C   GLU A 244       6.986  20.098   7.421  1.00 31.16           C  
ATOM   1926  O   GLU A 244       6.091  19.496   6.817  1.00 30.08           O  
ATOM   1927  CB  GLU A 244       9.320  19.236   7.189  1.00 29.21           C  
ATOM   1928  CG  GLU A 244      10.539  19.120   6.284  1.00 36.33           C  
ATOM   1929  CD  GLU A 244      10.180  18.700   4.860  1.00 43.23           C  
ATOM   1930  OE1 GLU A 244       9.561  17.630   4.693  1.00 48.65           O  
ATOM   1931  OE2 GLU A 244      10.515  19.437   3.906  1.00 49.65           O  
ATOM   1932  N   PHE A 245       6.838  20.567   8.661  1.00 27.98           N  
ATOM   1933  CA  PHE A 245       5.577  20.400   9.372  1.00 27.98           C  
ATOM   1934  C   PHE A 245       4.436  21.146   8.684  1.00 29.47           C  
ATOM   1935  O   PHE A 245       3.347  20.610   8.530  1.00 31.72           O  
ATOM   1936  CB  PHE A 245       5.658  20.906  10.810  1.00 25.13           C  
ATOM   1937  CG  PHE A 245       4.380  20.704  11.582  1.00 27.43           C  
ATOM   1938  CD1 PHE A 245       4.050  19.447  12.090  1.00 24.22           C  
ATOM   1939  CD2 PHE A 245       3.480  21.756  11.760  1.00 28.09           C  
ATOM   1940  CE1 PHE A 245       2.839  19.241  12.755  1.00 26.04           C  
ATOM   1941  CE2 PHE A 245       2.264  21.559  12.426  1.00 32.01           C  
ATOM   1942  CZ  PHE A 245       1.946  20.293  12.925  1.00 28.13           C  
ATOM   1943  N   MET A 246       4.674  22.395   8.304  1.00 29.13           N  
ATOM   1944  CA  MET A 246       3.632  23.168   7.640  1.00 31.19           C  
ATOM   1945  C   MET A 246       3.294  22.560   6.269  1.00 33.09           C  
ATOM   1946  O   MET A 246       2.149  22.610   5.821  1.00 33.19           O  
ATOM   1947  CB  MET A 246       4.073  24.625   7.479  1.00 30.45           C  
ATOM   1948  CG  MET A 246       4.171  25.399   8.798  1.00 27.24           C  
ATOM   1949  SD  MET A 246       2.662  25.297   9.769  1.00 33.32           S  
ATOM   1950  CE  MET A 246       1.512  26.214   8.700  1.00 29.39           C  
ATOM   1951  N   GLU A 247       4.292  21.975   5.616  1.00 34.20           N  
ATOM   1952  CA  GLU A 247       4.096  21.359   4.305  1.00 40.26           C  
ATOM   1953  C   GLU A 247       3.205  20.118   4.412  1.00 41.66           C  
ATOM   1954  O   GLU A 247       2.362  19.875   3.555  1.00 39.41           O  
ATOM   1955  CB  GLU A 247       5.450  20.970   3.706  1.00 42.52           C  
ATOM   1956  CG  GLU A 247       5.399  20.424   2.296  1.00 52.62           C  
ATOM   1957  CD  GLU A 247       5.162  21.507   1.270  1.00 57.55           C  
ATOM   1958  OE1 GLU A 247       5.960  22.468   1.228  1.00 67.07           O  
ATOM   1959  OE2 GLU A 247       4.183  21.401   0.501  1.00 60.64           O  
ATOM   1960  N   ALA A 248       3.398  19.332   5.469  1.00 41.90           N  
ATOM   1961  CA  ALA A 248       2.609  18.120   5.670  1.00 38.68           C  
ATOM   1962  C   ALA A 248       2.559  17.781   7.148  1.00 39.32           C  
ATOM   1963  O   ALA A 248       3.303  16.918   7.625  1.00 41.84           O  
ATOM   1964  CB  ALA A 248       3.219  16.963   4.890  1.00 34.21           C  
ATOM   1965  N   PRO A 249       1.683  18.464   7.900  1.00 39.53           N  
ATOM   1966  CA  PRO A 249       1.556  18.218   9.336  1.00 41.56           C  
ATOM   1967  C   PRO A 249       1.233  16.766   9.674  1.00 45.27           C  
ATOM   1968  O   PRO A 249       0.374  16.130   9.051  1.00 43.51           O  
ATOM   1969  CB  PRO A 249       0.466  19.204   9.769  1.00 40.78           C  
ATOM   1970  CG  PRO A 249      -0.296  19.473   8.518  1.00 39.07           C  
ATOM   1971  CD  PRO A 249       0.750  19.513   7.455  1.00 36.25           C  
ATOM   1972  N   SER A 250       1.935  16.252  10.674  1.00 40.02           N  
ATOM   1973  CA  SER A 250       1.770  14.874  11.097  1.00 38.59           C  
ATOM   1974  C   SER A 250       2.004  14.809  12.599  1.00 36.20           C  
ATOM   1975  O   SER A 250       2.827  15.548  13.127  1.00 38.36           O  
ATOM   1976  CB  SER A 250       2.791  14.002  10.358  1.00 34.42           C  
ATOM   1977  OG  SER A 250       2.740  12.657  10.789  1.00 46.88           O  
ATOM   1978  N   LEU A 251       1.279  13.933  13.287  1.00 34.15           N  
ATOM   1979  CA  LEU A 251       1.441  13.797  14.729  1.00 35.22           C  
ATOM   1980  C   LEU A 251       2.844  13.259  14.991  1.00 36.25           C  
ATOM   1981  O   LEU A 251       3.381  13.388  16.091  1.00 35.32           O  
ATOM   1982  CB  LEU A 251       0.389  12.832  15.291  1.00 35.61           C  
ATOM   1983  CG  LEU A 251       0.330  12.650  16.814  1.00 45.14           C  
ATOM   1984  CD1 LEU A 251       0.133  13.996  17.489  1.00 34.56           C  
ATOM   1985  CD2 LEU A 251      -0.810  11.705  17.180  1.00 46.05           C  
ATOM   1986  N   GLY A 252       3.429  12.667  13.955  1.00 33.99           N  
ATOM   1987  CA  GLY A 252       4.764  12.106  14.053  1.00 36.85           C  
ATOM   1988  C   GLY A 252       5.831  13.111  14.448  1.00 37.12           C  
ATOM   1989  O   GLY A 252       6.868  12.731  14.992  1.00 34.28           O  
ATOM   1990  N   PHE A 253       5.599  14.391  14.178  1.00 35.54           N  
ATOM   1991  CA  PHE A 253       6.584  15.400  14.553  1.00 36.56           C  
ATOM   1992  C   PHE A 253       6.640  15.538  16.067  1.00 36.72           C  
ATOM   1993  O   PHE A 253       7.593  16.094  16.611  1.00 38.07           O  
ATOM   1994  CB  PHE A 253       6.246  16.763  13.952  1.00 33.26           C  
ATOM   1995  CG  PHE A 253       6.509  16.860  12.485  1.00 33.61           C  
ATOM   1996  CD1 PHE A 253       5.607  16.339  11.566  1.00 29.57           C  
ATOM   1997  CD2 PHE A 253       7.667  17.479  12.018  1.00 29.95           C  
ATOM   1998  CE1 PHE A 253       5.851  16.432  10.200  1.00 31.17           C  
ATOM   1999  CE2 PHE A 253       7.922  17.578  10.661  1.00 30.89           C  
ATOM   2000  CZ  PHE A 253       7.012  17.053   9.745  1.00 34.14           C  
ATOM   2001  N   PHE A 254       5.617  15.039  16.751  1.00 37.13           N  
ATOM   2002  CA  PHE A 254       5.587  15.140  18.203  1.00 35.83           C  
ATOM   2003  C   PHE A 254       5.991  13.836  18.856  1.00 33.42           C  
ATOM   2004  O   PHE A 254       6.038  13.739  20.079  1.00 33.82           O  
ATOM   2005  CB  PHE A 254       4.195  15.537  18.704  1.00 32.57           C  
ATOM   2006  CG  PHE A 254       3.778  16.917  18.300  1.00 34.49           C  
ATOM   2007  CD1 PHE A 254       3.195  17.144  17.059  1.00 35.73           C  
ATOM   2008  CD2 PHE A 254       4.007  17.997  19.144  1.00 33.36           C  
ATOM   2009  CE1 PHE A 254       2.847  18.434  16.662  1.00 31.35           C  
ATOM   2010  CE2 PHE A 254       3.664  19.294  18.757  1.00 31.09           C  
ATOM   2011  CZ  PHE A 254       3.083  19.510  17.512  1.00 31.23           C  
ATOM   2012  N   LYS A 255       6.288  12.842  18.035  1.00 34.42           N  
ATOM   2013  CA  LYS A 255       6.672  11.536  18.541  1.00 40.67           C  
ATOM   2014  C   LYS A 255       8.159  11.263  18.362  1.00 39.80           C  
ATOM   2015  O   LYS A 255       8.728  11.534  17.310  1.00 40.37           O  
ATOM   2016  CB  LYS A 255       5.865  10.448  17.831  1.00 38.08           C  
ATOM   2017  CG  LYS A 255       4.365  10.550  18.051  1.00 49.81           C  
ATOM   2018  CD  LYS A 255       3.642   9.425  17.339  1.00 54.51           C  
ATOM   2019  CE  LYS A 255       2.159   9.412  17.656  1.00 57.51           C  
ATOM   2020  NZ  LYS A 255       1.454   8.416  16.800  1.00 56.71           N  
ATOM   2021  N   PRO A 256       8.812  10.733  19.402  1.00 47.94           N  
ATOM   2022  CA  PRO A 256      10.242  10.434  19.310  1.00 52.60           C  
ATOM   2023  C   PRO A 256      10.478   9.417  18.204  1.00 56.14           C  
ATOM   2024  O   PRO A 256       9.677   8.502  18.012  1.00 60.32           O  
ATOM   2025  CB  PRO A 256      10.566   9.870  20.691  1.00 55.20           C  
ATOM   2026  CG  PRO A 256       9.604  10.598  21.580  1.00 52.92           C  
ATOM   2027  CD  PRO A 256       8.324  10.544  20.780  1.00 51.34           C  
ATOM   2028  N   LYS A 257      11.568   9.585  17.470  1.00 56.66           N  
ATOM   2029  CA  LYS A 257      11.892   8.671  16.389  1.00 63.69           C  
ATOM   2030  C   LYS A 257      12.409   7.379  17.013  1.00 64.23           C  
ATOM   2031  O   LYS A 257      12.931   7.392  18.125  1.00 59.67           O  
ATOM   2032  CB  LYS A 257      12.940   9.318  15.483  1.00 66.24           C  
ATOM   2033  CG  LYS A 257      12.583  10.769  15.164  1.00 75.63           C  
ATOM   2034  CD  LYS A 257      13.401  11.374  14.035  1.00 79.63           C  
ATOM   2035  CE  LYS A 257      12.977  12.821  13.805  1.00 78.51           C  
ATOM   2036  NZ  LYS A 257      13.555  13.401  12.567  1.00 81.83           N  
ATOM   2037  N   HIS A 258      12.251   6.258  16.319  1.00 69.12           N  
ATOM   2038  CA  HIS A 258      12.716   4.999  16.881  1.00 72.95           C  
ATOM   2039  C   HIS A 258      14.092   4.531  16.447  1.00 71.90           C  
ATOM   2040  O   HIS A 258      14.423   4.521  15.262  1.00 73.05           O  
ATOM   2041  CB  HIS A 258      11.691   3.891  16.647  1.00 76.44           C  
ATOM   2042  CG  HIS A 258      10.681   3.783  17.744  1.00 81.52           C  
ATOM   2043  ND1 HIS A 258       9.732   2.784  17.795  1.00 80.40           N  
ATOM   2044  CD2 HIS A 258      10.478   4.548  18.843  1.00 82.31           C  
ATOM   2045  CE1 HIS A 258       8.990   2.939  18.875  1.00 81.71           C  
ATOM   2046  NE2 HIS A 258       9.422   4.003  19.530  1.00 84.48           N  
ATOM   2047  N   PRO A 259      14.913   4.131  17.429  1.00 72.76           N  
ATOM   2048  CA  PRO A 259      16.283   3.639  17.270  1.00 73.64           C  
ATOM   2049  C   PRO A 259      16.377   2.615  16.153  1.00 71.78           C  
ATOM   2050  O   PRO A 259      15.745   1.562  16.217  1.00 73.67           O  
ATOM   2051  CB  PRO A 259      16.584   3.027  18.634  1.00 74.25           C  
ATOM   2052  CG  PRO A 259      15.817   3.913  19.557  1.00 76.20           C  
ATOM   2053  CD  PRO A 259      14.498   4.054  18.840  1.00 73.59           C  
ATOM   2054  N   LEU A 260      17.161   2.929  15.129  1.00 68.76           N  
ATOM   2055  CA  LEU A 260      17.324   2.013  14.011  1.00 68.63           C  
ATOM   2056  C   LEU A 260      17.828   0.674  14.525  1.00 68.48           C  
ATOM   2057  O   LEU A 260      18.859   0.601  15.195  1.00 65.95           O  
ATOM   2058  CB  LEU A 260      18.321   2.572  12.994  1.00 68.12           C  
ATOM   2059  CG  LEU A 260      17.979   3.886  12.294  1.00 70.14           C  
ATOM   2060  CD1 LEU A 260      19.119   4.275  11.369  1.00 72.95           C  
ATOM   2061  CD2 LEU A 260      16.689   3.734  11.510  1.00 74.60           C  
ATOM   2062  N   GLU A 261      17.085  -0.383  14.224  1.00 69.35           N  
ATOM   2063  CA  GLU A 261      17.472  -1.723  14.638  1.00 70.54           C  
ATOM   2064  C   GLU A 261      18.258  -2.357  13.501  1.00 67.22           C  
ATOM   2065  O   GLU A 261      17.708  -2.668  12.444  1.00 66.57           O  
ATOM   2066  CB  GLU A 261      16.230  -2.551  14.968  1.00 72.60           C  
ATOM   2067  CG  GLU A 261      15.661  -2.247  16.342  1.00 75.88           C  
ATOM   2068  CD  GLU A 261      14.220  -2.692  16.496  1.00 78.41           C  
ATOM   2069  OE1 GLU A 261      13.758  -2.810  17.651  1.00 81.48           O  
ATOM   2070  OE2 GLU A 261      13.546  -2.908  15.466  1.00 76.15           O  
ATOM   2071  N   ILE A 262      19.555  -2.532  13.725  1.00 63.81           N  
ATOM   2072  CA  ILE A 262      20.431  -3.102  12.716  1.00 60.86           C  
ATOM   2073  C   ILE A 262      21.453  -4.043  13.338  1.00 56.77           C  
ATOM   2074  O   ILE A 262      22.067  -3.722  14.350  1.00 54.91           O  
ATOM   2075  CB  ILE A 262      21.165  -1.975  11.953  1.00 61.31           C  
ATOM   2076  CG1 ILE A 262      22.044  -2.562  10.849  1.00 63.94           C  
ATOM   2077  CG2 ILE A 262      21.986  -1.147  12.929  1.00 60.93           C  
ATOM   2078  CD1 ILE A 262      22.664  -1.512   9.948  1.00 57.19           C  
ATOM   2079  N   GLU A 263      21.622  -5.211  12.731  1.00 59.37           N  
ATOM   2080  CA  GLU A 263      22.578  -6.191  13.226  1.00 57.46           C  
ATOM   2081  C   GLU A 263      23.973  -5.728  12.836  1.00 53.54           C  
ATOM   2082  O   GLU A 263      24.133  -4.924  11.921  1.00 52.55           O  
ATOM   2083  CB  GLU A 263      22.332  -7.568  12.598  1.00 58.21           C  
ATOM   2084  CG  GLU A 263      20.907  -8.100  12.703  1.00 58.22           C  
ATOM   2085  CD  GLU A 263      20.811  -9.578  12.330  1.00 60.67           C  
ATOM   2086  OE1 GLU A 263      21.310  -9.969  11.252  1.00 59.50           O  
ATOM   2087  OE2 GLU A 263      20.232 -10.352  13.117  1.00 60.94           O  
ATOM   2088  N   PRO A 264      25.001  -6.227  13.533  1.00 50.47           N  
ATOM   2089  CA  PRO A 264      26.384  -5.855  13.234  1.00 48.20           C  
ATOM   2090  C   PRO A 264      26.769  -6.212  11.792  1.00 47.69           C  
ATOM   2091  O   PRO A 264      27.490  -5.462  11.131  1.00 40.15           O  
ATOM   2092  CB  PRO A 264      27.177  -6.656  14.259  1.00 49.88           C  
ATOM   2093  CG  PRO A 264      26.243  -6.682  15.434  1.00 48.75           C  
ATOM   2094  CD  PRO A 264      24.929  -7.004  14.783  1.00 51.08           C  
ATOM   2095  N   GLU A 265      26.284  -7.353  11.305  1.00 41.85           N  
ATOM   2096  CA  GLU A 265      26.599  -7.776   9.945  1.00 44.27           C  
ATOM   2097  C   GLU A 265      26.108  -6.766   8.907  1.00 37.12           C  
ATOM   2098  O   GLU A 265      26.778  -6.542   7.899  1.00 34.92           O  
ATOM   2099  CB  GLU A 265      26.003  -9.163   9.646  1.00 52.94           C  
ATOM   2100  CG  GLU A 265      26.575 -10.299  10.504  1.00 58.25           C  
ATOM   2101  CD  GLU A 265      26.094 -11.683  10.069  1.00 63.61           C  
ATOM   2102  OE1 GLU A 265      24.866 -11.875   9.907  1.00 64.10           O  
ATOM   2103  OE2 GLU A 265      26.948 -12.584   9.899  1.00 62.90           O  
ATOM   2104  N   ARG A 266      24.949  -6.157   9.148  1.00 35.62           N  
ATOM   2105  CA  ARG A 266      24.415  -5.178   8.203  1.00 38.91           C  
ATOM   2106  C   ARG A 266      25.183  -3.865   8.293  1.00 41.42           C  
ATOM   2107  O   ARG A 266      25.260  -3.112   7.327  1.00 43.65           O  
ATOM   2108  CB  ARG A 266      22.934  -4.904   8.458  1.00 39.46           C  
ATOM   2109  CG  ARG A 266      22.169  -4.571   7.179  1.00 50.78           C  
ATOM   2110  CD  ARG A 266      21.438  -3.229   7.248  1.00 57.50           C  
ATOM   2111  NE  ARG A 266      20.428  -3.203   8.302  1.00 59.63           N  
ATOM   2112  CZ  ARG A 266      19.565  -2.208   8.495  1.00 62.65           C  
ATOM   2113  NH1 ARG A 266      19.585  -1.140   7.698  1.00 57.08           N  
ATOM   2114  NH2 ARG A 266      18.682  -2.286   9.486  1.00 56.27           N  
ATOM   2115  N   LEU A 267      25.741  -3.588   9.464  1.00 38.62           N  
ATOM   2116  CA  LEU A 267      26.512  -2.372   9.652  1.00 34.41           C  
ATOM   2117  C   LEU A 267      27.835  -2.573   8.913  1.00 31.92           C  
ATOM   2118  O   LEU A 267      28.329  -1.671   8.232  1.00 28.58           O  
ATOM   2119  CB  LEU A 267      26.753  -2.144  11.144  1.00 38.91           C  
ATOM   2120  CG  LEU A 267      26.949  -0.705  11.615  1.00 48.87           C  
ATOM   2121  CD1 LEU A 267      25.928   0.218  10.963  1.00 46.55           C  
ATOM   2122  CD2 LEU A 267      26.807  -0.677  13.134  1.00 56.51           C  
ATOM   2123  N   ARG A 268      28.399  -3.771   9.042  1.00 30.30           N  
ATOM   2124  CA  ARG A 268      29.654  -4.088   8.373  1.00 31.97           C  
ATOM   2125  C   ARG A 268      29.448  -3.972   6.858  1.00 32.44           C  
ATOM   2126  O   ARG A 268      30.309  -3.468   6.137  1.00 27.09           O  
ATOM   2127  CB  ARG A 268      30.113  -5.509   8.738  1.00 35.40           C  
ATOM   2128  CG  ARG A 268      31.482  -5.858   8.186  1.00 36.66           C  
ATOM   2129  CD  ARG A 268      31.942  -7.249   8.608  1.00 48.05           C  
ATOM   2130  NE  ARG A 268      33.339  -7.469   8.244  1.00 54.44           N  
ATOM   2131  CZ  ARG A 268      34.017  -8.589   8.482  1.00 62.65           C  
ATOM   2132  NH1 ARG A 268      33.425  -9.612   9.090  1.00 62.66           N  
ATOM   2133  NH2 ARG A 268      35.292  -8.683   8.119  1.00 60.72           N  
ATOM   2134  N   LYS A 269      28.288  -4.426   6.394  1.00 30.62           N  
ATOM   2135  CA  LYS A 269      27.945  -4.385   4.977  1.00 29.27           C  
ATOM   2136  C   LYS A 269      27.866  -2.945   4.478  1.00 28.59           C  
ATOM   2137  O   LYS A 269      28.375  -2.608   3.416  1.00 29.83           O  
ATOM   2138  CB  LYS A 269      26.600  -5.079   4.763  1.00 29.25           C  
ATOM   2139  CG  LYS A 269      26.217  -5.267   3.312  1.00 29.79           C  
ATOM   2140  CD  LYS A 269      24.969  -6.137   3.207  1.00 43.74           C  
ATOM   2141  CE  LYS A 269      24.619  -6.405   1.761  1.00 45.34           C  
ATOM   2142  NZ  LYS A 269      24.505  -5.125   1.018  1.00 43.69           N  
ATOM   2143  N   ILE A 270      27.211  -2.097   5.254  1.00 29.70           N  
ATOM   2144  CA  ILE A 270      27.082  -0.689   4.895  1.00 30.34           C  
ATOM   2145  C   ILE A 270      28.462  -0.045   4.823  1.00 28.51           C  
ATOM   2146  O   ILE A 270      28.784   0.662   3.866  1.00 28.62           O  
ATOM   2147  CB  ILE A 270      26.237   0.050   5.934  1.00 27.42           C  
ATOM   2148  CG1 ILE A 270      24.803  -0.460   5.856  1.00 31.42           C  
ATOM   2149  CG2 ILE A 270      26.329   1.570   5.723  1.00 25.70           C  
ATOM   2150  CD1 ILE A 270      23.938   0.009   7.018  1.00 33.57           C  
ATOM   2151  N   VAL A 271      29.276  -0.291   5.842  1.00 24.12           N  
ATOM   2152  CA  VAL A 271      30.618   0.279   5.874  1.00 26.45           C  
ATOM   2153  C   VAL A 271      31.442  -0.225   4.686  1.00 28.80           C  
ATOM   2154  O   VAL A 271      32.028   0.569   3.965  1.00 23.89           O  
ATOM   2155  CB  VAL A 271      31.313  -0.059   7.196  1.00 27.52           C  
ATOM   2156  CG1 VAL A 271      32.760   0.429   7.181  1.00 26.24           C  
ATOM   2157  CG2 VAL A 271      30.541   0.578   8.341  1.00 22.05           C  
ATOM   2158  N   GLU A 272      31.463  -1.538   4.460  1.00 26.87           N  
ATOM   2159  CA  GLU A 272      32.221  -2.081   3.331  1.00 30.82           C  
ATOM   2160  C   GLU A 272      31.718  -1.546   1.985  1.00 27.73           C  
ATOM   2161  O   GLU A 272      32.495  -1.382   1.045  1.00 31.33           O  
ATOM   2162  CB  GLU A 272      32.193  -3.617   3.353  1.00 31.13           C  
ATOM   2163  CG  GLU A 272      33.199  -4.203   4.352  1.00 43.57           C  
ATOM   2164  CD  GLU A 272      33.094  -5.713   4.517  1.00 49.00           C  
ATOM   2165  OE1 GLU A 272      33.800  -6.263   5.389  1.00 56.29           O  
ATOM   2166  OE2 GLU A 272      32.311  -6.350   3.784  1.00 58.60           O  
ATOM   2167  N   GLU A 273      30.424  -1.259   1.906  1.00 28.56           N  
ATOM   2168  CA  GLU A 273      29.813  -0.720   0.688  1.00 34.37           C  
ATOM   2169  C   GLU A 273      30.221   0.756   0.476  1.00 30.41           C  
ATOM   2170  O   GLU A 273      30.390   1.224  -0.655  1.00 27.92           O  
ATOM   2171  CB  GLU A 273      28.297  -0.829   0.808  1.00 36.49           C  
ATOM   2172  CG  GLU A 273      27.568  -1.093  -0.474  1.00 51.68           C  
ATOM   2173  CD  GLU A 273      26.361  -2.004  -0.253  1.00 59.62           C  
ATOM   2174  OE1 GLU A 273      26.560  -3.214   0.009  1.00 58.76           O  
ATOM   2175  OE2 GLU A 273      25.216  -1.508  -0.328  1.00 63.46           O  
ATOM   2176  N   ARG A 274      30.351   1.488   1.575  1.00 25.54           N  
ATOM   2177  CA  ARG A 274      30.766   2.884   1.515  1.00 23.84           C  
ATOM   2178  C   ARG A 274      32.255   2.904   1.187  1.00 19.54           C  
ATOM   2179  O   ARG A 274      32.755   3.856   0.605  1.00 21.32           O  
ATOM   2180  CB  ARG A 274      30.487   3.567   2.859  1.00 23.83           C  
ATOM   2181  CG  ARG A 274      28.985   3.752   3.142  1.00 24.86           C  
ATOM   2182  CD  ARG A 274      28.704   4.187   4.591  1.00 22.31           C  
ATOM   2183  NE  ARG A 274      29.083   5.562   4.949  1.00 20.15           N  
ATOM   2184  CZ  ARG A 274      28.302   6.630   4.807  1.00 21.82           C  
ATOM   2185  NH1 ARG A 274      27.083   6.506   4.288  1.00 23.57           N  
ATOM   2186  NH2 ARG A 274      28.711   7.821   5.247  1.00 19.86           N  
ATOM   2187  N   GLY A 275      32.948   1.825   1.555  1.00 25.26           N  
ATOM   2188  CA  GLY A 275      34.377   1.694   1.292  1.00 23.57           C  
ATOM   2189  C   GLY A 275      35.257   2.629   2.115  1.00 23.12           C  
ATOM   2190  O   GLY A 275      36.367   2.981   1.728  1.00 22.84           O  
ATOM   2191  N   THR A 276      34.759   3.019   3.275  1.00 25.80           N  
ATOM   2192  CA  THR A 276      35.478   3.934   4.153  1.00 21.40           C  
ATOM   2193  C   THR A 276      36.134   3.230   5.329  1.00 23.20           C  
ATOM   2194  O   THR A 276      35.918   2.044   5.581  1.00 20.62           O  
ATOM   2195  CB  THR A 276      34.511   4.934   4.781  1.00 19.81           C  
ATOM   2196  OG1 THR A 276      33.446   4.204   5.412  1.00 19.11           O  
ATOM   2197  CG2 THR A 276      33.958   5.878   3.748  1.00 19.05           C  
ATOM   2198  N   ALA A 277      36.896   4.012   6.079  1.00 22.32           N  
ATOM   2199  CA  ALA A 277      37.533   3.528   7.283  1.00 20.10           C  
ATOM   2200  C   ALA A 277      36.645   4.061   8.396  1.00 22.23           C  
ATOM   2201  O   ALA A 277      36.484   5.278   8.545  1.00 25.31           O  
ATOM   2202  CB  ALA A 277      38.926   4.090   7.405  1.00 19.43           C  
ATOM   2203  N   VAL A 278      36.030   3.164   9.155  1.00 17.93           N  
ATOM   2204  CA  VAL A 278      35.170   3.593  10.245  1.00 23.78           C  
ATOM   2205  C   VAL A 278      35.786   3.055  11.522  1.00 22.48           C  
ATOM   2206  O   VAL A 278      36.097   1.865  11.622  1.00 25.64           O  
ATOM   2207  CB  VAL A 278      33.710   3.073  10.067  1.00 24.83           C  
ATOM   2208  CG1 VAL A 278      32.911   3.259  11.361  1.00 24.53           C  
ATOM   2209  CG2 VAL A 278      33.038   3.845   8.960  1.00 21.40           C  
ATOM   2210  N   PHE A 279      35.994   3.933  12.488  1.00 18.80           N  
ATOM   2211  CA  PHE A 279      36.616   3.505  13.732  1.00 19.04           C  
ATOM   2212  C   PHE A 279      36.298   4.453  14.889  1.00 22.29           C  
ATOM   2213  O   PHE A 279      35.699   5.534  14.696  1.00 20.64           O  
ATOM   2214  CB  PHE A 279      38.135   3.377  13.505  1.00 18.53           C  
ATOM   2215  CG  PHE A 279      38.818   4.690  13.176  1.00 23.43           C  
ATOM   2216  CD1 PHE A 279      39.321   5.496  14.190  1.00 19.45           C  
ATOM   2217  CD2 PHE A 279      38.957   5.108  11.850  1.00 15.88           C  
ATOM   2218  CE1 PHE A 279      39.968   6.706  13.889  1.00 27.34           C  
ATOM   2219  CE2 PHE A 279      39.594   6.304  11.531  1.00 22.52           C  
ATOM   2220  CZ  PHE A 279      40.106   7.114  12.559  1.00 21.30           C  
ATOM   2221  N   ALA A 280      36.671   4.033  16.096  1.00 21.21           N  
ATOM   2222  CA  ALA A 280      36.438   4.834  17.290  1.00 21.37           C  
ATOM   2223  C   ALA A 280      37.594   4.791  18.283  1.00 24.94           C  
ATOM   2224  O   ALA A 280      38.347   3.810  18.347  1.00 25.28           O  
ATOM   2225  CB  ALA A 280      35.150   4.369  18.001  1.00 22.38           C  
ATOM   2226  N   VAL A 281      37.739   5.877  19.036  1.00 20.67           N  
ATOM   2227  CA  VAL A 281      38.733   5.941  20.094  1.00 22.23           C  
ATOM   2228  C   VAL A 281      37.882   5.730  21.332  1.00 23.45           C  
ATOM   2229  O   VAL A 281      36.953   6.507  21.598  1.00 19.76           O  
ATOM   2230  CB  VAL A 281      39.420   7.329  20.220  1.00 27.39           C  
ATOM   2231  CG1 VAL A 281      40.362   7.327  21.435  1.00 24.60           C  
ATOM   2232  CG2 VAL A 281      40.176   7.659  18.969  1.00 18.29           C  
ATOM   2233  N   LYS A 282      38.164   4.658  22.065  1.00 20.24           N  
ATOM   2234  CA  LYS A 282      37.407   4.336  23.271  1.00 17.00           C  
ATOM   2235  C   LYS A 282      38.288   4.626  24.486  1.00 15.83           C  
ATOM   2236  O   LYS A 282      39.469   4.325  24.473  1.00 19.01           O  
ATOM   2237  CB  LYS A 282      37.011   2.854  23.257  1.00 20.29           C  
ATOM   2238  CG  LYS A 282      36.274   2.376  24.522  1.00 20.63           C  
ATOM   2239  CD  LYS A 282      36.021   0.874  24.445  1.00 24.96           C  
ATOM   2240  CE  LYS A 282      35.322   0.357  25.693  1.00 26.20           C  
ATOM   2241  NZ  LYS A 282      35.104  -1.123  25.580  1.00 37.28           N  
ATOM   2242  N   PHE A 283      37.722   5.247  25.514  1.00 19.38           N  
ATOM   2243  CA  PHE A 283      38.477   5.553  26.724  1.00 19.36           C  
ATOM   2244  C   PHE A 283      37.515   5.701  27.898  1.00 20.87           C  
ATOM   2245  O   PHE A 283      36.298   5.771  27.711  1.00 19.34           O  
ATOM   2246  CB  PHE A 283      39.336   6.826  26.531  1.00 19.72           C  
ATOM   2247  CG  PHE A 283      38.543   8.053  26.155  1.00 16.75           C  
ATOM   2248  CD1 PHE A 283      38.078   8.924  27.126  1.00 19.51           C  
ATOM   2249  CD2 PHE A 283      38.250   8.320  24.818  1.00 22.77           C  
ATOM   2250  CE1 PHE A 283      37.327  10.062  26.773  1.00 24.93           C  
ATOM   2251  CE2 PHE A 283      37.500   9.453  24.452  1.00 24.13           C  
ATOM   2252  CZ  PHE A 283      37.042  10.321  25.428  1.00 18.60           C  
ATOM   2253  N   ARG A 284      38.051   5.722  29.111  1.00 20.10           N  
ATOM   2254  CA  ARG A 284      37.201   5.836  30.290  1.00 23.95           C  
ATOM   2255  C   ARG A 284      36.657   7.240  30.423  1.00 23.44           C  
ATOM   2256  O   ARG A 284      37.368   8.234  30.234  1.00 22.73           O  
ATOM   2257  CB  ARG A 284      37.971   5.485  31.566  1.00 32.84           C  
ATOM   2258  CG  ARG A 284      38.784   4.198  31.493  1.00 42.16           C  
ATOM   2259  CD  ARG A 284      37.930   2.955  31.578  1.00 51.88           C  
ATOM   2260  NE  ARG A 284      37.179   2.878  32.830  1.00 60.83           N  
ATOM   2261  CZ  ARG A 284      36.545   1.789  33.258  1.00 61.70           C  
ATOM   2262  NH1 ARG A 284      36.575   0.671  32.540  1.00 65.54           N  
ATOM   2263  NH2 ARG A 284      35.859   1.820  34.394  1.00 64.93           N  
ATOM   2264  N   LYS A 285      35.380   7.306  30.750  1.00 24.86           N  
ATOM   2265  CA  LYS A 285      34.691   8.571  30.916  1.00 28.80           C  
ATOM   2266  C   LYS A 285      35.206   9.228  32.200  1.00 26.12           C  
ATOM   2267  O   LYS A 285      35.138   8.641  33.272  1.00 23.13           O  
ATOM   2268  CB  LYS A 285      33.193   8.287  31.006  1.00 23.80           C  
ATOM   2269  CG  LYS A 285      32.307   9.478  31.313  1.00 33.83           C  
ATOM   2270  CD  LYS A 285      30.873   8.994  31.418  1.00 34.90           C  
ATOM   2271  CE  LYS A 285      29.931  10.066  31.907  1.00 45.88           C  
ATOM   2272  NZ  LYS A 285      28.587   9.451  32.155  1.00 46.26           N  
ATOM   2273  N   PRO A 286      35.755  10.443  32.099  1.00 25.23           N  
ATOM   2274  CA  PRO A 286      36.244  11.084  33.321  1.00 30.08           C  
ATOM   2275  C   PRO A 286      35.072  11.479  34.231  1.00 32.72           C  
ATOM   2276  O   PRO A 286      33.950  11.682  33.754  1.00 26.29           O  
ATOM   2277  CB  PRO A 286      37.051  12.283  32.791  1.00 32.07           C  
ATOM   2278  CG  PRO A 286      36.410  12.599  31.459  1.00 25.22           C  
ATOM   2279  CD  PRO A 286      36.094  11.223  30.894  1.00 28.64           C  
ATOM   2280  N   ASP A 287      35.330  11.566  35.536  1.00 32.51           N  
ATOM   2281  CA  ASP A 287      34.295  11.916  36.503  1.00 34.27           C  
ATOM   2282  C   ASP A 287      34.007  13.406  36.583  1.00 33.85           C  
ATOM   2283  O   ASP A 287      34.447  14.092  37.505  1.00 33.98           O  
ATOM   2284  CB  ASP A 287      34.665  11.396  37.894  1.00 45.33           C  
ATOM   2285  CG  ASP A 287      34.531   9.892  38.002  1.00 53.56           C  
ATOM   2286  OD1 ASP A 287      34.815   9.340  39.091  1.00 67.89           O  
ATOM   2287  OD2 ASP A 287      34.135   9.261  36.994  1.00 59.00           O  
ATOM   2288  N   ILE A 288      33.255  13.900  35.609  1.00 29.52           N  
ATOM   2289  CA  ILE A 288      32.881  15.306  35.555  1.00 27.82           C  
ATOM   2290  C   ILE A 288      31.460  15.397  35.022  1.00 25.77           C  
ATOM   2291  O   ILE A 288      30.969  14.462  34.386  1.00 28.39           O  
ATOM   2292  CB  ILE A 288      33.816  16.105  34.631  1.00 28.83           C  
ATOM   2293  CG1 ILE A 288      33.813  15.501  33.226  1.00 29.24           C  
ATOM   2294  CG2 ILE A 288      35.227  16.110  35.191  1.00 32.31           C  
ATOM   2295  CD1 ILE A 288      34.689  16.250  32.250  1.00 25.86           C  
ATOM   2296  N   VAL A 289      30.802  16.522  35.274  1.00 23.89           N  
ATOM   2297  CA  VAL A 289      29.432  16.704  34.820  1.00 26.98           C  
ATOM   2298  C   VAL A 289      29.326  16.847  33.298  1.00 26.14           C  
ATOM   2299  O   VAL A 289      30.301  17.175  32.617  1.00 23.75           O  
ATOM   2300  CB  VAL A 289      28.781  17.935  35.518  1.00 26.28           C  
ATOM   2301  CG1 VAL A 289      28.791  17.725  37.041  1.00 28.18           C  
ATOM   2302  CG2 VAL A 289      29.529  19.192  35.152  1.00 29.03           C  
ATOM   2303  N   ASP A 290      28.129  16.595  32.779  1.00 24.32           N  
ATOM   2304  CA  ASP A 290      27.867  16.665  31.345  1.00 29.64           C  
ATOM   2305  C   ASP A 290      28.236  18.001  30.697  1.00 26.13           C  
ATOM   2306  O   ASP A 290      28.805  18.028  29.612  1.00 25.59           O  
ATOM   2307  CB  ASP A 290      26.384  16.344  31.065  1.00 29.19           C  
ATOM   2308  CG  ASP A 290      26.073  14.851  31.158  1.00 37.36           C  
ATOM   2309  OD1 ASP A 290      24.900  14.462  30.964  1.00 38.09           O  
ATOM   2310  OD2 ASP A 290      26.997  14.056  31.421  1.00 36.43           O  
ATOM   2311  N   ASP A 291      27.912  19.106  31.356  1.00 26.58           N  
ATOM   2312  CA  ASP A 291      28.215  20.422  30.801  1.00 22.66           C  
ATOM   2313  C   ASP A 291      29.711  20.664  30.713  1.00 24.59           C  
ATOM   2314  O   ASP A 291      30.155  21.580  30.039  1.00 24.67           O  
ATOM   2315  CB  ASP A 291      27.525  21.517  31.624  1.00 30.23           C  
ATOM   2316  CG  ASP A 291      26.068  21.746  31.191  1.00 32.03           C  
ATOM   2317  OD1 ASP A 291      25.335  22.452  31.913  1.00 38.89           O  
ATOM   2318  OD2 ASP A 291      25.656  21.229  30.125  1.00 27.34           O  
ATOM   2319  N   ASN A 292      30.486  19.834  31.402  1.00 27.13           N  
ATOM   2320  CA  ASN A 292      31.935  19.936  31.346  1.00 25.61           C  
ATOM   2321  C   ASN A 292      32.451  18.897  30.332  1.00 20.11           C  
ATOM   2322  O   ASN A 292      33.260  19.206  29.471  1.00 23.43           O  
ATOM   2323  CB  ASN A 292      32.524  19.673  32.731  1.00 27.82           C  
ATOM   2324  CG  ASN A 292      34.008  19.933  32.793  1.00 31.99           C  
ATOM   2325  OD1 ASN A 292      34.602  20.452  31.849  1.00 39.86           O  
ATOM   2326  ND2 ASN A 292      34.623  19.575  33.920  1.00 41.17           N  
ATOM   2327  N   LEU A 293      31.944  17.672  30.419  1.00 22.95           N  
ATOM   2328  CA  LEU A 293      32.363  16.591  29.519  1.00 23.76           C  
ATOM   2329  C   LEU A 293      32.037  16.787  28.039  1.00 24.34           C  
ATOM   2330  O   LEU A 293      32.898  16.601  27.163  1.00 24.43           O  
ATOM   2331  CB  LEU A 293      31.735  15.275  29.975  1.00 24.85           C  
ATOM   2332  CG  LEU A 293      32.035  14.029  29.122  1.00 27.62           C  
ATOM   2333  CD1 LEU A 293      33.560  13.754  29.104  1.00 20.12           C  
ATOM   2334  CD2 LEU A 293      31.298  12.847  29.691  1.00 22.18           C  
ATOM   2335  N   TYR A 294      30.795  17.167  27.748  1.00 20.44           N  
ATOM   2336  CA  TYR A 294      30.411  17.304  26.360  1.00 25.03           C  
ATOM   2337  C   TYR A 294      31.246  18.293  25.567  1.00 22.71           C  
ATOM   2338  O   TYR A 294      31.632  17.987  24.449  1.00 25.13           O  
ATOM   2339  CB  TYR A 294      28.907  17.556  26.243  1.00 22.48           C  
ATOM   2340  CG  TYR A 294      28.156  16.249  26.341  1.00 23.68           C  
ATOM   2341  CD1 TYR A 294      27.808  15.718  27.583  1.00 23.04           C  
ATOM   2342  CD2 TYR A 294      27.902  15.477  25.204  1.00 29.46           C  
ATOM   2343  CE1 TYR A 294      27.238  14.451  27.703  1.00 28.50           C  
ATOM   2344  CE2 TYR A 294      27.328  14.185  25.318  1.00 26.35           C  
ATOM   2345  CZ  TYR A 294      27.007  13.691  26.573  1.00 26.89           C  
ATOM   2346  OH  TYR A 294      26.479  12.436  26.724  1.00 28.92           O  
ATOM   2347  N   PRO A 295      31.549  19.481  26.130  1.00 23.58           N  
ATOM   2348  CA  PRO A 295      32.375  20.418  25.353  1.00 22.98           C  
ATOM   2349  C   PRO A 295      33.772  19.830  25.135  1.00 19.87           C  
ATOM   2350  O   PRO A 295      34.433  20.120  24.143  1.00 21.34           O  
ATOM   2351  CB  PRO A 295      32.414  21.661  26.227  1.00 26.34           C  
ATOM   2352  CG  PRO A 295      31.077  21.618  26.927  1.00 27.60           C  
ATOM   2353  CD  PRO A 295      30.971  20.145  27.307  1.00 25.08           C  
ATOM   2354  N   GLN A 296      34.229  19.012  26.078  1.00 20.14           N  
ATOM   2355  CA  GLN A 296      35.533  18.378  25.918  1.00 23.15           C  
ATOM   2356  C   GLN A 296      35.459  17.298  24.827  1.00 15.23           C  
ATOM   2357  O   GLN A 296      36.395  17.147  24.034  1.00 19.40           O  
ATOM   2358  CB  GLN A 296      36.020  17.792  27.256  1.00 23.04           C  
ATOM   2359  CG  GLN A 296      36.659  18.835  28.183  1.00 25.24           C  
ATOM   2360  CD  GLN A 296      37.197  18.225  29.479  1.00 26.80           C  
ATOM   2361  OE1 GLN A 296      37.994  17.287  29.451  1.00 28.14           O  
ATOM   2362  NE2 GLN A 296      36.753  18.754  30.618  1.00 27.62           N  
ATOM   2363  N   LEU A 297      34.346  16.565  24.755  1.00 19.70           N  
ATOM   2364  CA  LEU A 297      34.205  15.539  23.711  1.00 19.53           C  
ATOM   2365  C   LEU A 297      34.128  16.201  22.325  1.00 20.77           C  
ATOM   2366  O   LEU A 297      34.668  15.689  21.348  1.00 14.60           O  
ATOM   2367  CB  LEU A 297      32.964  14.668  23.946  1.00 16.98           C  
ATOM   2368  CG  LEU A 297      32.998  13.745  25.177  1.00 22.16           C  
ATOM   2369  CD1 LEU A 297      31.728  12.901  25.203  1.00 18.29           C  
ATOM   2370  CD2 LEU A 297      34.241  12.842  25.139  1.00 17.75           C  
ATOM   2371  N   GLU A 298      33.468  17.352  22.241  1.00 19.00           N  
ATOM   2372  CA  GLU A 298      33.400  18.057  20.966  1.00 19.57           C  
ATOM   2373  C   GLU A 298      34.802  18.523  20.551  1.00 19.60           C  
ATOM   2374  O   GLU A 298      35.190  18.430  19.386  1.00 20.78           O  
ATOM   2375  CB  GLU A 298      32.469  19.274  21.075  1.00 21.04           C  
ATOM   2376  CG  GLU A 298      31.026  18.901  21.402  1.00 24.11           C  
ATOM   2377  CD  GLU A 298      30.160  20.107  21.761  1.00 33.91           C  
ATOM   2378  OE1 GLU A 298      30.706  21.107  22.275  1.00 32.79           O  
ATOM   2379  OE2 GLU A 298      28.930  20.046  21.551  1.00 33.28           O  
ATOM   2380  N   ARG A 299      35.561  19.033  21.511  1.00 18.12           N  
ATOM   2381  CA  ARG A 299      36.901  19.518  21.212  1.00 19.94           C  
ATOM   2382  C   ARG A 299      37.805  18.367  20.742  1.00 22.31           C  
ATOM   2383  O   ARG A 299      38.465  18.463  19.699  1.00 21.24           O  
ATOM   2384  CB  ARG A 299      37.502  20.166  22.460  1.00 27.09           C  
ATOM   2385  CG  ARG A 299      38.907  20.711  22.262  1.00 28.02           C  
ATOM   2386  CD  ARG A 299      39.468  21.251  23.576  1.00 31.51           C  
ATOM   2387  NE  ARG A 299      40.884  21.562  23.445  1.00 36.68           N  
ATOM   2388  CZ  ARG A 299      41.361  22.683  22.918  1.00 45.09           C  
ATOM   2389  NH1 ARG A 299      40.529  23.622  22.471  1.00 43.10           N  
ATOM   2390  NH2 ARG A 299      42.674  22.855  22.829  1.00 45.41           N  
ATOM   2391  N   ALA A 300      37.811  17.284  21.513  1.00 18.34           N  
ATOM   2392  CA  ALA A 300      38.635  16.116  21.203  1.00 22.55           C  
ATOM   2393  C   ALA A 300      38.306  15.596  19.811  1.00 17.43           C  
ATOM   2394  O   ALA A 300      39.194  15.285  19.030  1.00 17.38           O  
ATOM   2395  CB  ALA A 300      38.409  15.027  22.253  1.00 17.26           C  
ATOM   2396  N   SER A 301      37.013  15.499  19.515  1.00 23.74           N  
ATOM   2397  CA  SER A 301      36.546  15.033  18.213  1.00 20.22           C  
ATOM   2398  C   SER A 301      37.041  15.964  17.088  1.00 22.66           C  
ATOM   2399  O   SER A 301      37.518  15.501  16.045  1.00 20.37           O  
ATOM   2400  CB  SER A 301      35.015  14.953  18.226  1.00 21.97           C  
ATOM   2401  OG  SER A 301      34.529  14.534  16.979  1.00 34.43           O  
ATOM   2402  N   ARG A 302      36.961  17.273  17.314  1.00 21.39           N  
ATOM   2403  CA  ARG A 302      37.405  18.250  16.337  1.00 17.52           C  
ATOM   2404  C   ARG A 302      38.913  18.194  16.089  1.00 22.81           C  
ATOM   2405  O   ARG A 302      39.356  18.211  14.948  1.00 22.64           O  
ATOM   2406  CB  ARG A 302      37.032  19.667  16.794  1.00 26.98           C  
ATOM   2407  CG  ARG A 302      37.502  20.771  15.853  1.00 24.09           C  
ATOM   2408  CD  ARG A 302      36.890  22.109  16.257  1.00 35.57           C  
ATOM   2409  NE  ARG A 302      37.270  22.507  17.611  1.00 35.03           N  
ATOM   2410  CZ  ARG A 302      38.459  23.009  17.941  1.00 40.80           C  
ATOM   2411  NH1 ARG A 302      39.386  23.182  17.011  1.00 44.05           N  
ATOM   2412  NH2 ARG A 302      38.726  23.330  19.203  1.00 36.85           N  
ATOM   2413  N   LYS A 303      39.706  18.151  17.155  1.00 25.42           N  
ATOM   2414  CA  LYS A 303      41.162  18.100  17.013  1.00 18.34           C  
ATOM   2415  C   LYS A 303      41.601  16.855  16.232  1.00 16.83           C  
ATOM   2416  O   LYS A 303      42.479  16.917  15.379  1.00 18.16           O  
ATOM   2417  CB  LYS A 303      41.817  18.086  18.389  1.00 22.38           C  
ATOM   2418  CG  LYS A 303      41.645  19.388  19.174  1.00 27.92           C  
ATOM   2419  CD  LYS A 303      42.465  20.498  18.584  1.00 26.98           C  
ATOM   2420  CE  LYS A 303      42.311  21.776  19.414  1.00 43.13           C  
ATOM   2421  NZ  LYS A 303      43.122  22.883  18.832  1.00 35.89           N  
ATOM   2422  N   ILE A 304      40.990  15.717  16.523  1.00 19.11           N  
ATOM   2423  CA  ILE A 304      41.365  14.506  15.809  1.00 20.12           C  
ATOM   2424  C   ILE A 304      40.891  14.601  14.358  1.00 18.70           C  
ATOM   2425  O   ILE A 304      41.588  14.188  13.425  1.00 20.36           O  
ATOM   2426  CB  ILE A 304      40.793  13.267  16.539  1.00 17.52           C  
ATOM   2427  CG1 ILE A 304      41.514  13.109  17.888  1.00 19.38           C  
ATOM   2428  CG2 ILE A 304      40.993  12.021  15.697  1.00 19.33           C  
ATOM   2429  CD1 ILE A 304      40.856  12.116  18.858  1.00 15.41           C  
ATOM   2430  N   PHE A 305      39.709  15.170  14.161  1.00 20.42           N  
ATOM   2431  CA  PHE A 305      39.184  15.335  12.809  1.00 17.64           C  
ATOM   2432  C   PHE A 305      40.185  16.203  12.041  1.00 17.62           C  
ATOM   2433  O   PHE A 305      40.591  15.891  10.914  1.00 19.40           O  
ATOM   2434  CB  PHE A 305      37.822  16.048  12.855  1.00 20.28           C  
ATOM   2435  CG  PHE A 305      37.122  16.111  11.521  1.00 18.53           C  
ATOM   2436  CD1 PHE A 305      36.170  15.161  11.174  1.00 24.58           C  
ATOM   2437  CD2 PHE A 305      37.435  17.112  10.600  1.00 28.41           C  
ATOM   2438  CE1 PHE A 305      35.528  15.206   9.913  1.00 24.18           C  
ATOM   2439  CE2 PHE A 305      36.799  17.164   9.342  1.00 22.37           C  
ATOM   2440  CZ  PHE A 305      35.851  16.208   9.004  1.00 22.20           C  
ATOM   2441  N   GLU A 306      40.593  17.308  12.659  1.00 21.63           N  
ATOM   2442  CA  GLU A 306      41.543  18.213  12.011  1.00 21.01           C  
ATOM   2443  C   GLU A 306      42.879  17.513  11.730  1.00 23.13           C  
ATOM   2444  O   GLU A 306      43.512  17.752  10.696  1.00 21.42           O  
ATOM   2445  CB  GLU A 306      41.767  19.430  12.889  1.00 19.58           C  
ATOM   2446  CG  GLU A 306      40.493  20.204  13.110  1.00 27.84           C  
ATOM   2447  CD  GLU A 306      40.694  21.453  13.952  1.00 31.30           C  
ATOM   2448  OE1 GLU A 306      41.736  21.554  14.639  1.00 22.95           O  
ATOM   2449  OE2 GLU A 306      39.789  22.317  13.929  1.00 28.29           O  
ATOM   2450  N   PHE A 307      43.310  16.664  12.657  1.00 20.61           N  
ATOM   2451  CA  PHE A 307      44.549  15.923  12.455  1.00 18.11           C  
ATOM   2452  C   PHE A 307      44.378  15.012  11.237  1.00 19.87           C  
ATOM   2453  O   PHE A 307      45.260  14.916  10.379  1.00 20.74           O  
ATOM   2454  CB  PHE A 307      44.859  15.082  13.691  1.00 18.35           C  
ATOM   2455  CG  PHE A 307      45.847  13.981  13.436  1.00 20.60           C  
ATOM   2456  CD1 PHE A 307      47.205  14.259  13.297  1.00 24.74           C  
ATOM   2457  CD2 PHE A 307      45.411  12.665  13.310  1.00 23.64           C  
ATOM   2458  CE1 PHE A 307      48.114  13.231  13.035  1.00 27.71           C  
ATOM   2459  CE2 PHE A 307      46.314  11.625  13.048  1.00 22.75           C  
ATOM   2460  CZ  PHE A 307      47.662  11.911  12.912  1.00 22.36           C  
ATOM   2461  N   LEU A 308      43.239  14.335  11.164  1.00 23.50           N  
ATOM   2462  CA  LEU A 308      42.974  13.442  10.035  1.00 24.98           C  
ATOM   2463  C   LEU A 308      42.958  14.218   8.710  1.00 24.19           C  
ATOM   2464  O   LEU A 308      43.475  13.732   7.701  1.00 22.18           O  
ATOM   2465  CB  LEU A 308      41.649  12.693  10.251  1.00 18.23           C  
ATOM   2466  CG  LEU A 308      41.677  11.708  11.438  1.00 24.71           C  
ATOM   2467  CD1 LEU A 308      40.266  11.271  11.796  1.00 18.05           C  
ATOM   2468  CD2 LEU A 308      42.543  10.500  11.068  1.00 19.03           C  
ATOM   2469  N   GLU A 309      42.388  15.428   8.711  1.00 24.35           N  
ATOM   2470  CA  GLU A 309      42.358  16.240   7.494  1.00 20.78           C  
ATOM   2471  C   GLU A 309      43.773  16.583   7.079  1.00 17.86           C  
ATOM   2472  O   GLU A 309      44.130  16.431   5.905  1.00 21.28           O  
ATOM   2473  CB  GLU A 309      41.629  17.576   7.685  1.00 24.28           C  
ATOM   2474  CG  GLU A 309      40.200  17.540   8.098  1.00 42.91           C  
ATOM   2475  CD  GLU A 309      39.654  18.955   8.282  1.00 50.08           C  
ATOM   2476  OE1 GLU A 309      39.353  19.616   7.263  1.00 58.72           O  
ATOM   2477  OE2 GLU A 309      39.545  19.414   9.440  1.00 46.45           O  
ATOM   2478  N   ARG A 310      44.570  17.071   8.038  1.00 20.79           N  
ATOM   2479  CA  ARG A 310      45.962  17.453   7.780  1.00 20.85           C  
ATOM   2480  C   ARG A 310      46.788  16.303   7.238  1.00 21.99           C  
ATOM   2481  O   ARG A 310      47.638  16.498   6.381  1.00 20.81           O  
ATOM   2482  CB  ARG A 310      46.664  17.937   9.066  1.00 30.02           C  
ATOM   2483  CG  ARG A 310      46.460  19.386   9.436  1.00 33.94           C  
ATOM   2484  CD  ARG A 310      47.493  19.794  10.487  1.00 36.85           C  
ATOM   2485  NE  ARG A 310      47.471  18.955  11.684  1.00 30.46           N  
ATOM   2486  CZ  ARG A 310      46.582  19.063  12.668  1.00 29.93           C  
ATOM   2487  NH1 ARG A 310      45.621  19.980  12.610  1.00 26.68           N  
ATOM   2488  NH2 ARG A 310      46.667  18.257  13.725  1.00 31.62           N  
ATOM   2489  N   GLU A 311      46.548  15.100   7.761  1.00 21.40           N  
ATOM   2490  CA  GLU A 311      47.312  13.927   7.338  1.00 20.90           C  
ATOM   2491  C   GLU A 311      46.730  13.275   6.092  1.00 21.72           C  
ATOM   2492  O   GLU A 311      47.107  12.168   5.702  1.00 22.35           O  
ATOM   2493  CB  GLU A 311      47.421  12.927   8.494  1.00 19.47           C  
ATOM   2494  CG  GLU A 311      48.231  13.483   9.689  1.00 25.38           C  
ATOM   2495  CD  GLU A 311      49.719  13.680   9.392  1.00 28.61           C  
ATOM   2496  OE1 GLU A 311      50.360  14.486  10.098  1.00 28.14           O  
ATOM   2497  OE2 GLU A 311      50.259  13.023   8.473  1.00 26.72           O  
ATOM   2498  N   ASN A 312      45.808  13.993   5.460  1.00 24.68           N  
ATOM   2499  CA  ASN A 312      45.188  13.554   4.223  1.00 19.96           C  
ATOM   2500  C   ASN A 312      44.424  12.233   4.219  1.00 21.29           C  
ATOM   2501  O   ASN A 312      44.478  11.491   3.232  1.00 20.09           O  
ATOM   2502  CB  ASN A 312      46.244  13.529   3.122  1.00 23.18           C  
ATOM   2503  CG  ASN A 312      46.850  14.901   2.871  1.00 29.05           C  
ATOM   2504  OD1 ASN A 312      46.142  15.839   2.493  1.00 26.53           O  
ATOM   2505  ND2 ASN A 312      48.162  15.026   3.080  1.00 20.15           N  
ATOM   2506  N   PHE A 313      43.717  11.937   5.304  1.00 18.16           N  
ATOM   2507  CA  PHE A 313      42.896  10.726   5.366  1.00 20.00           C  
ATOM   2508  C   PHE A 313      41.460  11.079   4.975  1.00 23.26           C  
ATOM   2509  O   PHE A 313      40.554  10.231   4.975  1.00 19.93           O  
ATOM   2510  CB  PHE A 313      42.959  10.117   6.766  1.00 17.93           C  
ATOM   2511  CG  PHE A 313      44.261   9.398   7.038  1.00 19.37           C  
ATOM   2512  CD1 PHE A 313      45.160   9.878   7.999  1.00 20.10           C  
ATOM   2513  CD2 PHE A 313      44.599   8.257   6.299  1.00 17.89           C  
ATOM   2514  CE1 PHE A 313      46.390   9.232   8.220  1.00 23.67           C  
ATOM   2515  CE2 PHE A 313      45.823   7.601   6.505  1.00 19.62           C  
ATOM   2516  CZ  PHE A 313      46.720   8.087   7.464  1.00 17.75           C  
ATOM   2517  N   MET A 314      41.258  12.353   4.636  1.00 19.39           N  
ATOM   2518  CA  MET A 314      39.947  12.828   4.194  1.00 18.69           C  
ATOM   2519  C   MET A 314      38.770  12.390   5.061  1.00 19.45           C  
ATOM   2520  O   MET A 314      37.869  11.643   4.639  1.00 17.11           O  
ATOM   2521  CB  MET A 314      39.745  12.390   2.754  1.00 22.12           C  
ATOM   2522  CG  MET A 314      40.882  12.860   1.882  1.00 31.41           C  
ATOM   2523  SD  MET A 314      40.721  12.283   0.243  1.00 37.19           S  
ATOM   2524  CE  MET A 314      39.146  13.128  -0.234  1.00 36.26           C  
ATOM   2525  N   PRO A 315      38.763  12.842   6.309  1.00 20.10           N  
ATOM   2526  CA  PRO A 315      37.649  12.447   7.163  1.00 21.30           C  
ATOM   2527  C   PRO A 315      36.330  13.003   6.604  1.00 25.24           C  
ATOM   2528  O   PRO A 315      36.272  14.113   6.062  1.00 21.66           O  
ATOM   2529  CB  PRO A 315      38.039  13.035   8.525  1.00 25.39           C  
ATOM   2530  CG  PRO A 315      38.806  14.302   8.123  1.00 17.37           C  
ATOM   2531  CD  PRO A 315      39.674  13.774   6.998  1.00 22.36           C  
ATOM   2532  N   LEU A 316      35.282  12.198   6.701  1.00 24.07           N  
ATOM   2533  CA  LEU A 316      33.963  12.580   6.211  1.00 26.47           C  
ATOM   2534  C   LEU A 316      33.184  13.255   7.307  1.00 29.89           C  
ATOM   2535  O   LEU A 316      32.659  14.364   7.144  1.00 26.34           O  
ATOM   2536  CB  LEU A 316      33.161  11.343   5.787  1.00 31.79           C  
ATOM   2537  CG  LEU A 316      33.209  10.795   4.364  1.00 35.02           C  
ATOM   2538  CD1 LEU A 316      32.284   9.588   4.275  1.00 25.74           C  
ATOM   2539  CD2 LEU A 316      32.784  11.875   3.368  1.00 30.06           C  
ATOM   2540  N   ARG A 317      33.126  12.576   8.446  1.00 24.01           N  
ATOM   2541  CA  ARG A 317      32.350  13.077   9.555  1.00 25.98           C  
ATOM   2542  C   ARG A 317      32.808  12.451  10.869  1.00 29.81           C  
ATOM   2543  O   ARG A 317      33.523  11.447  10.865  1.00 22.21           O  
ATOM   2544  CB  ARG A 317      30.901  12.710   9.286  1.00 30.32           C  
ATOM   2545  CG  ARG A 317      29.940  13.748   9.694  1.00 36.84           C  
ATOM   2546  CD  ARG A 317      28.576  13.482   9.111  1.00 34.66           C  
ATOM   2547  NE  ARG A 317      27.623  14.317   9.828  1.00 32.69           N  
ATOM   2548  CZ  ARG A 317      26.360  13.985  10.038  1.00 31.13           C  
ATOM   2549  NH1 ARG A 317      25.893  12.836   9.572  1.00 24.45           N  
ATOM   2550  NH2 ARG A 317      25.584  14.784  10.752  1.00 27.50           N  
ATOM   2551  N   SER A 318      32.396  13.040  11.985  1.00 24.29           N  
ATOM   2552  CA  SER A 318      32.762  12.493  13.277  1.00 26.60           C  
ATOM   2553  C   SER A 318      31.563  12.558  14.195  1.00 28.04           C  
ATOM   2554  O   SER A 318      30.556  13.193  13.880  1.00 30.48           O  
ATOM   2555  CB  SER A 318      33.944  13.263  13.880  1.00 25.56           C  
ATOM   2556  OG  SER A 318      33.572  14.603  14.200  1.00 31.62           O  
ATOM   2557  N   ALA A 319      31.660  11.877  15.325  1.00 23.87           N  
ATOM   2558  CA  ALA A 319      30.576  11.859  16.296  1.00 24.08           C  
ATOM   2559  C   ALA A 319      31.144  11.310  17.590  1.00 23.16           C  
ATOM   2560  O   ALA A 319      32.254  10.787  17.616  1.00 19.94           O  
ATOM   2561  CB  ALA A 319      29.428  10.963  15.798  1.00 22.53           C  
ATOM   2562  N   PHE A 320      30.393  11.435  18.674  1.00 27.38           N  
ATOM   2563  CA  PHE A 320      30.866  10.914  19.951  1.00 25.22           C  
ATOM   2564  C   PHE A 320      29.700  10.418  20.773  1.00 25.65           C  
ATOM   2565  O   PHE A 320      28.543  10.748  20.503  1.00 28.91           O  
ATOM   2566  CB  PHE A 320      31.658  11.980  20.726  1.00 22.83           C  
ATOM   2567  CG  PHE A 320      30.948  13.301  20.851  1.00 26.56           C  
ATOM   2568  CD1 PHE A 320      29.939  13.481  21.784  1.00 29.61           C  
ATOM   2569  CD2 PHE A 320      31.286  14.361  20.012  1.00 27.89           C  
ATOM   2570  CE1 PHE A 320      29.266  14.707  21.889  1.00 26.13           C  
ATOM   2571  CE2 PHE A 320      30.628  15.583  20.106  1.00 32.70           C  
ATOM   2572  CZ  PHE A 320      29.613  15.755  21.047  1.00 28.86           C  
ATOM   2573  N   LYS A 321      30.019   9.621  21.776  1.00 22.99           N  
ATOM   2574  CA  LYS A 321      29.022   9.040  22.655  1.00 26.68           C  
ATOM   2575  C   LYS A 321      29.639   8.895  24.037  1.00 27.26           C  
ATOM   2576  O   LYS A 321      30.824   8.584  24.172  1.00 24.06           O  
ATOM   2577  CB  LYS A 321      28.614   7.665  22.124  1.00 24.59           C  
ATOM   2578  CG  LYS A 321      27.918   6.750  23.133  1.00 30.38           C  
ATOM   2579  CD  LYS A 321      26.435   7.005  23.224  1.00 31.95           C  
ATOM   2580  CE  LYS A 321      25.761   5.892  24.036  1.00 38.60           C  
ATOM   2581  NZ  LYS A 321      24.288   5.955  23.923  1.00 45.80           N  
ATOM   2582  N   ALA A 322      28.836   9.147  25.061  1.00 29.27           N  
ATOM   2583  CA  ALA A 322      29.292   9.006  26.426  1.00 28.72           C  
ATOM   2584  C   ALA A 322      28.394   7.945  27.027  1.00 31.64           C  
ATOM   2585  O   ALA A 322      27.182   8.100  27.028  1.00 30.27           O  
ATOM   2586  CB  ALA A 322      29.123  10.310  27.173  1.00 29.20           C  
ATOM   2587  N   SER A 323      28.968   6.846  27.492  1.00 29.77           N  
ATOM   2588  CA  SER A 323      28.151   5.821  28.117  1.00 34.68           C  
ATOM   2589  C   SER A 323      28.328   6.043  29.609  1.00 31.54           C  
ATOM   2590  O   SER A 323      28.750   7.113  30.027  1.00 32.35           O  
ATOM   2591  CB  SER A 323      28.625   4.416  27.731  1.00 34.39           C  
ATOM   2592  OG  SER A 323      29.920   4.161  28.249  1.00 47.23           O  
ATOM   2593  N   GLU A 324      28.002   5.034  30.403  1.00 34.43           N  
ATOM   2594  CA  GLU A 324      28.144   5.116  31.847  1.00 36.33           C  
ATOM   2595  C   GLU A 324      29.608   5.102  32.279  1.00 35.08           C  
ATOM   2596  O   GLU A 324      30.025   5.863  33.161  1.00 34.98           O  
ATOM   2597  CB  GLU A 324      27.434   3.928  32.499  1.00 47.59           C  
ATOM   2598  CG  GLU A 324      25.998   4.192  32.858  1.00 57.11           C  
ATOM   2599  CD  GLU A 324      25.874   5.357  33.814  1.00 60.96           C  
ATOM   2600  OE1 GLU A 324      26.608   5.359  34.828  1.00 63.07           O  
ATOM   2601  OE2 GLU A 324      25.051   6.267  33.553  1.00 65.88           O  
ATOM   2602  N   GLU A 325      30.386   4.239  31.640  1.00 29.47           N  
ATOM   2603  CA  GLU A 325      31.785   4.065  31.988  1.00 30.50           C  
ATOM   2604  C   GLU A 325      32.804   4.492  30.940  1.00 29.31           C  
ATOM   2605  O   GLU A 325      33.967   4.774  31.264  1.00 26.22           O  
ATOM   2606  CB  GLU A 325      32.022   2.597  32.331  1.00 34.50           C  
ATOM   2607  CG  GLU A 325      31.186   2.087  33.497  1.00 44.04           C  
ATOM   2608  CD  GLU A 325      31.369   2.924  34.759  1.00 52.89           C  
ATOM   2609  OE1 GLU A 325      32.509   3.366  35.022  1.00 55.09           O  
ATOM   2610  OE2 GLU A 325      30.378   3.131  35.498  1.00 57.82           O  
ATOM   2611  N   PHE A 326      32.374   4.541  29.686  1.00 27.56           N  
ATOM   2612  CA  PHE A 326      33.286   4.884  28.606  1.00 27.12           C  
ATOM   2613  C   PHE A 326      32.780   5.997  27.709  1.00 26.86           C  
ATOM   2614  O   PHE A 326      31.592   6.309  27.697  1.00 27.66           O  
ATOM   2615  CB  PHE A 326      33.542   3.647  27.728  1.00 25.07           C  
ATOM   2616  CG  PHE A 326      34.183   2.491  28.455  1.00 27.67           C  
ATOM   2617  CD1 PHE A 326      33.410   1.433  28.933  1.00 33.60           C  
ATOM   2618  CD2 PHE A 326      35.557   2.436  28.626  1.00 24.76           C  
ATOM   2619  CE1 PHE A 326      34.002   0.334  29.579  1.00 31.86           C  
ATOM   2620  CE2 PHE A 326      36.160   1.341  29.273  1.00 30.46           C  
ATOM   2621  CZ  PHE A 326      35.376   0.287  29.745  1.00 29.13           C  
ATOM   2622  N   CYS A 327      33.706   6.589  26.962  1.00 23.86           N  
ATOM   2623  CA  CYS A 327      33.385   7.616  25.981  1.00 26.28           C  
ATOM   2624  C   CYS A 327      33.906   7.091  24.648  1.00 24.59           C  
ATOM   2625  O   CYS A 327      34.883   6.333  24.613  1.00 25.91           O  
ATOM   2626  CB  CYS A 327      34.062   8.941  26.316  1.00 21.98           C  
ATOM   2627  SG  CYS A 327      33.248   9.782  27.646  1.00 28.62           S  
ATOM   2628  N   TYR A 328      33.253   7.485  23.560  1.00 22.08           N  
ATOM   2629  CA  TYR A 328      33.656   7.045  22.230  1.00 21.52           C  
ATOM   2630  C   TYR A 328      33.741   8.213  21.257  1.00 22.64           C  
ATOM   2631  O   TYR A 328      32.797   9.004  21.136  1.00 18.79           O  
ATOM   2632  CB  TYR A 328      32.667   6.020  21.657  1.00 23.44           C  
ATOM   2633  CG  TYR A 328      32.454   4.797  22.528  1.00 24.74           C  
ATOM   2634  CD1 TYR A 328      31.612   4.846  23.629  1.00 26.00           C  
ATOM   2635  CD2 TYR A 328      33.118   3.603  22.259  1.00 28.51           C  
ATOM   2636  CE1 TYR A 328      31.429   3.740  24.452  1.00 31.77           C  
ATOM   2637  CE2 TYR A 328      32.945   2.482  23.076  1.00 28.57           C  
ATOM   2638  CZ  TYR A 328      32.103   2.559  24.166  1.00 29.65           C  
ATOM   2639  OH  TYR A 328      31.923   1.468  24.980  1.00 32.82           O  
ATOM   2640  N   LEU A 329      34.883   8.343  20.587  1.00 18.43           N  
ATOM   2641  CA  LEU A 329      35.044   9.395  19.576  1.00 18.23           C  
ATOM   2642  C   LEU A 329      35.008   8.589  18.281  1.00 20.32           C  
ATOM   2643  O   LEU A 329      35.897   7.776  18.028  1.00 23.83           O  
ATOM   2644  CB  LEU A 329      36.384  10.137  19.765  1.00 18.20           C  
ATOM   2645  CG  LEU A 329      36.549  10.753  21.174  1.00 18.97           C  
ATOM   2646  CD1 LEU A 329      37.919  11.407  21.346  1.00 22.03           C  
ATOM   2647  CD2 LEU A 329      35.449  11.779  21.404  1.00 20.01           C  
ATOM   2648  N   LEU A 330      33.940   8.773  17.506  1.00 22.07           N  
ATOM   2649  CA  LEU A 330      33.719   8.058  16.239  1.00 24.12           C  
ATOM   2650  C   LEU A 330      34.145   8.862  15.011  1.00 23.79           C  
ATOM   2651  O   LEU A 330      33.919  10.078  14.962  1.00 20.44           O  
ATOM   2652  CB  LEU A 330      32.236   7.715  16.091  1.00 25.21           C  
ATOM   2653  CG  LEU A 330      31.565   6.870  17.180  1.00 36.51           C  
ATOM   2654  CD1 LEU A 330      30.066   6.865  16.959  1.00 38.60           C  
ATOM   2655  CD2 LEU A 330      32.092   5.454  17.134  1.00 41.74           C  
ATOM   2656  N   PHE A 331      34.733   8.174  14.028  1.00 17.65           N  
ATOM   2657  CA  PHE A 331      35.192   8.788  12.776  1.00 18.11           C  
ATOM   2658  C   PHE A 331      34.978   7.900  11.547  1.00 22.76           C  
ATOM   2659  O   PHE A 331      35.001   6.665  11.632  1.00 22.79           O  
ATOM   2660  CB  PHE A 331      36.701   9.106  12.814  1.00 17.83           C  
ATOM   2661  CG  PHE A 331      37.133   9.917  14.000  1.00 19.98           C  
ATOM   2662  CD1 PHE A 331      37.488   9.293  15.190  1.00 18.16           C  
ATOM   2663  CD2 PHE A 331      37.110  11.306  13.952  1.00 18.11           C  
ATOM   2664  CE1 PHE A 331      37.800  10.042  16.319  1.00 25.06           C  
ATOM   2665  CE2 PHE A 331      37.421  12.063  15.077  1.00 21.42           C  
ATOM   2666  CZ  PHE A 331      37.762  11.433  16.260  1.00 20.69           C  
ATOM   2667  N   GLU A 332      34.778   8.537  10.399  1.00 18.78           N  
ATOM   2668  CA  GLU A 332      34.666   7.823   9.125  1.00 19.04           C  
ATOM   2669  C   GLU A 332      35.553   8.583   8.133  1.00 19.16           C  
ATOM   2670  O   GLU A 332      35.421   9.799   7.951  1.00 20.48           O  
ATOM   2671  CB  GLU A 332      33.216   7.751   8.622  1.00 19.65           C  
ATOM   2672  CG  GLU A 332      33.114   7.152   7.218  1.00 20.46           C  
ATOM   2673  CD  GLU A 332      31.675   6.913   6.757  1.00 21.23           C  
ATOM   2674  OE1 GLU A 332      30.837   7.794   6.974  1.00 25.36           O  
ATOM   2675  OE2 GLU A 332      31.384   5.844   6.169  1.00 27.44           O  
ATOM   2676  N   CYS A 333      36.489   7.871   7.519  1.00 17.82           N  
ATOM   2677  CA  CYS A 333      37.421   8.492   6.600  1.00 19.52           C  
ATOM   2678  C   CYS A 333      37.338   7.874   5.220  1.00 23.39           C  
ATOM   2679  O   CYS A 333      37.096   6.669   5.085  1.00 18.92           O  
ATOM   2680  CB  CYS A 333      38.855   8.336   7.117  1.00 17.43           C  
ATOM   2681  SG  CYS A 333      39.250   9.226   8.635  1.00 21.29           S  
ATOM   2682  N   GLN A 334      37.585   8.696   4.201  1.00 21.85           N  
ATOM   2683  CA  GLN A 334      37.541   8.231   2.814  1.00 17.04           C  
ATOM   2684  C   GLN A 334      38.787   7.470   2.394  1.00 21.13           C  
ATOM   2685  O   GLN A 334      38.783   6.777   1.368  1.00 22.02           O  
ATOM   2686  CB  GLN A 334      37.308   9.416   1.887  1.00 18.64           C  
ATOM   2687  CG  GLN A 334      35.984  10.134   2.194  1.00 18.99           C  
ATOM   2688  CD  GLN A 334      35.863  11.451   1.453  1.00 23.94           C  
ATOM   2689  OE1 GLN A 334      35.522  11.487   0.273  1.00 24.42           O  
ATOM   2690  NE2 GLN A 334      36.165  12.549   2.148  1.00 23.26           N  
ATOM   2691  N   ILE A 335      39.849   7.592   3.183  1.00 18.22           N  
ATOM   2692  CA  ILE A 335      41.102   6.909   2.891  1.00 20.42           C  
ATOM   2693  C   ILE A 335      41.343   5.822   3.948  1.00 22.49           C  
ATOM   2694  O   ILE A 335      41.469   6.127   5.134  1.00 22.22           O  
ATOM   2695  CB  ILE A 335      42.326   7.907   2.931  1.00 22.35           C  
ATOM   2696  CG1 ILE A 335      42.117   9.074   1.954  1.00 20.48           C  
ATOM   2697  CG2 ILE A 335      43.632   7.159   2.596  1.00 21.04           C  
ATOM   2698  CD1 ILE A 335      41.916   8.648   0.479  1.00 26.22           C  
ATOM   2699  N   LYS A 336      41.408   4.562   3.532  1.00 21.48           N  
ATOM   2700  CA  LYS A 336      41.679   3.482   4.478  1.00 16.19           C  
ATOM   2701  C   LYS A 336      43.181   3.287   4.601  1.00 21.49           C  
ATOM   2702  O   LYS A 336      43.681   2.871   5.649  1.00 22.16           O  
ATOM   2703  CB  LYS A 336      41.013   2.177   4.021  1.00 19.40           C  
ATOM   2704  CG  LYS A 336      39.497   2.155   4.202  1.00 21.61           C  
ATOM   2705  CD  LYS A 336      38.883   0.783   3.905  1.00 30.06           C  
ATOM   2706  CE  LYS A 336      38.684   0.556   2.434  1.00 41.14           C  
ATOM   2707  NZ  LYS A 336      39.942   0.660   1.630  1.00 46.25           N  
ATOM   2708  N   GLU A 337      43.902   3.623   3.531  1.00 22.90           N  
ATOM   2709  CA  GLU A 337      45.346   3.465   3.505  1.00 24.63           C  
ATOM   2710  C   GLU A 337      46.019   4.474   2.574  1.00 23.43           C  
ATOM   2711  O   GLU A 337      45.565   4.705   1.457  1.00 19.34           O  
ATOM   2712  CB  GLU A 337      45.683   2.048   3.041  1.00 29.83           C  
ATOM   2713  CG  GLU A 337      47.152   1.741   2.881  1.00 44.23           C  
ATOM   2714  CD  GLU A 337      47.375   0.347   2.293  1.00 52.36           C  
ATOM   2715  OE1 GLU A 337      46.964   0.096   1.131  1.00 54.50           O  
ATOM   2716  OE2 GLU A 337      47.950  -0.499   3.001  1.00 49.69           O  
ATOM   2717  N   ILE A 338      47.100   5.072   3.049  1.00 21.50           N  
ATOM   2718  CA  ILE A 338      47.858   6.028   2.260  1.00 23.18           C  
ATOM   2719  C   ILE A 338      49.266   5.450   2.073  1.00 24.43           C  
ATOM   2720  O   ILE A 338      49.732   4.634   2.896  1.00 21.60           O  
ATOM   2721  CB  ILE A 338      47.921   7.403   2.958  1.00 26.91           C  
ATOM   2722  CG1 ILE A 338      48.423   8.466   1.979  1.00 16.63           C  
ATOM   2723  CG2 ILE A 338      48.839   7.334   4.183  1.00 26.40           C  
ATOM   2724  CD1 ILE A 338      47.951   9.880   2.380  1.00 19.81           C  
ATOM   2725  N   SER A 339      49.941   5.850   0.995  1.00 20.01           N  
ATOM   2726  CA  SER A 339      51.274   5.317   0.707  1.00 21.76           C  
ATOM   2727  C   SER A 339      52.287   5.623   1.806  1.00 22.62           C  
ATOM   2728  O   SER A 339      52.148   6.594   2.548  1.00 19.69           O  
ATOM   2729  CB  SER A 339      51.791   5.864  -0.629  1.00 23.00           C  
ATOM   2730  OG  SER A 339      52.066   7.260  -0.547  1.00 24.32           O  
ATOM   2731  N   ARG A 340      53.308   4.786   1.902  1.00 21.18           N  
ATOM   2732  CA  ARG A 340      54.356   4.984   2.881  1.00 24.21           C  
ATOM   2733  C   ARG A 340      55.148   6.247   2.487  1.00 21.34           C  
ATOM   2734  O   ARG A 340      55.462   7.083   3.332  1.00 22.91           O  
ATOM   2735  CB  ARG A 340      55.290   3.774   2.882  1.00 29.94           C  
ATOM   2736  CG  ARG A 340      56.285   3.763   4.027  1.00 41.54           C  
ATOM   2737  CD  ARG A 340      55.710   3.025   5.225  1.00 44.44           C  
ATOM   2738  NE  ARG A 340      55.807   3.807   6.456  1.00 59.25           N  
ATOM   2739  CZ  ARG A 340      55.379   3.381   7.641  1.00 60.04           C  
ATOM   2740  NH1 ARG A 340      54.829   2.176   7.753  1.00 62.92           N  
ATOM   2741  NH2 ARG A 340      55.492   4.158   8.712  1.00 66.97           N  
ATOM   2742  N   VAL A 341      55.436   6.387   1.196  1.00 16.75           N  
ATOM   2743  CA  VAL A 341      56.196   7.526   0.698  1.00 19.03           C  
ATOM   2744  C   VAL A 341      55.356   8.801   0.602  1.00 23.67           C  
ATOM   2745  O   VAL A 341      54.154   8.766   0.296  1.00 20.21           O  
ATOM   2746  CB  VAL A 341      56.802   7.232  -0.704  1.00 27.78           C  
ATOM   2747  CG1 VAL A 341      57.685   8.397  -1.150  1.00 30.51           C  
ATOM   2748  CG2 VAL A 341      57.634   5.968  -0.656  1.00 36.16           C  
ATOM   2749  N   PHE A 342      55.999   9.930   0.869  1.00 20.01           N  
ATOM   2750  CA  PHE A 342      55.343  11.227   0.803  1.00 22.06           C  
ATOM   2751  C   PHE A 342      56.405  12.218   0.367  1.00 22.69           C  
ATOM   2752  O   PHE A 342      57.594  11.890   0.383  1.00 20.40           O  
ATOM   2753  CB  PHE A 342      54.735  11.613   2.169  1.00 20.17           C  
ATOM   2754  CG  PHE A 342      55.731  12.165   3.177  1.00 23.94           C  
ATOM   2755  CD1 PHE A 342      55.928  13.539   3.307  1.00 23.98           C  
ATOM   2756  CD2 PHE A 342      56.407  11.312   4.041  1.00 25.58           C  
ATOM   2757  CE1 PHE A 342      56.777  14.052   4.296  1.00 26.15           C  
ATOM   2758  CE2 PHE A 342      57.261  11.813   5.035  1.00 26.90           C  
ATOM   2759  CZ  PHE A 342      57.443  13.185   5.162  1.00 27.03           C  
ATOM   2760  N   ARG A 343      55.978  13.410  -0.045  1.00 22.04           N  
ATOM   2761  CA  ARG A 343      56.905  14.456  -0.502  1.00 26.35           C  
ATOM   2762  C   ARG A 343      57.231  15.449   0.594  1.00 26.16           C  
ATOM   2763  O   ARG A 343      56.338  16.070   1.145  1.00 31.11           O  
ATOM   2764  CB  ARG A 343      56.300  15.227  -1.690  1.00 26.01           C  
ATOM   2765  CG  ARG A 343      56.416  14.515  -3.006  1.00 28.12           C  
ATOM   2766  CD  ARG A 343      55.542  15.175  -4.069  1.00 38.97           C  
ATOM   2767  NE  ARG A 343      55.807  16.602  -4.196  1.00 34.03           N  
ATOM   2768  CZ  ARG A 343      56.123  17.199  -5.338  1.00 33.83           C  
ATOM   2769  NH1 ARG A 343      56.214  16.494  -6.457  1.00 31.22           N  
ATOM   2770  NH2 ARG A 343      56.348  18.503  -5.360  1.00 34.21           N  
ATOM   2771  N   ARG A 344      58.507  15.595   0.911  1.00 25.60           N  
ATOM   2772  CA  ARG A 344      58.937  16.541   1.939  1.00 27.21           C  
ATOM   2773  C   ARG A 344      59.486  17.755   1.190  1.00 23.74           C  
ATOM   2774  O   ARG A 344      60.367  17.619   0.357  1.00 23.85           O  
ATOM   2775  CB  ARG A 344      60.028  15.899   2.812  1.00 30.27           C  
ATOM   2776  CG  ARG A 344      60.879  16.862   3.644  1.00 37.88           C  
ATOM   2777  CD  ARG A 344      60.097  17.583   4.729  1.00 43.01           C  
ATOM   2778  NE  ARG A 344      59.503  16.653   5.681  1.00 50.16           N  
ATOM   2779  CZ  ARG A 344      58.933  17.014   6.827  1.00 59.99           C  
ATOM   2780  NH1 ARG A 344      58.888  18.295   7.176  1.00 63.35           N  
ATOM   2781  NH2 ARG A 344      58.385  16.095   7.617  1.00 58.85           N  
ATOM   2782  N   MET A 345      58.954  18.936   1.471  1.00 27.43           N  
ATOM   2783  CA  MET A 345      59.401  20.139   0.782  1.00 24.71           C  
ATOM   2784  C   MET A 345      60.759  20.633   1.268  1.00 29.40           C  
ATOM   2785  O   MET A 345      61.002  20.724   2.477  1.00 29.51           O  
ATOM   2786  CB  MET A 345      58.362  21.251   0.943  1.00 27.01           C  
ATOM   2787  CG  MET A 345      58.776  22.585   0.319  1.00 34.00           C  
ATOM   2788  SD  MET A 345      57.540  23.883   0.585  1.00 40.88           S  
ATOM   2789  CE  MET A 345      56.668  23.766  -0.963  1.00 41.21           C  
ATOM   2790  N   GLY A 346      61.632  20.953   0.317  1.00 27.62           N  
ATOM   2791  CA  GLY A 346      62.964  21.450   0.630  1.00 27.33           C  
ATOM   2792  C   GLY A 346      63.122  22.928   0.288  1.00 25.71           C  
ATOM   2793  O   GLY A 346      62.130  23.619   0.034  1.00 22.71           O  
ATOM   2794  N   PRO A 347      64.359  23.452   0.266  1.00 27.41           N  
ATOM   2795  CA  PRO A 347      64.483  24.874  -0.060  1.00 26.46           C  
ATOM   2796  C   PRO A 347      64.648  25.210  -1.545  1.00 28.54           C  
ATOM   2797  O   PRO A 347      64.907  24.337  -2.378  1.00 23.04           O  
ATOM   2798  CB  PRO A 347      65.691  25.306   0.777  1.00 31.92           C  
ATOM   2799  CG  PRO A 347      66.604  24.114   0.675  1.00 31.25           C  
ATOM   2800  CD  PRO A 347      65.635  22.900   0.766  1.00 31.17           C  
ATOM   2801  N   GLN A 348      64.472  26.491  -1.872  1.00 27.12           N  
ATOM   2802  CA  GLN A 348      64.665  26.960  -3.238  1.00 26.16           C  
ATOM   2803  C   GLN A 348      66.105  26.616  -3.613  1.00 24.73           C  
ATOM   2804  O   GLN A 348      66.981  26.600  -2.743  1.00 26.10           O  
ATOM   2805  CB  GLN A 348      64.446  28.475  -3.319  1.00 30.40           C  
ATOM   2806  CG  GLN A 348      63.006  28.886  -3.153  1.00 33.50           C  
ATOM   2807  CD  GLN A 348      62.746  30.283  -3.675  1.00 42.57           C  
ATOM   2808  OE1 GLN A 348      61.597  30.665  -3.903  1.00 45.33           O  
ATOM   2809  NE2 GLN A 348      63.814  31.055  -3.869  1.00 45.60           N  
ATOM   2810  N   PHE A 349      66.362  26.363  -4.900  1.00 25.61           N  
ATOM   2811  CA  PHE A 349      67.701  25.970  -5.336  1.00 26.98           C  
ATOM   2812  C   PHE A 349      68.780  26.999  -5.039  1.00 26.41           C  
ATOM   2813  O   PHE A 349      69.951  26.637  -4.925  1.00 24.05           O  
ATOM   2814  CB  PHE A 349      67.724  25.616  -6.840  1.00 20.73           C  
ATOM   2815  CG  PHE A 349      67.771  26.822  -7.765  1.00 21.81           C  
ATOM   2816  CD1 PHE A 349      68.996  27.411  -8.111  1.00 20.72           C  
ATOM   2817  CD2 PHE A 349      66.593  27.360  -8.285  1.00 22.61           C  
ATOM   2818  CE1 PHE A 349      69.053  28.530  -8.964  1.00 20.77           C  
ATOM   2819  CE2 PHE A 349      66.629  28.481  -9.140  1.00 27.23           C  
ATOM   2820  CZ  PHE A 349      67.866  29.063  -9.479  1.00 24.14           C  
ATOM   2821  N   GLU A 350      68.384  28.264  -4.899  1.00 26.93           N  
ATOM   2822  CA  GLU A 350      69.334  29.346  -4.614  1.00 28.57           C  
ATOM   2823  C   GLU A 350      70.034  29.289  -3.252  1.00 31.73           C  
ATOM   2824  O   GLU A 350      71.219  29.640  -3.155  1.00 31.34           O  
ATOM   2825  CB  GLU A 350      68.651  30.715  -4.741  1.00 23.31           C  
ATOM   2826  CG  GLU A 350      68.326  31.122  -6.168  1.00 26.01           C  
ATOM   2827  CD  GLU A 350      66.891  30.820  -6.547  1.00 28.48           C  
ATOM   2828  OE1 GLU A 350      66.300  29.903  -5.930  1.00 26.21           O  
ATOM   2829  OE2 GLU A 350      66.357  31.496  -7.465  1.00 25.88           O  
ATOM   2830  N   ASP A 351      69.306  28.866  -2.214  1.00 30.79           N  
ATOM   2831  CA  ASP A 351      69.843  28.800  -0.849  1.00 33.49           C  
ATOM   2832  C   ASP A 351      70.826  27.661  -0.678  1.00 35.27           C  
ATOM   2833  O   ASP A 351      70.466  26.567  -0.230  1.00 35.79           O  
ATOM   2834  CB  ASP A 351      68.705  28.649   0.171  1.00 37.17           C  
ATOM   2835  CG  ASP A 351      69.179  28.812   1.625  1.00 48.60           C  
ATOM   2836  OD1 ASP A 351      70.395  28.995   1.883  1.00 38.13           O  
ATOM   2837  OD2 ASP A 351      68.315  28.754   2.524  1.00 55.73           O  
ATOM   2838  N   GLU A 352      72.083  27.947  -1.000  1.00 32.38           N  
ATOM   2839  CA  GLU A 352      73.150  26.969  -0.936  1.00 31.61           C  
ATOM   2840  C   GLU A 352      73.307  26.216   0.382  1.00 32.96           C  
ATOM   2841  O   GLU A 352      73.382  24.979   0.384  1.00 28.50           O  
ATOM   2842  CB  GLU A 352      74.468  27.642  -1.316  1.00 37.16           C  
ATOM   2843  CG  GLU A 352      75.615  26.693  -1.576  1.00 47.07           C  
ATOM   2844  CD  GLU A 352      76.784  27.398  -2.251  1.00 53.25           C  
ATOM   2845  OE1 GLU A 352      76.771  28.649  -2.282  1.00 56.63           O  
ATOM   2846  OE2 GLU A 352      77.713  26.709  -2.739  1.00 50.94           O  
ATOM   2847  N   ARG A 353      73.361  26.936   1.498  1.00 27.41           N  
ATOM   2848  CA  ARG A 353      73.535  26.256   2.780  1.00 31.49           C  
ATOM   2849  C   ARG A 353      72.369  25.358   3.151  1.00 26.15           C  
ATOM   2850  O   ARG A 353      72.572  24.249   3.623  1.00 26.65           O  
ATOM   2851  CB  ARG A 353      73.778  27.254   3.918  1.00 32.45           C  
ATOM   2852  CG  ARG A 353      75.156  27.861   3.898  1.00 35.27           C  
ATOM   2853  CD  ARG A 353      75.486  28.532   5.229  1.00 48.64           C  
ATOM   2854  NE  ARG A 353      76.707  29.331   5.123  1.00 53.88           N  
ATOM   2855  CZ  ARG A 353      77.918  28.832   4.886  1.00 53.04           C  
ATOM   2856  NH1 ARG A 353      78.086  27.522   4.737  1.00 41.94           N  
ATOM   2857  NH2 ARG A 353      78.957  29.651   4.772  1.00 45.75           N  
ATOM   2858  N   ASN A 354      71.150  25.840   2.956  1.00 24.49           N  
ATOM   2859  CA  ASN A 354      70.017  25.017   3.287  1.00 29.21           C  
ATOM   2860  C   ASN A 354      69.904  23.820   2.361  1.00 28.33           C  
ATOM   2861  O   ASN A 354      69.478  22.756   2.798  1.00 28.47           O  
ATOM   2862  CB  ASN A 354      68.743  25.854   3.306  1.00 33.14           C  
ATOM   2863  CG  ASN A 354      68.667  26.728   4.539  1.00 41.07           C  
ATOM   2864  OD1 ASN A 354      67.783  27.576   4.675  1.00 49.73           O  
ATOM   2865  ND2 ASN A 354      69.610  26.518   5.460  1.00 47.53           N  
ATOM   2866  N   VAL A 355      70.322  23.973   1.105  1.00 27.89           N  
ATOM   2867  CA  VAL A 355      70.261  22.855   0.167  1.00 29.82           C  
ATOM   2868  C   VAL A 355      71.218  21.763   0.619  1.00 30.93           C  
ATOM   2869  O   VAL A 355      70.856  20.580   0.626  1.00 29.99           O  
ATOM   2870  CB  VAL A 355      70.586  23.308  -1.291  1.00 28.90           C  
ATOM   2871  CG1 VAL A 355      70.775  22.096  -2.208  1.00 25.88           C  
ATOM   2872  CG2 VAL A 355      69.438  24.156  -1.820  1.00 20.36           C  
ATOM   2873  N   LYS A 356      72.428  22.150   1.029  1.00 29.20           N  
ATOM   2874  CA  LYS A 356      73.409  21.172   1.499  1.00 30.61           C  
ATOM   2875  C   LYS A 356      72.857  20.461   2.739  1.00 28.27           C  
ATOM   2876  O   LYS A 356      73.037  19.256   2.915  1.00 31.43           O  
ATOM   2877  CB  LYS A 356      74.736  21.856   1.847  1.00 36.39           C  
ATOM   2878  CG  LYS A 356      75.782  20.902   2.412  1.00 41.89           C  
ATOM   2879  CD  LYS A 356      77.094  21.610   2.777  1.00 50.86           C  
ATOM   2880  CE  LYS A 356      77.909  22.018   1.539  1.00 51.42           C  
ATOM   2881  NZ  LYS A 356      77.238  23.062   0.711  1.00 49.23           N  
ATOM   2882  N   LYS A 357      72.198  21.219   3.607  1.00 28.45           N  
ATOM   2883  CA  LYS A 357      71.605  20.646   4.814  1.00 32.75           C  
ATOM   2884  C   LYS A 357      70.506  19.646   4.408  1.00 29.90           C  
ATOM   2885  O   LYS A 357      70.487  18.502   4.867  1.00 31.12           O  
ATOM   2886  CB  LYS A 357      71.007  21.760   5.678  1.00 32.77           C  
ATOM   2887  CG  LYS A 357      70.390  21.288   6.963  1.00 41.10           C  
ATOM   2888  CD  LYS A 357      69.813  22.462   7.752  1.00 48.65           C  
ATOM   2889  CE  LYS A 357      69.241  21.999   9.094  1.00 49.90           C  
ATOM   2890  NZ  LYS A 357      68.558  23.108   9.832  1.00 53.98           N  
ATOM   2891  N   PHE A 358      69.606  20.080   3.531  1.00 29.50           N  
ATOM   2892  CA  PHE A 358      68.506  19.230   3.062  1.00 29.31           C  
ATOM   2893  C   PHE A 358      69.033  17.938   2.440  1.00 30.38           C  
ATOM   2894  O   PHE A 358      68.457  16.870   2.642  1.00 31.51           O  
ATOM   2895  CB  PHE A 358      67.659  19.993   2.032  1.00 29.74           C  
ATOM   2896  CG  PHE A 358      66.353  19.316   1.668  1.00 29.94           C  
ATOM   2897  CD1 PHE A 358      65.356  19.111   2.627  1.00 31.26           C  
ATOM   2898  CD2 PHE A 358      66.102  18.924   0.349  1.00 29.90           C  
ATOM   2899  CE1 PHE A 358      64.126  18.523   2.282  1.00 24.93           C  
ATOM   2900  CE2 PHE A 358      64.878  18.335  -0.009  1.00 24.52           C  
ATOM   2901  CZ  PHE A 358      63.889  18.136   0.958  1.00 22.03           C  
ATOM   2902  N   LEU A 359      70.141  18.029   1.705  1.00 28.33           N  
ATOM   2903  CA  LEU A 359      70.696  16.856   1.040  1.00 30.75           C  
ATOM   2904  C   LEU A 359      71.598  15.969   1.889  1.00 35.93           C  
ATOM   2905  O   LEU A 359      71.870  14.827   1.507  1.00 34.33           O  
ATOM   2906  CB  LEU A 359      71.464  17.266  -0.220  1.00 30.40           C  
ATOM   2907  CG  LEU A 359      70.670  18.035  -1.279  1.00 32.80           C  
ATOM   2908  CD1 LEU A 359      71.577  18.310  -2.474  1.00 33.08           C  
ATOM   2909  CD2 LEU A 359      69.446  17.231  -1.707  1.00 28.75           C  
ATOM   2910  N   SER A 360      72.059  16.488   3.026  1.00 34.89           N  
ATOM   2911  CA  SER A 360      72.952  15.730   3.904  1.00 35.90           C  
ATOM   2912  C   SER A 360      72.239  14.570   4.598  1.00 37.04           C  
ATOM   2913  O   SER A 360      72.888  13.640   5.071  1.00 37.87           O  
ATOM   2914  CB  SER A 360      73.561  16.652   4.966  1.00 33.90           C  
ATOM   2915  OG  SER A 360      72.550  17.149   5.829  1.00 38.53           O  
ATOM   2916  N   ARG A 361      70.911  14.631   4.670  1.00 37.99           N  
ATOM   2917  CA  ARG A 361      70.155  13.566   5.312  1.00 41.56           C  
ATOM   2918  C   ARG A 361      70.108  12.300   4.460  1.00 41.32           C  
ATOM   2919  O   ARG A 361      69.904  12.345   3.245  1.00 34.17           O  
ATOM   2920  CB  ARG A 361      68.728  14.033   5.650  1.00 47.43           C  
ATOM   2921  CG  ARG A 361      68.679  15.175   6.683  1.00 58.19           C  
ATOM   2922  CD  ARG A 361      67.273  15.417   7.275  1.00 57.95           C  
ATOM   2923  NE  ARG A 361      66.263  15.780   6.276  1.00 62.81           N  
ATOM   2924  CZ  ARG A 361      64.984  16.040   6.560  1.00 60.80           C  
ATOM   2925  NH1 ARG A 361      64.554  15.982   7.817  1.00 59.49           N  
ATOM   2926  NH2 ARG A 361      64.130  16.351   5.589  1.00 43.25           N  
ATOM   2927  N   ASN A 362      70.317  11.169   5.122  1.00 40.90           N  
ATOM   2928  CA  ASN A 362      70.292   9.868   4.465  1.00 43.29           C  
ATOM   2929  C   ASN A 362      68.838   9.511   4.157  1.00 37.35           C  
ATOM   2930  O   ASN A 362      67.977   9.613   5.022  1.00 36.11           O  
ATOM   2931  CB  ASN A 362      70.903   8.818   5.398  1.00 45.92           C  
ATOM   2932  CG  ASN A 362      72.135   9.339   6.134  1.00 56.77           C  
ATOM   2933  OD1 ASN A 362      72.046  10.267   6.950  1.00 53.18           O  
ATOM   2934  ND2 ASN A 362      73.289   8.750   5.846  1.00 57.00           N  
ATOM   2935  N   ARG A 363      68.566   9.103   2.923  1.00 37.41           N  
ATOM   2936  CA  ARG A 363      67.209   8.730   2.518  1.00 32.43           C  
ATOM   2937  C   ARG A 363      67.289   7.578   1.527  1.00 31.24           C  
ATOM   2938  O   ARG A 363      68.279   7.456   0.816  1.00 26.74           O  
ATOM   2939  CB  ARG A 363      66.504   9.911   1.847  1.00 26.86           C  
ATOM   2940  CG  ARG A 363      66.271  11.117   2.728  1.00 29.70           C  
ATOM   2941  CD  ARG A 363      65.425  12.151   1.967  1.00 22.58           C  
ATOM   2942  NE  ARG A 363      65.303  13.428   2.662  1.00 28.33           N  
ATOM   2943  CZ  ARG A 363      66.203  14.405   2.603  1.00 22.19           C  
ATOM   2944  NH1 ARG A 363      67.310  14.249   1.885  1.00 23.81           N  
ATOM   2945  NH2 ARG A 363      65.975  15.551   3.237  1.00 26.88           N  
ATOM   2946  N   ALA A 364      66.242   6.750   1.475  1.00 33.91           N  
ATOM   2947  CA  ALA A 364      66.193   5.595   0.571  1.00 31.59           C  
ATOM   2948  C   ALA A 364      66.143   5.973  -0.903  1.00 31.80           C  
ATOM   2949  O   ALA A 364      66.590   5.210  -1.766  1.00 30.72           O  
ATOM   2950  CB  ALA A 364      64.987   4.707   0.910  1.00 28.27           C  
ATOM   2951  N   PHE A 365      65.585   7.142  -1.197  1.00 28.40           N  
ATOM   2952  CA  PHE A 365      65.481   7.602  -2.579  1.00 24.92           C  
ATOM   2953  C   PHE A 365      66.094   8.993  -2.724  1.00 26.25           C  
ATOM   2954  O   PHE A 365      66.158   9.744  -1.762  1.00 24.57           O  
ATOM   2955  CB  PHE A 365      64.013   7.638  -3.024  1.00 26.65           C  
ATOM   2956  CG  PHE A 365      63.324   6.310  -2.931  1.00 25.20           C  
ATOM   2957  CD1 PHE A 365      62.591   5.969  -1.800  1.00 23.08           C  
ATOM   2958  CD2 PHE A 365      63.429   5.391  -3.965  1.00 26.23           C  
ATOM   2959  CE1 PHE A 365      61.965   4.716  -1.697  1.00 22.14           C  
ATOM   2960  CE2 PHE A 365      62.810   4.138  -3.875  1.00 30.99           C  
ATOM   2961  CZ  PHE A 365      62.077   3.805  -2.737  1.00 23.72           C  
ATOM   2962  N   ARG A 366      66.533   9.332  -3.934  1.00 28.14           N  
ATOM   2963  CA  ARG A 366      67.174  10.628  -4.190  1.00 30.29           C  
ATOM   2964  C   ARG A 366      66.226  11.812  -4.239  1.00 25.38           C  
ATOM   2965  O   ARG A 366      65.151  11.728  -4.824  1.00 23.83           O  
ATOM   2966  CB  ARG A 366      67.933  10.581  -5.521  1.00 31.95           C  
ATOM   2967  CG  ARG A 366      68.942   9.448  -5.624  1.00 47.66           C  
ATOM   2968  CD  ARG A 366      69.490   9.313  -7.042  1.00 47.74           C  
ATOM   2969  NE  ARG A 366      68.415   9.063  -7.997  1.00 55.99           N  
ATOM   2970  CZ  ARG A 366      68.597   8.759  -9.277  1.00 55.67           C  
ATOM   2971  NH1 ARG A 366      69.826   8.661  -9.770  1.00 63.75           N  
ATOM   2972  NH2 ARG A 366      67.548   8.553 -10.067  1.00 54.06           N  
ATOM   2973  N   PRO A 367      66.602  12.934  -3.612  1.00 27.56           N  
ATOM   2974  CA  PRO A 367      65.690  14.081  -3.680  1.00 27.32           C  
ATOM   2975  C   PRO A 367      65.739  14.656  -5.095  1.00 23.21           C  
ATOM   2976  O   PRO A 367      66.566  14.241  -5.908  1.00 24.81           O  
ATOM   2977  CB  PRO A 367      66.234  15.032  -2.611  1.00 26.74           C  
ATOM   2978  CG  PRO A 367      67.652  14.612  -2.436  1.00 30.26           C  
ATOM   2979  CD  PRO A 367      67.599  13.125  -2.548  1.00 30.68           C  
ATOM   2980  N   PHE A 368      64.868  15.611  -5.392  1.00 24.35           N  
ATOM   2981  CA  PHE A 368      64.801  16.167  -6.737  1.00 22.33           C  
ATOM   2982  C   PHE A 368      64.359  17.617  -6.751  1.00 21.92           C  
ATOM   2983  O   PHE A 368      63.809  18.127  -5.780  1.00 21.02           O  
ATOM   2984  CB  PHE A 368      63.816  15.336  -7.586  1.00 21.38           C  
ATOM   2985  CG  PHE A 368      62.411  15.287  -7.021  1.00 27.19           C  
ATOM   2986  CD1 PHE A 368      61.422  16.148  -7.491  1.00 24.41           C  
ATOM   2987  CD2 PHE A 368      62.086  14.392  -6.001  1.00 27.00           C  
ATOM   2988  CE1 PHE A 368      60.131  16.119  -6.961  1.00 25.00           C  
ATOM   2989  CE2 PHE A 368      60.795  14.355  -5.459  1.00 23.97           C  
ATOM   2990  CZ  PHE A 368      59.814  15.218  -5.937  1.00 25.83           C  
ATOM   2991  N   ILE A 369      64.590  18.267  -7.881  1.00 22.11           N  
ATOM   2992  CA  ILE A 369      64.204  19.652  -8.062  1.00 23.28           C  
ATOM   2993  C   ILE A 369      62.916  19.713  -8.859  1.00 21.52           C  
ATOM   2994  O   ILE A 369      62.757  19.003  -9.862  1.00 22.57           O  
ATOM   2995  CB  ILE A 369      65.300  20.442  -8.841  1.00 25.59           C  
ATOM   2996  CG1 ILE A 369      66.601  20.455  -8.045  1.00 27.69           C  
ATOM   2997  CG2 ILE A 369      64.850  21.861  -9.089  1.00 24.62           C  
ATOM   2998  CD1 ILE A 369      67.802  20.930  -8.845  1.00 25.43           C  
ATOM   2999  N   GLU A 370      61.992  20.559  -8.416  1.00 24.77           N  
ATOM   3000  CA  GLU A 370      60.733  20.742  -9.120  1.00 26.79           C  
ATOM   3001  C   GLU A 370      60.267  22.167  -8.921  1.00 21.98           C  
ATOM   3002  O   GLU A 370      60.158  22.628  -7.797  1.00 22.16           O  
ATOM   3003  CB  GLU A 370      59.654  19.781  -8.609  1.00 27.98           C  
ATOM   3004  CG  GLU A 370      58.287  19.996  -9.268  1.00 29.83           C  
ATOM   3005  CD  GLU A 370      57.199  19.153  -8.614  1.00 34.53           C  
ATOM   3006  OE1 GLU A 370      57.239  17.919  -8.783  1.00 33.25           O  
ATOM   3007  OE2 GLU A 370      56.325  19.717  -7.917  1.00 35.60           O  
ATOM   3008  N   ASN A 371      59.987  22.857 -10.025  1.00 24.78           N  
ATOM   3009  CA  ASN A 371      59.550  24.252  -9.973  1.00 26.17           C  
ATOM   3010  C   ASN A 371      60.499  25.103  -9.152  1.00 21.32           C  
ATOM   3011  O   ASN A 371      60.076  25.892  -8.318  1.00 28.94           O  
ATOM   3012  CB  ASN A 371      58.128  24.365  -9.415  1.00 27.25           C  
ATOM   3013  CG  ASN A 371      57.085  23.754 -10.347  1.00 42.13           C  
ATOM   3014  OD1 ASN A 371      56.153  23.075  -9.896  1.00 44.03           O  
ATOM   3015  ND2 ASN A 371      57.236  23.992 -11.647  1.00 33.11           N  
ATOM   3016  N   GLY A 372      61.791  24.907  -9.388  1.00 25.22           N  
ATOM   3017  CA  GLY A 372      62.823  25.685  -8.726  1.00 27.23           C  
ATOM   3018  C   GLY A 372      63.100  25.383  -7.268  1.00 28.41           C  
ATOM   3019  O   GLY A 372      63.896  26.082  -6.650  1.00 26.03           O  
ATOM   3020  N   ARG A 373      62.463  24.351  -6.720  1.00 24.19           N  
ATOM   3021  CA  ARG A 373      62.658  23.996  -5.318  1.00 25.24           C  
ATOM   3022  C   ARG A 373      63.048  22.524  -5.132  1.00 25.47           C  
ATOM   3023  O   ARG A 373      62.702  21.655  -5.941  1.00 23.81           O  
ATOM   3024  CB  ARG A 373      61.370  24.301  -4.539  1.00 31.27           C  
ATOM   3025  CG  ARG A 373      61.377  23.917  -3.073  1.00 31.51           C  
ATOM   3026  CD  ARG A 373      60.021  24.229  -2.457  1.00 32.40           C  
ATOM   3027  NE  ARG A 373      59.723  25.660  -2.457  1.00 36.56           N  
ATOM   3028  CZ  ARG A 373      60.144  26.525  -1.532  1.00 36.93           C  
ATOM   3029  NH1 ARG A 373      60.893  26.123  -0.512  1.00 29.39           N  
ATOM   3030  NH2 ARG A 373      59.791  27.801  -1.615  1.00 40.00           N  
ATOM   3031  N   TRP A 374      63.787  22.238  -4.072  1.00 27.83           N  
ATOM   3032  CA  TRP A 374      64.156  20.854  -3.812  1.00 26.75           C  
ATOM   3033  C   TRP A 374      63.032  20.148  -3.065  1.00 25.28           C  
ATOM   3034  O   TRP A 374      62.288  20.767  -2.301  1.00 23.67           O  
ATOM   3035  CB  TRP A 374      65.442  20.766  -2.990  1.00 22.89           C  
ATOM   3036  CG  TRP A 374      66.682  20.957  -3.804  1.00 26.53           C  
ATOM   3037  CD1 TRP A 374      67.363  22.130  -4.012  1.00 19.08           C  
ATOM   3038  CD2 TRP A 374      67.425  19.939  -4.487  1.00 27.19           C  
ATOM   3039  NE1 TRP A 374      68.478  21.897  -4.765  1.00 22.04           N  
ATOM   3040  CE2 TRP A 374      68.551  20.565  -5.069  1.00 24.47           C  
ATOM   3041  CE3 TRP A 374      67.251  18.558  -4.660  1.00 22.90           C  
ATOM   3042  CZ2 TRP A 374      69.507  19.857  -5.811  1.00 26.65           C  
ATOM   3043  CZ3 TRP A 374      68.195  17.856  -5.392  1.00 22.38           C  
ATOM   3044  CH2 TRP A 374      69.314  18.507  -5.960  1.00 22.86           C  
ATOM   3045  N   TRP A 375      62.906  18.851  -3.313  1.00 22.05           N  
ATOM   3046  CA  TRP A 375      61.909  18.018  -2.657  1.00 23.03           C  
ATOM   3047  C   TRP A 375      62.559  16.670  -2.386  1.00 20.24           C  
ATOM   3048  O   TRP A 375      63.520  16.296  -3.053  1.00 23.56           O  
ATOM   3049  CB  TRP A 375      60.682  17.782  -3.551  1.00 24.20           C  
ATOM   3050  CG  TRP A 375      59.863  19.002  -3.810  1.00 23.09           C  
ATOM   3051  CD1 TRP A 375      60.119  19.981  -4.724  1.00 26.25           C  
ATOM   3052  CD2 TRP A 375      58.671  19.392  -3.129  1.00 25.18           C  
ATOM   3053  NE1 TRP A 375      59.163  20.959  -4.651  1.00 25.33           N  
ATOM   3054  CE2 TRP A 375      58.262  20.627  -3.675  1.00 27.52           C  
ATOM   3055  CE3 TRP A 375      57.909  18.824  -2.100  1.00 26.51           C  
ATOM   3056  CZ2 TRP A 375      57.124  21.298  -3.243  1.00 23.99           C  
ATOM   3057  CZ3 TRP A 375      56.778  19.491  -1.668  1.00 32.29           C  
ATOM   3058  CH2 TRP A 375      56.398  20.721  -2.237  1.00 31.12           C  
ATOM   3059  N   ALA A 376      62.050  15.955  -1.394  1.00 22.11           N  
ATOM   3060  CA  ALA A 376      62.568  14.631  -1.094  1.00 24.64           C  
ATOM   3061  C   ALA A 376      61.427  13.685  -0.772  1.00 26.07           C  
ATOM   3062  O   ALA A 376      60.413  14.090  -0.192  1.00 25.58           O  
ATOM   3063  CB  ALA A 376      63.523  14.684   0.094  1.00 29.90           C  
ATOM   3064  N   PHE A 377      61.601  12.431  -1.168  1.00 24.01           N  
ATOM   3065  CA  PHE A 377      60.645  11.384  -0.854  1.00 26.76           C  
ATOM   3066  C   PHE A 377      61.091  10.911   0.525  1.00 23.42           C  
ATOM   3067  O   PHE A 377      62.268  10.617   0.733  1.00 24.38           O  
ATOM   3068  CB  PHE A 377      60.762  10.232  -1.851  1.00 25.05           C  
ATOM   3069  CG  PHE A 377      60.297  10.579  -3.242  1.00 26.03           C  
ATOM   3070  CD1 PHE A 377      61.153  10.450  -4.327  1.00 26.92           C  
ATOM   3071  CD2 PHE A 377      58.995  11.034  -3.459  1.00 22.54           C  
ATOM   3072  CE1 PHE A 377      60.722  10.765  -5.620  1.00 28.95           C  
ATOM   3073  CE2 PHE A 377      58.556  11.348  -4.733  1.00 16.35           C  
ATOM   3074  CZ  PHE A 377      59.419  11.216  -5.818  1.00 24.66           C  
ATOM   3075  N   GLU A 378      60.157  10.893   1.467  1.00 26.33           N  
ATOM   3076  CA  GLU A 378      60.417  10.446   2.823  1.00 27.73           C  
ATOM   3077  C   GLU A 378      59.291   9.512   3.218  1.00 28.41           C  
ATOM   3078  O   GLU A 378      58.286   9.431   2.512  1.00 26.42           O  
ATOM   3079  CB  GLU A 378      60.531  11.642   3.774  1.00 26.43           C  
ATOM   3080  CG  GLU A 378      61.898  12.331   3.663  1.00 26.78           C  
ATOM   3081  CD  GLU A 378      62.036  13.546   4.561  1.00 32.87           C  
ATOM   3082  OE1 GLU A 378      61.133  13.782   5.399  1.00 24.28           O  
ATOM   3083  OE2 GLU A 378      63.056  14.262   4.420  1.00 29.43           O  
ATOM   3084  N   MET A 379      59.457   8.810   4.339  1.00 25.65           N  
ATOM   3085  CA  MET A 379      58.471   7.832   4.786  1.00 26.90           C  
ATOM   3086  C   MET A 379      57.584   8.250   5.950  1.00 21.86           C  
ATOM   3087  O   MET A 379      58.074   8.734   6.947  1.00 27.34           O  
ATOM   3088  CB  MET A 379      59.180   6.521   5.178  1.00 27.47           C  
ATOM   3089  CG  MET A 379      60.104   5.952   4.116  1.00 35.81           C  
ATOM   3090  SD  MET A 379      59.260   5.629   2.558  1.00 40.79           S  
ATOM   3091  CE  MET A 379      59.178   3.798   2.558  1.00 47.67           C  
ATOM   3092  N   ARG A 380      56.280   8.034   5.812  1.00 20.95           N  
ATOM   3093  CA  ARG A 380      55.311   8.326   6.867  1.00 18.35           C  
ATOM   3094  C   ARG A 380      55.536   7.326   7.992  1.00 25.24           C  
ATOM   3095  O   ARG A 380      56.075   6.246   7.762  1.00 24.32           O  
ATOM   3096  CB  ARG A 380      53.882   8.116   6.359  1.00 19.58           C  
ATOM   3097  CG  ARG A 380      53.400   9.125   5.327  1.00 23.97           C  
ATOM   3098  CD  ARG A 380      51.900   8.947   5.040  1.00 24.59           C  
ATOM   3099  NE  ARG A 380      51.410  10.126   4.347  1.00 27.12           N  
ATOM   3100  CZ  ARG A 380      51.605  10.371   3.061  1.00 23.36           C  
ATOM   3101  NH1 ARG A 380      52.262   9.499   2.314  1.00 21.43           N  
ATOM   3102  NH2 ARG A 380      51.197  11.520   2.541  1.00 23.88           N  
ATOM   3103  N   LYS A 381      55.093   7.671   9.196  1.00 25.91           N  
ATOM   3104  CA  LYS A 381      55.230   6.781  10.333  1.00 26.64           C  
ATOM   3105  C   LYS A 381      53.942   6.007  10.576  1.00 23.13           C  
ATOM   3106  O   LYS A 381      53.827   5.299  11.564  1.00 26.87           O  
ATOM   3107  CB  LYS A 381      55.626   7.558  11.588  1.00 27.83           C  
ATOM   3108  CG  LYS A 381      57.036   8.132  11.508  1.00 37.39           C  
ATOM   3109  CD  LYS A 381      57.473   8.772  12.821  1.00 38.16           C  
ATOM   3110  CE  LYS A 381      58.880   9.324  12.695  1.00 39.39           C  
ATOM   3111  NZ  LYS A 381      58.976  10.279  11.557  1.00 38.18           N  
ATOM   3112  N   PHE A 382      52.974   6.168   9.677  1.00 21.72           N  
ATOM   3113  CA  PHE A 382      51.697   5.454   9.739  1.00 22.54           C  
ATOM   3114  C   PHE A 382      51.062   5.508   8.358  1.00 24.56           C  
ATOM   3115  O   PHE A 382      51.320   6.434   7.594  1.00 25.87           O  
ATOM   3116  CB  PHE A 382      50.744   6.043  10.790  1.00 19.82           C  
ATOM   3117  CG  PHE A 382      50.694   7.549  10.815  1.00 24.24           C  
ATOM   3118  CD1 PHE A 382      50.031   8.265   9.819  1.00 28.61           C  
ATOM   3119  CD2 PHE A 382      51.278   8.247  11.864  1.00 22.00           C  
ATOM   3120  CE1 PHE A 382      49.949   9.667   9.873  1.00 30.68           C  
ATOM   3121  CE2 PHE A 382      51.204   9.642  11.932  1.00 27.55           C  
ATOM   3122  CZ  PHE A 382      50.537  10.355  10.933  1.00 34.25           C  
ATOM   3123  N   THR A 383      50.236   4.523   8.033  1.00 24.55           N  
ATOM   3124  CA  THR A 383      49.613   4.506   6.712  1.00 21.87           C  
ATOM   3125  C   THR A 383      48.103   4.351   6.744  1.00 18.80           C  
ATOM   3126  O   THR A 383      47.453   4.378   5.695  1.00 25.30           O  
ATOM   3127  CB  THR A 383      50.207   3.392   5.815  1.00 26.45           C  
ATOM   3128  OG1 THR A 383      49.978   2.119   6.423  1.00 23.88           O  
ATOM   3129  CG2 THR A 383      51.719   3.606   5.587  1.00 27.66           C  
ATOM   3130  N   THR A 384      47.527   4.179   7.930  1.00 17.88           N  
ATOM   3131  CA  THR A 384      46.078   4.085   8.031  1.00 18.43           C  
ATOM   3132  C   THR A 384      45.594   5.176   8.981  1.00 19.99           C  
ATOM   3133  O   THR A 384      46.344   5.666   9.820  1.00 16.90           O  
ATOM   3134  CB  THR A 384      45.588   2.715   8.569  1.00 19.07           C  
ATOM   3135  OG1 THR A 384      46.012   2.548   9.933  1.00 23.56           O  
ATOM   3136  CG2 THR A 384      46.140   1.557   7.702  1.00 15.22           C  
ATOM   3137  N   PRO A 385      44.332   5.588   8.847  1.00 21.30           N  
ATOM   3138  CA  PRO A 385      43.872   6.631   9.769  1.00 23.61           C  
ATOM   3139  C   PRO A 385      43.886   6.125  11.229  1.00 25.29           C  
ATOM   3140  O   PRO A 385      44.108   6.901  12.158  1.00 19.65           O  
ATOM   3141  CB  PRO A 385      42.480   6.981   9.223  1.00 19.40           C  
ATOM   3142  CG  PRO A 385      42.061   5.740   8.495  1.00 19.30           C  
ATOM   3143  CD  PRO A 385      43.320   5.290   7.818  1.00 19.87           C  
ATOM   3144  N   GLU A 386      43.652   4.827  11.429  1.00 19.39           N  
ATOM   3145  CA  GLU A 386      43.697   4.259  12.779  1.00 18.67           C  
ATOM   3146  C   GLU A 386      45.100   4.418  13.384  1.00 16.69           C  
ATOM   3147  O   GLU A 386      45.241   4.766  14.553  1.00 19.63           O  
ATOM   3148  CB  GLU A 386      43.346   2.755  12.775  1.00 20.24           C  
ATOM   3149  CG  GLU A 386      41.897   2.403  12.431  1.00 22.14           C  
ATOM   3150  CD  GLU A 386      41.644   2.246  10.932  1.00 32.86           C  
ATOM   3151  OE1 GLU A 386      40.618   1.625  10.597  1.00 33.69           O  
ATOM   3152  OE2 GLU A 386      42.436   2.735  10.086  1.00 23.26           O  
ATOM   3153  N   GLU A 387      46.130   4.132  12.594  1.00 17.78           N  
ATOM   3154  CA  GLU A 387      47.509   4.256  13.064  1.00 19.43           C  
ATOM   3155  C   GLU A 387      47.845   5.721  13.305  1.00 20.25           C  
ATOM   3156  O   GLU A 387      48.591   6.055  14.225  1.00 19.87           O  
ATOM   3157  CB  GLU A 387      48.473   3.666  12.043  1.00 19.45           C  
ATOM   3158  CG  GLU A 387      48.422   2.150  12.001  1.00 26.73           C  
ATOM   3159  CD  GLU A 387      49.212   1.587  10.838  1.00 32.98           C  
ATOM   3160  OE1 GLU A 387      49.593   0.397  10.913  1.00 26.46           O  
ATOM   3161  OE2 GLU A 387      49.442   2.338   9.854  1.00 24.29           O  
ATOM   3162  N   GLY A 388      47.304   6.592  12.459  1.00 20.72           N  
ATOM   3163  CA  GLY A 388      47.545   8.011  12.633  1.00 20.44           C  
ATOM   3164  C   GLY A 388      46.972   8.465  13.967  1.00 22.75           C  
ATOM   3165  O   GLY A 388      47.638   9.185  14.713  1.00 23.59           O  
ATOM   3166  N   VAL A 389      45.743   8.052  14.279  1.00 20.61           N  
ATOM   3167  CA  VAL A 389      45.137   8.459  15.539  1.00 21.67           C  
ATOM   3168  C   VAL A 389      45.828   7.820  16.746  1.00 19.63           C  
ATOM   3169  O   VAL A 389      45.934   8.433  17.795  1.00 21.51           O  
ATOM   3170  CB  VAL A 389      43.610   8.185  15.539  1.00 23.86           C  
ATOM   3171  CG1 VAL A 389      42.976   8.581  16.895  1.00 19.59           C  
ATOM   3172  CG2 VAL A 389      42.968   9.026  14.447  1.00 18.98           C  
ATOM   3173  N   ARG A 390      46.296   6.589  16.625  1.00 21.57           N  
ATOM   3174  CA  ARG A 390      47.012   5.988  17.760  1.00 18.60           C  
ATOM   3175  C   ARG A 390      48.194   6.894  18.112  1.00 18.14           C  
ATOM   3176  O   ARG A 390      48.506   7.146  19.291  1.00 18.92           O  
ATOM   3177  CB  ARG A 390      47.537   4.598  17.393  1.00 18.87           C  
ATOM   3178  CG  ARG A 390      48.452   3.977  18.452  1.00 23.34           C  
ATOM   3179  CD  ARG A 390      48.913   2.575  18.028  1.00 25.46           C  
ATOM   3180  NE  ARG A 390      49.711   2.632  16.811  1.00 26.88           N  
ATOM   3181  CZ  ARG A 390      49.873   1.631  15.948  1.00 26.93           C  
ATOM   3182  NH1 ARG A 390      49.294   0.444  16.139  1.00 26.27           N  
ATOM   3183  NH2 ARG A 390      50.616   1.829  14.875  1.00 25.19           N  
ATOM   3184  N   SER A 391      48.862   7.387  17.082  1.00 22.17           N  
ATOM   3185  CA  SER A 391      50.015   8.252  17.290  1.00 22.93           C  
ATOM   3186  C   SER A 391      49.606   9.587  17.901  1.00 23.34           C  
ATOM   3187  O   SER A 391      50.173  10.035  18.897  1.00 23.48           O  
ATOM   3188  CB  SER A 391      50.733   8.489  15.967  1.00 22.31           C  
ATOM   3189  OG  SER A 391      51.827   9.375  16.130  1.00 24.49           O  
ATOM   3190  N   TYR A 392      48.608  10.221  17.305  1.00 23.57           N  
ATOM   3191  CA  TYR A 392      48.150  11.513  17.796  1.00 21.98           C  
ATOM   3192  C   TYR A 392      47.659  11.478  19.251  1.00 24.43           C  
ATOM   3193  O   TYR A 392      48.045  12.319  20.060  1.00 22.35           O  
ATOM   3194  CB  TYR A 392      47.035  12.047  16.880  1.00 24.21           C  
ATOM   3195  CG  TYR A 392      46.636  13.467  17.191  1.00 24.14           C  
ATOM   3196  CD1 TYR A 392      47.358  14.549  16.676  1.00 23.92           C  
ATOM   3197  CD2 TYR A 392      45.562  13.734  18.048  1.00 29.80           C  
ATOM   3198  CE1 TYR A 392      47.019  15.883  17.012  1.00 22.62           C  
ATOM   3199  CE2 TYR A 392      45.222  15.055  18.387  1.00 34.33           C  
ATOM   3200  CZ  TYR A 392      45.959  16.119  17.863  1.00 27.07           C  
ATOM   3201  OH  TYR A 392      45.626  17.409  18.228  1.00 28.90           O  
ATOM   3202  N   ALA A 393      46.809  10.506  19.584  1.00 22.83           N  
ATOM   3203  CA  ALA A 393      46.257  10.394  20.935  1.00 24.65           C  
ATOM   3204  C   ALA A 393      47.311  10.015  21.972  1.00 26.47           C  
ATOM   3205  O   ALA A 393      47.125  10.282  23.150  1.00 20.92           O  
ATOM   3206  CB  ALA A 393      45.118   9.366  20.965  1.00 22.68           C  
ATOM   3207  N   SER A 394      48.394   9.378  21.530  1.00 21.38           N  
ATOM   3208  CA  SER A 394      49.472   8.981  22.430  1.00 27.96           C  
ATOM   3209  C   SER A 394      50.364  10.157  22.842  1.00 22.37           C  
ATOM   3210  O   SER A 394      50.905  10.159  23.939  1.00 23.51           O  
ATOM   3211  CB  SER A 394      50.359   7.913  21.779  1.00 25.29           C  
ATOM   3212  OG  SER A 394      49.656   6.687  21.630  1.00 26.44           O  
ATOM   3213  N   THR A 395      50.521  11.151  21.974  1.00 22.54           N  
ATOM   3214  CA  THR A 395      51.394  12.277  22.309  1.00 23.71           C  
ATOM   3215  C   THR A 395      50.713  13.632  22.365  1.00 29.06           C  
ATOM   3216  O   THR A 395      51.248  14.574  22.966  1.00 30.41           O  
ATOM   3217  CB  THR A 395      52.576  12.373  21.320  1.00 28.01           C  
ATOM   3218  OG1 THR A 395      52.075  12.532  19.987  1.00 32.62           O  
ATOM   3219  CG2 THR A 395      53.443  11.104  21.403  1.00 31.80           C  
ATOM   3220  N   HIS A 396      49.538  13.743  21.749  1.00 23.62           N  
ATOM   3221  CA  HIS A 396      48.826  15.013  21.743  1.00 22.25           C  
ATOM   3222  C   HIS A 396      47.504  15.004  22.494  1.00 25.13           C  
ATOM   3223  O   HIS A 396      46.609  15.784  22.179  1.00 24.87           O  
ATOM   3224  CB  HIS A 396      48.609  15.487  20.311  1.00 27.79           C  
ATOM   3225  CG  HIS A 396      49.870  15.903  19.623  1.00 34.95           C  
ATOM   3226  ND1 HIS A 396      50.667  15.022  18.924  1.00 36.91           N  
ATOM   3227  CD2 HIS A 396      50.504  17.101  19.568  1.00 33.38           C  
ATOM   3228  CE1 HIS A 396      51.731  15.656  18.470  1.00 37.15           C  
ATOM   3229  NE2 HIS A 396      51.656  16.920  18.850  1.00 36.54           N  
ATOM   3230  N   TRP A 397      47.397  14.125  23.493  1.00 22.28           N  
ATOM   3231  CA  TRP A 397      46.195  14.019  24.315  1.00 24.05           C  
ATOM   3232  C   TRP A 397      45.889  15.315  25.069  1.00 23.28           C  
ATOM   3233  O   TRP A 397      44.756  15.530  25.496  1.00 22.08           O  
ATOM   3234  CB  TRP A 397      46.346  12.895  25.339  1.00 26.19           C  
ATOM   3235  CG  TRP A 397      47.702  12.877  26.009  1.00 34.63           C  
ATOM   3236  CD1 TRP A 397      48.800  12.154  25.621  1.00 39.13           C  
ATOM   3237  CD2 TRP A 397      48.117  13.650  27.145  1.00 35.25           C  
ATOM   3238  NE1 TRP A 397      49.867  12.429  26.442  1.00 36.11           N  
ATOM   3239  CE2 TRP A 397      49.478  13.342  27.385  1.00 38.13           C  
ATOM   3240  CE3 TRP A 397      47.475  14.571  27.981  1.00 37.04           C  
ATOM   3241  CZ2 TRP A 397      50.209  13.927  28.432  1.00 40.63           C  
ATOM   3242  CZ3 TRP A 397      48.203  15.154  29.025  1.00 40.71           C  
ATOM   3243  CH2 TRP A 397      49.557  14.827  29.238  1.00 39.87           C  
ATOM   3244  N   HIS A 398      46.894  16.171  25.236  1.00 22.06           N  
ATOM   3245  CA  HIS A 398      46.699  17.430  25.947  1.00 28.50           C  
ATOM   3246  C   HIS A 398      45.792  18.376  25.193  1.00 29.17           C  
ATOM   3247  O   HIS A 398      45.190  19.273  25.785  1.00 27.49           O  
ATOM   3248  CB  HIS A 398      48.050  18.114  26.223  1.00 28.94           C  
ATOM   3249  CG  HIS A 398      48.916  18.266  25.013  1.00 31.73           C  
ATOM   3250  ND1 HIS A 398      48.941  19.417  24.250  1.00 38.44           N  
ATOM   3251  CD2 HIS A 398      49.774  17.403  24.416  1.00 31.97           C  
ATOM   3252  CE1 HIS A 398      49.773  19.255  23.238  1.00 38.67           C  
ATOM   3253  NE2 HIS A 398      50.292  18.040  23.315  1.00 38.34           N  
ATOM   3254  N   THR A 399      45.689  18.179  23.886  1.00 26.21           N  
ATOM   3255  CA  THR A 399      44.839  19.039  23.066  1.00 31.68           C  
ATOM   3256  C   THR A 399      43.377  18.573  23.055  1.00 27.45           C  
ATOM   3257  O   THR A 399      42.512  19.230  22.471  1.00 21.43           O  
ATOM   3258  CB  THR A 399      45.305  19.045  21.593  1.00 31.42           C  
ATOM   3259  OG1 THR A 399      45.032  17.764  21.000  1.00 30.74           O  
ATOM   3260  CG2 THR A 399      46.780  19.326  21.506  1.00 37.11           C  
ATOM   3261  N   LEU A 400      43.112  17.444  23.707  1.00 25.79           N  
ATOM   3262  CA  LEU A 400      41.783  16.832  23.700  1.00 27.52           C  
ATOM   3263  C   LEU A 400      40.858  17.202  24.845  1.00 26.12           C  
ATOM   3264  O   LEU A 400      39.907  16.483  25.128  1.00 25.56           O  
ATOM   3265  CB  LEU A 400      41.949  15.302  23.655  1.00 23.12           C  
ATOM   3266  CG  LEU A 400      42.870  14.814  22.521  1.00 22.37           C  
ATOM   3267  CD1 LEU A 400      42.932  13.269  22.527  1.00 22.90           C  
ATOM   3268  CD2 LEU A 400      42.341  15.310  21.179  1.00 21.67           C  
ATOM   3269  N   GLY A 401      41.118  18.334  25.491  1.00 29.24           N  
ATOM   3270  CA  GLY A 401      40.298  18.717  26.631  1.00 26.31           C  
ATOM   3271  C   GLY A 401      41.066  18.272  27.858  1.00 23.73           C  
ATOM   3272  O   GLY A 401      41.699  17.222  27.837  1.00 26.69           O  
ATOM   3273  N   LYS A 402      41.014  19.062  28.926  1.00 27.65           N  
ATOM   3274  CA  LYS A 402      41.742  18.759  30.157  1.00 31.84           C  
ATOM   3275  C   LYS A 402      41.502  17.365  30.758  1.00 31.84           C  
ATOM   3276  O   LYS A 402      42.454  16.626  31.041  1.00 26.69           O  
ATOM   3277  CB  LYS A 402      41.425  19.825  31.218  1.00 40.01           C  
ATOM   3278  CG  LYS A 402      42.240  19.722  32.506  1.00 45.64           C  
ATOM   3279  CD  LYS A 402      41.803  20.802  33.504  1.00 52.24           C  
ATOM   3280  CE  LYS A 402      42.471  20.651  34.867  1.00 55.84           C  
ATOM   3281  NZ  LYS A 402      43.955  20.844  34.824  1.00 49.40           N  
ATOM   3282  N   ASN A 403      40.241  17.004  30.945  1.00 24.92           N  
ATOM   3283  CA  ASN A 403      39.915  15.721  31.554  1.00 25.42           C  
ATOM   3284  C   ASN A 403      39.845  14.586  30.544  1.00 26.37           C  
ATOM   3285  O   ASN A 403      40.270  13.463  30.837  1.00 26.18           O  
ATOM   3286  CB  ASN A 403      38.607  15.845  32.328  1.00 24.88           C  
ATOM   3287  CG  ASN A 403      38.653  16.975  33.333  1.00 30.09           C  
ATOM   3288  OD1 ASN A 403      39.397  16.920  34.312  1.00 32.08           O  
ATOM   3289  ND2 ASN A 403      37.882  18.014  33.082  1.00 27.48           N  
ATOM   3290  N   VAL A 404      39.301  14.860  29.364  1.00 23.79           N  
ATOM   3291  CA  VAL A 404      39.260  13.832  28.331  1.00 21.10           C  
ATOM   3292  C   VAL A 404      40.709  13.458  27.963  1.00 20.98           C  
ATOM   3293  O   VAL A 404      41.052  12.279  27.857  1.00 23.20           O  
ATOM   3294  CB  VAL A 404      38.505  14.330  27.084  1.00 25.31           C  
ATOM   3295  CG1 VAL A 404      38.810  13.429  25.896  1.00 22.75           C  
ATOM   3296  CG2 VAL A 404      37.011  14.343  27.363  1.00 20.30           C  
ATOM   3297  N   GLY A 405      41.568  14.461  27.789  1.00 23.09           N  
ATOM   3298  CA  GLY A 405      42.956  14.179  27.460  1.00 24.80           C  
ATOM   3299  C   GLY A 405      43.677  13.360  28.529  1.00 24.39           C  
ATOM   3300  O   GLY A 405      44.451  12.454  28.214  1.00 26.59           O  
ATOM   3301  N   GLU A 406      43.423  13.669  29.796  1.00 25.27           N  
ATOM   3302  CA  GLU A 406      44.057  12.949  30.899  1.00 25.81           C  
ATOM   3303  C   GLU A 406      43.615  11.488  30.954  1.00 28.16           C  
ATOM   3304  O   GLU A 406      44.395  10.601  31.303  1.00 27.21           O  
ATOM   3305  CB  GLU A 406      43.745  13.634  32.231  1.00 27.45           C  
ATOM   3306  CG  GLU A 406      44.248  12.862  33.439  1.00 44.99           C  
ATOM   3307  CD  GLU A 406      45.762  12.940  33.617  1.00 52.14           C  
ATOM   3308  OE1 GLU A 406      46.293  12.187  34.466  1.00 53.96           O  
ATOM   3309  OE2 GLU A 406      46.413  13.760  32.924  1.00 51.31           O  
ATOM   3310  N   SER A 407      42.358  11.228  30.616  1.00 28.33           N  
ATOM   3311  CA  SER A 407      41.866   9.855  30.620  1.00 26.12           C  
ATOM   3312  C   SER A 407      42.550   9.093  29.482  1.00 27.20           C  
ATOM   3313  O   SER A 407      43.041   7.971  29.667  1.00 25.87           O  
ATOM   3314  CB  SER A 407      40.348   9.843  30.429  1.00 28.53           C  
ATOM   3315  OG  SER A 407      39.854   8.522  30.396  1.00 35.21           O  
ATOM   3316  N   ILE A 408      42.589   9.717  28.309  1.00 21.75           N  
ATOM   3317  CA  ILE A 408      43.214   9.118  27.136  1.00 27.23           C  
ATOM   3318  C   ILE A 408      44.704   8.888  27.369  1.00 28.13           C  
ATOM   3319  O   ILE A 408      45.284   7.943  26.844  1.00 22.69           O  
ATOM   3320  CB  ILE A 408      42.954   9.997  25.893  1.00 22.77           C  
ATOM   3321  CG1 ILE A 408      41.481   9.803  25.483  1.00 19.85           C  
ATOM   3322  CG2 ILE A 408      43.928   9.659  24.741  1.00 21.80           C  
ATOM   3323  CD1 ILE A 408      41.027  10.678  24.319  1.00 22.29           C  
ATOM   3324  N   ARG A 409      45.312   9.750  28.176  1.00 29.41           N  
ATOM   3325  CA  ARG A 409      46.724   9.608  28.502  1.00 27.44           C  
ATOM   3326  C   ARG A 409      46.917   8.292  29.239  1.00 28.52           C  
ATOM   3327  O   ARG A 409      47.874   7.569  28.984  1.00 26.08           O  
ATOM   3328  CB  ARG A 409      47.185  10.759  29.389  1.00 32.39           C  
ATOM   3329  CG  ARG A 409      48.612  10.606  29.901  1.00 38.42           C  
ATOM   3330  CD  ARG A 409      48.993  11.800  30.759  1.00 44.11           C  
ATOM   3331  NE  ARG A 409      50.376  11.735  31.213  1.00 53.18           N  
ATOM   3332  CZ  ARG A 409      50.975  12.693  31.915  1.00 57.82           C  
ATOM   3333  NH1 ARG A 409      50.307  13.793  32.245  1.00 63.04           N  
ATOM   3334  NH2 ARG A 409      52.242  12.553  32.284  1.00 59.46           N  
ATOM   3335  N   GLU A 410      45.986   7.976  30.133  1.00 24.05           N  
ATOM   3336  CA  GLU A 410      46.050   6.750  30.914  1.00 26.52           C  
ATOM   3337  C   GLU A 410      45.690   5.499  30.122  1.00 31.12           C  
ATOM   3338  O   GLU A 410      46.273   4.432  30.336  1.00 24.70           O  
ATOM   3339  CB  GLU A 410      45.106   6.828  32.113  1.00 30.48           C  
ATOM   3340  CG  GLU A 410      45.508   7.813  33.186  1.00 41.93           C  
ATOM   3341  CD  GLU A 410      44.390   8.058  34.187  1.00 49.80           C  
ATOM   3342  OE1 GLU A 410      43.906   7.082  34.803  1.00 53.82           O  
ATOM   3343  OE2 GLU A 410      43.998   9.233  34.360  1.00 51.85           O  
ATOM   3344  N   TYR A 411      44.711   5.623  29.229  1.00 26.59           N  
ATOM   3345  CA  TYR A 411      44.264   4.481  28.446  1.00 27.43           C  
ATOM   3346  C   TYR A 411      43.272   4.836  27.360  1.00 25.69           C  
ATOM   3347  O   TYR A 411      42.363   5.649  27.564  1.00 24.51           O  
ATOM   3348  CB  TYR A 411      43.613   3.434  29.364  1.00 29.40           C  
ATOM   3349  CG  TYR A 411      42.571   2.577  28.670  1.00 34.59           C  
ATOM   3350  CD1 TYR A 411      42.938   1.508  27.849  1.00 39.57           C  
ATOM   3351  CD2 TYR A 411      41.222   2.907  28.751  1.00 31.71           C  
ATOM   3352  CE1 TYR A 411      41.972   0.793  27.124  1.00 37.66           C  
ATOM   3353  CE2 TYR A 411      40.267   2.221  28.041  1.00 36.89           C  
ATOM   3354  CZ  TYR A 411      40.639   1.173  27.220  1.00 43.53           C  
ATOM   3355  OH  TYR A 411      39.661   0.558  26.469  1.00 50.55           O  
ATOM   3356  N   PHE A 412      43.472   4.224  26.203  1.00 23.33           N  
ATOM   3357  CA  PHE A 412      42.569   4.383  25.067  1.00 26.99           C  
ATOM   3358  C   PHE A 412      42.825   3.210  24.131  1.00 26.48           C  
ATOM   3359  O   PHE A 412      43.850   2.537  24.231  1.00 23.89           O  
ATOM   3360  CB  PHE A 412      42.823   5.707  24.329  1.00 16.22           C  
ATOM   3361  CG  PHE A 412      44.006   5.685  23.392  1.00 24.85           C  
ATOM   3362  CD1 PHE A 412      43.870   5.234  22.081  1.00 23.07           C  
ATOM   3363  CD2 PHE A 412      45.256   6.149  23.811  1.00 25.22           C  
ATOM   3364  CE1 PHE A 412      44.950   5.253  21.204  1.00 23.95           C  
ATOM   3365  CE2 PHE A 412      46.343   6.167  22.937  1.00 23.01           C  
ATOM   3366  CZ  PHE A 412      46.190   5.723  21.639  1.00 20.71           C  
ATOM   3367  N   GLU A 413      41.872   2.936  23.256  1.00 23.50           N  
ATOM   3368  CA  GLU A 413      42.069   1.900  22.262  1.00 28.14           C  
ATOM   3369  C   GLU A 413      41.338   2.344  21.014  1.00 27.56           C  
ATOM   3370  O   GLU A 413      40.363   3.099  21.100  1.00 25.35           O  
ATOM   3371  CB  GLU A 413      41.573   0.527  22.748  1.00 33.15           C  
ATOM   3372  CG  GLU A 413      40.213   0.495  23.399  1.00 40.08           C  
ATOM   3373  CD  GLU A 413      39.805  -0.923  23.794  1.00 49.32           C  
ATOM   3374  OE1 GLU A 413      38.998  -1.065  24.744  1.00 44.67           O  
ATOM   3375  OE2 GLU A 413      40.282  -1.888  23.147  1.00 36.38           O  
ATOM   3376  N   ILE A 414      41.837   1.927  19.854  1.00 22.45           N  
ATOM   3377  CA  ILE A 414      41.191   2.274  18.603  1.00 23.67           C  
ATOM   3378  C   ILE A 414      40.454   1.013  18.192  1.00 29.46           C  
ATOM   3379  O   ILE A 414      41.068  -0.047  18.044  1.00 28.04           O  
ATOM   3380  CB  ILE A 414      42.193   2.619  17.491  1.00 29.47           C  
ATOM   3381  CG1 ILE A 414      43.171   3.698  17.966  1.00 30.32           C  
ATOM   3382  CG2 ILE A 414      41.422   3.109  16.256  1.00 20.57           C  
ATOM   3383  CD1 ILE A 414      42.481   4.961  18.419  1.00 32.25           C  
ATOM   3384  N   ILE A 415      39.145   1.113  18.028  1.00 22.33           N  
ATOM   3385  CA  ILE A 415      38.385  -0.056  17.643  1.00 27.67           C  
ATOM   3386  C   ILE A 415      37.679   0.141  16.320  1.00 29.73           C  
ATOM   3387  O   ILE A 415      37.282   1.254  15.969  1.00 26.12           O  
ATOM   3388  CB  ILE A 415      37.358  -0.416  18.721  1.00 29.77           C  
ATOM   3389  CG1 ILE A 415      36.501   0.809  19.042  1.00 33.52           C  
ATOM   3390  CG2 ILE A 415      38.071  -0.874  19.986  1.00 27.82           C  
ATOM   3391  CD1 ILE A 415      35.598   0.613  20.229  1.00 43.34           C  
ATOM   3392  N   SER A 416      37.539  -0.958  15.591  1.00 30.20           N  
ATOM   3393  CA  SER A 416      36.871  -0.963  14.303  1.00 35.75           C  
ATOM   3394  C   SER A 416      36.198  -2.314  14.090  1.00 34.25           C  
ATOM   3395  O   SER A 416      36.317  -3.215  14.919  1.00 32.74           O  
ATOM   3396  CB  SER A 416      37.883  -0.722  13.190  1.00 33.01           C  
ATOM   3397  OG  SER A 416      38.903  -1.699  13.235  1.00 35.15           O  
ATOM   3398  N   GLY A 417      35.480  -2.432  12.980  1.00 38.51           N  
ATOM   3399  CA  GLY A 417      34.811  -3.672  12.640  1.00 38.40           C  
ATOM   3400  C   GLY A 417      33.776  -4.161  13.630  1.00 44.32           C  
ATOM   3401  O   GLY A 417      33.190  -3.385  14.403  1.00 40.33           O  
ATOM   3402  N   GLU A 418      33.559  -5.474  13.604  1.00 41.86           N  
ATOM   3403  CA  GLU A 418      32.593  -6.119  14.475  1.00 43.67           C  
ATOM   3404  C   GLU A 418      32.816  -5.725  15.922  1.00 41.78           C  
ATOM   3405  O   GLU A 418      31.867  -5.589  16.690  1.00 42.45           O  
ATOM   3406  CB  GLU A 418      32.688  -7.640  14.324  1.00 55.96           C  
ATOM   3407  CG  GLU A 418      31.689  -8.406  15.166  1.00 62.07           C  
ATOM   3408  CD  GLU A 418      31.707  -9.891  14.865  1.00 71.46           C  
ATOM   3409  OE1 GLU A 418      32.776 -10.390  14.441  1.00 76.65           O  
ATOM   3410  OE2 GLU A 418      30.665 -10.558  15.066  1.00 66.12           O  
ATOM   3411  N   LYS A 419      34.077  -5.545  16.296  1.00 39.79           N  
ATOM   3412  CA  LYS A 419      34.398  -5.149  17.659  1.00 40.29           C  
ATOM   3413  C   LYS A 419      33.704  -3.817  17.925  1.00 35.75           C  
ATOM   3414  O   LYS A 419      33.025  -3.653  18.932  1.00 35.88           O  
ATOM   3415  CB  LYS A 419      35.915  -5.002  17.820  1.00 45.09           C  
ATOM   3416  CG  LYS A 419      36.377  -4.683  19.228  1.00 50.09           C  
ATOM   3417  CD  LYS A 419      37.885  -4.438  19.257  1.00 51.50           C  
ATOM   3418  CE  LYS A 419      38.331  -3.946  20.620  1.00 57.16           C  
ATOM   3419  NZ  LYS A 419      39.760  -3.493  20.641  1.00 58.90           N  
ATOM   3420  N   LEU A 420      33.864  -2.872  17.005  1.00 34.58           N  
ATOM   3421  CA  LEU A 420      33.243  -1.557  17.150  1.00 35.67           C  
ATOM   3422  C   LEU A 420      31.723  -1.687  17.202  1.00 30.71           C  
ATOM   3423  O   LEU A 420      31.067  -1.122  18.077  1.00 37.14           O  
ATOM   3424  CB  LEU A 420      33.623  -0.650  15.971  1.00 36.33           C  
ATOM   3425  CG  LEU A 420      33.585   0.876  16.154  1.00 43.30           C  
ATOM   3426  CD1 LEU A 420      33.255   1.508  14.817  1.00 38.70           C  
ATOM   3427  CD2 LEU A 420      32.569   1.302  17.202  1.00 43.24           C  
ATOM   3428  N   PHE A 421      31.160  -2.434  16.263  1.00 33.29           N  
ATOM   3429  CA  PHE A 421      29.714  -2.596  16.223  1.00 38.43           C  
ATOM   3430  C   PHE A 421      29.125  -3.157  17.526  1.00 39.52           C  
ATOM   3431  O   PHE A 421      27.980  -2.876  17.858  1.00 50.62           O  
ATOM   3432  CB  PHE A 421      29.313  -3.458  15.016  1.00 37.36           C  
ATOM   3433  CG  PHE A 421      29.932  -3.004  13.713  1.00 36.68           C  
ATOM   3434  CD1 PHE A 421      30.139  -1.649  13.451  1.00 37.25           C  
ATOM   3435  CD2 PHE A 421      30.338  -3.933  12.765  1.00 36.39           C  
ATOM   3436  CE1 PHE A 421      30.745  -1.237  12.267  1.00 35.80           C  
ATOM   3437  CE2 PHE A 421      30.944  -3.531  11.579  1.00 37.88           C  
ATOM   3438  CZ  PHE A 421      31.151  -2.183  11.327  1.00 37.95           C  
ATOM   3439  N   LYS A 422      29.906  -3.919  18.282  1.00 40.82           N  
ATOM   3440  CA  LYS A 422      29.406  -4.472  19.538  1.00 39.58           C  
ATOM   3441  C   LYS A 422      29.238  -3.418  20.620  1.00 41.30           C  
ATOM   3442  O   LYS A 422      28.407  -3.572  21.514  1.00 42.61           O  
ATOM   3443  CB  LYS A 422      30.342  -5.563  20.061  1.00 46.30           C  
ATOM   3444  CG  LYS A 422      30.338  -6.841  19.249  1.00 50.45           C  
ATOM   3445  CD  LYS A 422      31.132  -7.912  19.977  1.00 54.71           C  
ATOM   3446  CE  LYS A 422      31.190  -9.207  19.194  1.00 53.25           C  
ATOM   3447  NZ  LYS A 422      31.817 -10.276  20.022  1.00 55.10           N  
ATOM   3448  N   GLU A 423      30.032  -2.349  20.547  1.00 39.18           N  
ATOM   3449  CA  GLU A 423      29.962  -1.278  21.540  1.00 34.42           C  
ATOM   3450  C   GLU A 423      28.609  -0.591  21.442  1.00 32.88           C  
ATOM   3451  O   GLU A 423      27.916  -0.719  20.436  1.00 37.08           O  
ATOM   3452  CB  GLU A 423      31.073  -0.250  21.284  1.00 39.02           C  
ATOM   3453  CG  GLU A 423      32.490  -0.815  21.324  1.00 31.10           C  
ATOM   3454  CD  GLU A 423      32.865  -1.331  22.697  1.00 40.06           C  
ATOM   3455  OE1 GLU A 423      32.478  -0.693  23.702  1.00 38.33           O  
ATOM   3456  OE2 GLU A 423      33.557  -2.367  22.777  1.00 42.19           O  
ATOM   3457  N   PRO A 424      28.206   0.137  22.488  1.00 31.22           N  
ATOM   3458  CA  PRO A 424      26.913   0.838  22.467  1.00 33.27           C  
ATOM   3459  C   PRO A 424      27.002   2.172  21.694  1.00 30.66           C  
ATOM   3460  O   PRO A 424      26.779   3.242  22.254  1.00 34.17           O  
ATOM   3461  CB  PRO A 424      26.625   1.052  23.948  1.00 34.96           C  
ATOM   3462  CG  PRO A 424      28.015   1.298  24.506  1.00 33.07           C  
ATOM   3463  CD  PRO A 424      28.818   0.200  23.829  1.00 30.62           C  
ATOM   3464  N   VAL A 425      27.310   2.093  20.404  1.00 30.27           N  
ATOM   3465  CA  VAL A 425      27.453   3.285  19.576  1.00 31.57           C  
ATOM   3466  C   VAL A 425      26.714   3.165  18.253  1.00 35.82           C  
ATOM   3467  O   VAL A 425      26.807   4.053  17.406  1.00 30.70           O  
ATOM   3468  CB  VAL A 425      28.943   3.561  19.250  1.00 31.93           C  
ATOM   3469  CG1 VAL A 425      29.710   3.899  20.519  1.00 25.10           C  
ATOM   3470  CG2 VAL A 425      29.558   2.328  18.589  1.00 30.25           C  
ATOM   3471  N   THR A 426      25.983   2.067  18.078  1.00 32.03           N  
ATOM   3472  CA  THR A 426      25.248   1.835  16.838  1.00 35.74           C  
ATOM   3473  C   THR A 426      24.377   3.010  16.376  1.00 33.91           C  
ATOM   3474  O   THR A 426      24.354   3.338  15.185  1.00 34.03           O  
ATOM   3475  CB  THR A 426      24.383   0.541  16.947  1.00 36.86           C  
ATOM   3476  OG1 THR A 426      23.786   0.478  18.242  1.00 45.94           O  
ATOM   3477  CG2 THR A 426      25.238  -0.697  16.756  1.00 34.54           C  
ATOM   3478  N   ALA A 427      23.662   3.646  17.300  1.00 30.87           N  
ATOM   3479  CA  ALA A 427      22.811   4.777  16.932  1.00 32.01           C  
ATOM   3480  C   ALA A 427      23.642   5.943  16.382  1.00 32.00           C  
ATOM   3481  O   ALA A 427      23.268   6.575  15.393  1.00 27.17           O  
ATOM   3482  CB  ALA A 427      21.994   5.241  18.137  1.00 36.66           C  
ATOM   3483  N   GLU A 428      24.769   6.221  17.030  1.00 28.04           N  
ATOM   3484  CA  GLU A 428      25.644   7.297  16.602  1.00 27.83           C  
ATOM   3485  C   GLU A 428      26.286   6.978  15.247  1.00 28.50           C  
ATOM   3486  O   GLU A 428      26.433   7.863  14.399  1.00 24.19           O  
ATOM   3487  CB  GLU A 428      26.712   7.552  17.665  1.00 28.21           C  
ATOM   3488  CG  GLU A 428      26.194   8.229  18.957  1.00 32.87           C  
ATOM   3489  CD  GLU A 428      25.242   7.353  19.769  1.00 35.95           C  
ATOM   3490  OE1 GLU A 428      25.391   6.107  19.770  1.00 40.14           O  
ATOM   3491  OE2 GLU A 428      24.345   7.916  20.427  1.00 42.87           O  
ATOM   3492  N   LEU A 429      26.664   5.716  15.041  1.00 24.80           N  
ATOM   3493  CA  LEU A 429      27.238   5.305  13.760  1.00 29.80           C  
ATOM   3494  C   LEU A 429      26.240   5.497  12.621  1.00 29.08           C  
ATOM   3495  O   LEU A 429      26.576   6.046  11.564  1.00 25.73           O  
ATOM   3496  CB  LEU A 429      27.656   3.830  13.800  1.00 27.20           C  
ATOM   3497  CG  LEU A 429      28.968   3.589  14.548  1.00 35.30           C  
ATOM   3498  CD1 LEU A 429      29.266   2.088  14.618  1.00 31.20           C  
ATOM   3499  CD2 LEU A 429      30.102   4.346  13.844  1.00 29.99           C  
ATOM   3500  N   CYS A 430      25.016   5.029  12.832  1.00 26.75           N  
ATOM   3501  CA  CYS A 430      23.977   5.133  11.810  1.00 28.02           C  
ATOM   3502  C   CYS A 430      23.677   6.579  11.459  1.00 26.39           C  
ATOM   3503  O   CYS A 430      23.582   6.948  10.290  1.00 25.02           O  
ATOM   3504  CB  CYS A 430      22.701   4.431  12.289  1.00 33.19           C  
ATOM   3505  SG  CYS A 430      22.862   2.616  12.248  1.00 35.33           S  
ATOM   3506  N   GLU A 431      23.523   7.393  12.486  1.00 28.44           N  
ATOM   3507  CA  GLU A 431      23.242   8.808  12.313  1.00 29.68           C  
ATOM   3508  C   GLU A 431      24.394   9.461  11.524  1.00 26.63           C  
ATOM   3509  O   GLU A 431      24.181  10.189  10.557  1.00 26.22           O  
ATOM   3510  CB  GLU A 431      23.089   9.434  13.706  1.00 34.71           C  
ATOM   3511  CG  GLU A 431      22.631  10.878  13.752  1.00 49.59           C  
ATOM   3512  CD  GLU A 431      22.493  11.388  15.181  1.00 61.80           C  
ATOM   3513  OE1 GLU A 431      22.867  10.643  16.123  1.00 65.24           O  
ATOM   3514  OE2 GLU A 431      22.017  12.536  15.370  1.00 66.36           O  
ATOM   3515  N   MET A 432      25.620   9.163  11.931  1.00 27.42           N  
ATOM   3516  CA  MET A 432      26.811   9.722  11.297  1.00 33.41           C  
ATOM   3517  C   MET A 432      26.878   9.413   9.802  1.00 32.29           C  
ATOM   3518  O   MET A 432      27.250  10.274   8.996  1.00 29.04           O  
ATOM   3519  CB  MET A 432      28.061   9.176  11.993  1.00 28.59           C  
ATOM   3520  CG  MET A 432      29.373   9.752  11.525  1.00 39.61           C  
ATOM   3521  SD  MET A 432      30.756   9.163  12.552  1.00 43.56           S  
ATOM   3522  CE  MET A 432      30.767   7.439  12.151  1.00 39.86           C  
ATOM   3523  N   MET A 433      26.502   8.190   9.439  1.00 26.92           N  
ATOM   3524  CA  MET A 433      26.543   7.761   8.045  1.00 22.51           C  
ATOM   3525  C   MET A 433      25.257   8.009   7.255  1.00 20.65           C  
ATOM   3526  O   MET A 433      25.221   7.766   6.052  1.00 22.88           O  
ATOM   3527  CB  MET A 433      26.923   6.268   7.974  1.00 21.95           C  
ATOM   3528  CG  MET A 433      28.283   5.957   8.587  1.00 17.74           C  
ATOM   3529  SD  MET A 433      28.815   4.235   8.368  1.00 24.60           S  
ATOM   3530  CE  MET A 433      27.715   3.444   9.580  1.00 21.23           C  
ATOM   3531  N   GLY A 434      24.218   8.500   7.929  1.00 24.60           N  
ATOM   3532  CA  GLY A 434      22.945   8.767   7.278  1.00 25.13           C  
ATOM   3533  C   GLY A 434      22.172   7.501   6.925  1.00 26.80           C  
ATOM   3534  O   GLY A 434      21.462   7.436   5.914  1.00 24.42           O  
ATOM   3535  N   VAL A 435      22.322   6.473   7.749  1.00 28.73           N  
ATOM   3536  CA  VAL A 435      21.624   5.225   7.504  1.00 30.47           C  
ATOM   3537  C   VAL A 435      20.133   5.422   7.772  1.00 32.98           C  
ATOM   3538  O   VAL A 435      19.744   6.088   8.728  1.00 34.61           O  
ATOM   3539  CB  VAL A 435      22.157   4.105   8.419  1.00 27.74           C  
ATOM   3540  CG1 VAL A 435      21.362   2.826   8.195  1.00 32.27           C  
ATOM   3541  CG2 VAL A 435      23.638   3.862   8.130  1.00 24.33           C  
ATOM   3542  N   LYS A 436      19.290   4.863   6.920  1.00 38.89           N  
ATOM   3543  CA  LYS A 436      17.866   5.005   7.156  1.00 43.57           C  
ATOM   3544  C   LYS A 436      17.174   3.700   7.505  1.00 46.59           C  
ATOM   3545  O   LYS A 436      17.785   2.632   7.472  1.00 41.45           O  
ATOM   3546  CB  LYS A 436      17.184   5.681   5.966  1.00 48.32           C  
ATOM   3547  CG  LYS A 436      17.725   5.375   4.598  1.00 43.56           C  
ATOM   3548  CD  LYS A 436      17.167   6.428   3.649  1.00 50.40           C  
ATOM   3549  CE  LYS A 436      17.624   6.241   2.223  1.00 52.09           C  
ATOM   3550  NZ  LYS A 436      17.150   7.373   1.372  1.00 45.25           N  
ATOM   3551  N   ASP A 437      15.896   3.805   7.856  1.00 51.78           N  
ATOM   3552  CA  ASP A 437      15.088   2.657   8.240  1.00 59.36           C  
ATOM   3553  C   ASP A 437      14.762   1.730   7.071  1.00 65.34           C  
ATOM   3554  O   ASP A 437      13.657   1.149   7.083  1.00 74.84           O  
ATOM   3555  CB  ASP A 437      13.788   3.151   8.879  1.00 64.87           C  
ATOM   3556  CG  ASP A 437      13.568   2.586  10.268  1.00 68.86           C  
ATOM   3557  OD1 ASP A 437      14.484   1.905  10.783  1.00 71.49           O  
ATOM   3558  OD2 ASP A 437      12.483   2.824  10.846  1.00 68.38           O  
ATOM   3559  OXT ASP A 437      15.611   1.570   6.169  1.00 70.05           O  
TER    3560      ASP A 437                                                      
HETATM 3561  C   ACT A 601      23.810  18.508  19.499  1.00 34.72           C  
HETATM 3562  O   ACT A 601      23.205  18.885  18.467  1.00 31.91           O  
HETATM 3563  OXT ACT A 601      23.606  17.418  20.064  1.00 35.87           O  
HETATM 3564  CH3 ACT A 601      24.869  19.432  20.108  1.00 33.38           C  
HETATM 3565 CA    CA A 501      21.564  16.390  18.745  1.00 43.87          CA  
HETATM 3566 MG    MG A 502      15.457  22.341  38.124  1.00 40.39          MG  
HETATM 3567 CA    CA A 503      50.722   0.519   8.397  1.00 46.62          CA  
HETATM 3568 CA    CA A 504      23.621  15.369  21.726  1.00 51.35          CA  
HETATM 3569  O   HOH A 602      21.064  16.717  10.238  1.00 17.52           O  
HETATM 3570  O   HOH A 603       8.578  25.851  40.157  1.00 18.54           O  
HETATM 3571  O   HOH A 604      32.754  18.712  36.683  1.00 20.97           O  
HETATM 3572  O   HOH A 605       9.462  21.506  30.865  1.00 21.55           O  
HETATM 3573  O   HOH A 606      14.965  27.395  31.050  1.00 24.30           O  
HETATM 3574  O   HOH A 607      48.557  -0.854   7.579  1.00 34.52           O  
HETATM 3575  O   HOH A 608       9.413  48.548  18.486  1.00 19.85           O  
HETATM 3576  O   HOH A 609      26.383  10.741  24.494  1.00 23.40           O  
HETATM 3577  O   HOH A 610      53.288  14.061  -0.122  1.00 22.26           O  
HETATM 3578  O   HOH A 611      27.443  17.994  22.868  1.00 21.36           O  
HETATM 3579  O   HOH A 612       5.694  31.321  45.114  1.00 24.06           O  
HETATM 3580  O   HOH A 613       9.526  36.451  12.794  1.00 22.94           O  
HETATM 3581  O   HOH A 614      63.541   8.182   0.559  1.00 24.68           O  
HETATM 3582  O   HOH A 615      34.867   0.169   4.126  1.00 24.19           O  
HETATM 3583  O   HOH A 616      50.236  13.685   4.356  1.00 30.05           O  
HETATM 3584  O   HOH A 617      24.113  30.109  19.410  1.00 26.59           O  
HETATM 3585  O   HOH A 618      26.856  26.954  16.827  1.00 25.77           O  
HETATM 3586  O   HOH A 619      49.771  11.658   6.218  1.00 24.47           O  
HETATM 3587  O   HOH A 620      18.517  27.935  24.003  1.00 25.36           O  
HETATM 3588  O   HOH A 621      63.986   7.124   3.255  1.00 22.90           O  
HETATM 3589  O   HOH A 622       9.761  26.654  30.558  1.00 26.21           O  
HETATM 3590  O   HOH A 623      72.445  32.048  -2.611  1.00 38.85           O  
HETATM 3591  O   HOH A 624      49.732  16.538  11.601  1.00 31.70           O  
HETATM 3592  O   HOH A 625       3.693  32.638   7.726  1.00 27.31           O  
HETATM 3593  O   HOH A 626      13.724  16.334   5.461  1.00 46.99           O  
HETATM 3594  O   HOH A 627      12.326  29.535  34.379  1.00 41.62           O  
HETATM 3595  O   HOH A 628      70.443  24.063  -5.545  1.00 22.78           O  
HETATM 3596  O   HOH A 629      42.426  15.020   4.303  1.00 26.19           O  
HETATM 3597  O   HOH A 630      40.837   5.975  29.697  1.00 24.46           O  
HETATM 3598  O   HOH A 631      20.509  18.250  20.257  1.00 20.98           O  
HETATM 3599  O   HOH A 632      54.398  10.453   9.563  1.00 24.67           O  
HETATM 3600  O   HOH A 633      25.106  18.552  29.076  1.00 24.09           O  
HETATM 3601  O   HOH A 634      62.029   8.912   5.838  1.00 27.19           O  
HETATM 3602  O   HOH A 635      30.016  -7.190   4.371  1.00 36.82           O  
HETATM 3603  O   HOH A 636      58.524  16.827 -10.524  1.00 26.85           O  
HETATM 3604  O   HOH A 637      49.609  16.573  14.521  1.00 32.29           O  
HETATM 3605  O   HOH A 638      56.684  19.203   3.548  1.00 29.57           O  
HETATM 3606  O   HOH A 639      25.819  15.530  34.527  1.00 35.37           O  
HETATM 3607  O   HOH A 640      42.141   1.634   7.372  1.00 22.33           O  
HETATM 3608  O   HOH A 641      42.583   0.907   0.780  1.00 29.47           O  
HETATM 3609  O   HOH A 642      25.132  -9.698  13.037  1.00 37.01           O  
HETATM 3610  O   HOH A 643      39.336  21.440  28.706  1.00 31.28           O  
HETATM 3611  O   HOH A 644       6.236  25.054   4.890  1.00 26.83           O  
HETATM 3612  O   HOH A 645      69.070  12.416   0.699  1.00 26.07           O  
HETATM 3613  O   HOH A 646      14.107  23.585   4.175  1.00 28.71           O  
HETATM 3614  O   HOH A 647      15.034  37.961   9.909  1.00 37.74           O  
HETATM 3615  O   HOH A 648      12.162   5.451   6.870  1.00 53.81           O  
HETATM 3616  O   HOH A 649      13.956  41.809  24.652  1.00 31.96           O  
HETATM 3617  O   HOH A 650      21.699  42.573  18.447  1.00 45.31           O  
HETATM 3618  O   HOH A 651      18.112  30.387  27.964  1.00 28.74           O  
HETATM 3619  O   HOH A 652      72.828  25.716   7.574  1.00 46.39           O  
HETATM 3620  O   HOH A 653      60.724  17.947 -11.383  1.00 35.05           O  
HETATM 3621  O   HOH A 654      15.446  17.335  23.403  1.00 27.73           O  
HETATM 3622  O   HOH A 655      25.240  35.067  21.597  1.00 33.78           O  
HETATM 3623  O   HOH A 656      -0.463  34.004  17.360  1.00 38.15           O  
HETATM 3624  O   HOH A 657       7.790  36.461   9.614  1.00 32.26           O  
HETATM 3625  O   HOH A 658      18.613  32.792  29.561  1.00 33.51           O  
HETATM 3626  O   HOH A 659       5.587  21.029  58.024  1.00 58.06           O  
HETATM 3627  O   HOH A 660      70.549  13.927  -0.703  1.00 44.35           O  
HETATM 3628  O   HOH A 661      44.360  21.986  10.656  1.00 30.78           O  
HETATM 3629  O   HOH A 662      13.917  28.229  35.943  1.00 45.70           O  
HETATM 3630  O   HOH A 663      51.933   9.747  29.699  1.00 51.27           O  
HETATM 3631  O   HOH A 664      50.613   1.992   2.277  1.00 28.38           O  
HETATM 3632  O   HOH A 665       8.845  43.918  28.454  1.00 36.36           O  
HETATM 3633  O   HOH A 666      14.919   6.869   6.724  1.00 47.72           O  
HETATM 3634  O   HOH A 667      33.848  14.692  40.084  1.00 52.07           O  
HETATM 3635  O   HOH A 668      66.456   3.885  -4.347  1.00 34.84           O  
HETATM 3636  O   HOH A 669      74.153  23.527  -1.869  1.00 29.45           O  
HETATM 3637  O   HOH A 670      53.230  13.857  24.602  1.00 33.24           O  
HETATM 3638  O   HOH A 671      19.918  -5.672  10.654  1.00 39.59           O  
HETATM 3639  O   HOH A 672      50.958   4.920  14.699  1.00 32.13           O  
HETATM 3640  O   HOH A 673      28.019  13.209  18.190  1.00 34.01           O  
HETATM 3641  O   HOH A 674      23.952  32.434  13.931  1.00 32.80           O  
HETATM 3642  O   HOH A 675      44.984  10.115  36.500  1.00 48.88           O  
HETATM 3643  O   HOH A 676      35.604  15.725   1.966  1.00 37.35           O  
HETATM 3644  O   HOH A 677      20.457  29.196  25.292  1.00 24.93           O  
HETATM 3645  O   HOH A 678      72.863  29.889   1.628  1.00 34.35           O  
HETATM 3646  O   HOH A 679      24.331  36.167  26.073  1.00 34.67           O  
HETATM 3647  O   HOH A 680      77.156  24.252  -1.770  1.00 52.37           O  
HETATM 3648  O   HOH A 681      20.164  17.767  16.753  1.00 25.74           O  
HETATM 3649  O   HOH A 682      74.734  17.429   1.535  1.00 40.87           O  
HETATM 3650  O   HOH A 683      45.059  18.057   3.784  1.00 32.26           O  
HETATM 3651  O   HOH A 684      25.801  19.189  33.568  1.00 26.31           O  
HETATM 3652  O   HOH A 685      44.669  18.414  15.849  1.00 23.64           O  
HETATM 3653  O   HOH A 686      25.547  25.878  21.251  1.00 40.94           O  
HETATM 3654  O   HOH A 687      44.325   0.286  20.240  1.00 39.55           O  
HETATM 3655  O   HOH A 688      34.328  21.708  29.333  1.00 35.37           O  
HETATM 3656  O   HOH A 689      34.602  -0.415  11.194  1.00 36.37           O  
HETATM 3657  O   HOH A 690      69.035  10.210  -0.950  1.00 33.13           O  
HETATM 3658  O   HOH A 691      45.596   0.071  10.904  1.00 29.89           O  
HETATM 3659  O   HOH A 692      39.768   4.088   0.973  1.00 31.67           O  
HETATM 3660  O   HOH A 693      48.979   0.314   5.036  1.00 50.03           O  
HETATM 3661  O   HOH A 694      44.208  21.102  15.056  1.00 35.14           O  
HETATM 3662  O   HOH A 695       9.132  11.740  14.769  1.00 44.34           O  
HETATM 3663  O   HOH A 696      33.061  18.103  17.295  1.00 36.52           O  
HETATM 3664  O   HOH A 697      14.048  34.997   5.888  1.00 29.75           O  
HETATM 3665  O   HOH A 698      48.892   9.580  33.272  1.00 61.47           O  
HETATM 3666  O   HOH A 699      16.884  18.021  27.370  1.00 37.00           O  
HETATM 3667  O   HOH A 700       2.492  36.736  13.201  1.00 49.87           O  
HETATM 3668  O   HOH A 701      23.143  16.680  30.160  1.00 32.39           O  
HETATM 3669  O   HOH A 702      46.711   2.104  22.717  1.00 62.38           O  
HETATM 3670  O   HOH A 703      55.846  22.379  -7.367  1.00 34.48           O  
HETATM 3671  O   HOH A 704      17.447  24.084  29.132  1.00 31.18           O  
HETATM 3672  O   HOH A 705      -2.696  27.545  25.805  1.00 43.17           O  
HETATM 3673  O   HOH A 706      10.002  35.333  10.419  1.00 34.15           O  
HETATM 3674  O   HOH A 707      34.637  12.047  17.190  1.00 33.01           O  
HETATM 3675  O   HOH A 708      54.427   2.721  10.392  1.00 61.98           O  
HETATM 3676  O   HOH A 709      40.207  12.354  34.031  1.00 43.17           O  
HETATM 3677  O   HOH A 710      47.562   8.673  25.315  1.00 28.45           O  
HETATM 3678  O   HOH A 711      34.251  17.623  14.140  1.00 55.19           O  
HETATM 3679  O   HOH A 712      53.711  18.866  -8.164  1.00 35.48           O  
HETATM 3680  O   HOH A 713      26.624  27.678   6.180  1.00 38.74           O  
HETATM 3681  O   HOH A 714      47.816   5.073  27.089  1.00 38.35           O  
HETATM 3682  O   HOH A 715       8.198  37.488   6.504  1.00 34.92           O  
HETATM 3683  O   HOH A 716      58.960  28.349  -4.308  1.00 39.51           O  
HETATM 3684  O   HOH A 717      76.891  24.952   5.741  1.00 49.98           O  
HETATM 3685  O   HOH A 718      30.389  16.153  13.811  1.00 38.94           O  
HETATM 3686  O   HOH A 719      52.804   1.874   9.191  1.00 38.50           O  
HETATM 3687  O   HOH A 720       0.424  30.064  33.614  1.00 39.17           O  
HETATM 3688  O   HOH A 721      71.002   9.266   1.648  1.00 42.46           O  
HETATM 3689  O   HOH A 722      -0.722  26.428  18.140  1.00 29.56           O  
HETATM 3690  O   HOH A 723      11.819  23.978  35.868  1.00 46.89           O  
HETATM 3691  O   HOH A 724      22.752  13.996  10.969  1.00 40.73           O  
HETATM 3692  O   HOH A 725      36.292   0.518   8.127  1.00 34.87           O  
HETATM 3693  O   HOH A 726      24.230   8.916  25.091  1.00 50.17           O  
HETATM 3694  O   HOH A 727       8.997  47.280  25.616  1.00 30.19           O  
HETATM 3695  O   HOH A 728      15.438  17.574  55.987  1.00 59.08           O  
HETATM 3696  O   HOH A 729      51.296   0.349  12.839  1.00 30.76           O  
HETATM 3697  O   HOH A 730      -1.540  35.464  26.625  1.00 50.84           O  
HETATM 3698  O   HOH A 731      27.383  11.393  30.901  1.00 41.37           O  
HETATM 3699  O   HOH A 732      21.819  29.455  16.855  1.00 35.54           O  
HETATM 3700  O   HOH A 733      31.497  15.739  11.596  1.00 36.15           O  
HETATM 3701  O   HOH A 734      72.906  12.337   2.044  1.00 37.37           O  
HETATM 3702  O   HOH A 735      -3.575  23.129  31.921  1.00 56.48           O  
HETATM 3703  O   HOH A 736      52.458  11.586  26.509  1.00 37.64           O  
HETATM 3704  O   HOH A 737      64.315  11.491  -1.463  1.00 31.00           O  
HETATM 3705  O   HOH A 738      10.441  47.330  14.216  1.00 37.69           O  
HETATM 3706  O   HOH A 739      45.336  22.302  22.264  1.00 56.07           O  
HETATM 3707  O   HOH A 740      41.296  25.172  19.564  1.00 39.48           O  
HETATM 3708  O   HOH A 741      37.526  18.414   5.594  1.00 40.11           O  
HETATM 3709  O   HOH A 742      51.590  16.014  26.546  1.00 48.68           O  
HETATM 3710  O   HOH A 743       1.401  36.993  22.777  1.00 34.90           O  
HETATM 3711  O   HOH A 744      57.201  11.212   8.998  1.00 47.34           O  
HETATM 3712  O   HOH A 745      37.681  15.219   4.090  1.00 42.40           O  
HETATM 3713  O   HOH A 746      75.024  15.148   0.173  1.00 51.70           O  
HETATM 3714  O   HOH A 747      66.063  34.293  -6.338  1.00 48.62           O  
HETATM 3715  O   HOH A 748      26.380  24.167  14.930  1.00 27.77           O  
HETATM 3716  O   HOH A 749      61.804  26.628   2.637  1.00 63.96           O  
HETATM 3717  O   HOH A 750       3.211  31.582  39.535  1.00 59.31           O  
HETATM 3718  O   HOH A 751       7.535  30.823   4.612  1.00 37.35           O  
HETATM 3719  O   HOH A 752      38.739   0.784   9.795  1.00 44.65           O  
HETATM 3720  O   HOH A 753      25.684  32.307  20.677  1.00 55.76           O  
HETATM 3721  O   HOH A 754      74.388  23.558   5.303  1.00 47.46           O  
HETATM 3722  O   HOH A 755      29.730  29.076  26.636  1.00 65.95           O  
HETATM 3723  O   HOH A 756      48.942  18.246   2.260  1.00 51.88           O  
HETATM 3724  O   HOH A 757      28.917  13.062  32.734  1.00 36.98           O  
HETATM 3725  O   HOH A 758      39.338  -3.004  16.387  1.00 28.23           O  
HETATM 3726  O   HOH A 759      45.104   3.413  -0.894  1.00 38.75           O  
HETATM 3727  O   HOH A 760      37.596  23.905  21.994  1.00 56.52           O  
HETATM 3728  O   HOH A 761      20.070  13.003  51.911  1.00 49.58           O  
HETATM 3729  O   HOH A 762       4.403  34.628  41.334  1.00 56.62           O  
HETATM 3730  O   HOH A 763      14.872  34.532  53.588  1.00 59.23           O  
HETATM 3731  O   HOH A 764      26.357  12.544  20.256  1.00 44.27           O  
HETATM 3732  O   HOH A 765       6.795  17.832   4.934  1.00 37.41           O  
HETATM 3733  O   HOH A 766       0.128  37.599  36.843  1.00 48.45           O  
HETATM 3734  O   HOH A 767      35.940  22.672  20.054  1.00 60.26           O  
HETATM 3735  O   HOH A 768      64.233  18.893   6.205  1.00 40.44           O  
HETATM 3736  O   HOH A 769      38.247   1.964   0.089  1.00 36.95           O  
HETATM 3737  O   HOH A 770      38.065  22.777   7.298  1.00 62.72           O  
HETATM 3738  O   HOH A 771      24.384   9.228  27.944  1.00 58.73           O  
HETATM 3739  O   HOH A 772      27.670  31.004   9.047  1.00 44.27           O  
HETATM 3740  O   HOH A 773      22.783  30.846  28.686  1.00 51.09           O  
HETATM 3741  O   HOH A 774      38.057  11.536  36.093  1.00 35.43           O  
HETATM 3742  O   HOH A 775      28.657  34.585  20.349  1.00 53.51           O  
HETATM 3743  O   HOH A 776       3.682  36.669  10.180  1.00 32.51           O  
HETATM 3744  O   HOH A 777       9.165  21.750   2.884  1.00 60.78           O  
HETATM 3745  O   HOH A 778      42.924  20.382  25.788  1.00 41.78           O  
HETATM 3746  O   HOH A 779       3.623  11.575  25.880  1.00 57.17           O  
HETATM 3747  O   HOH A 780      25.540  19.356  13.685  1.00 33.25           O  
HETATM 3748  O   HOH A 781      20.441   6.129  14.554  1.00 50.30           O  
HETATM 3749  O   HOH A 782      46.604  21.179  32.568  1.00 58.31           O  
HETATM 3750  O   HOH A 783      25.326  34.350  44.844  1.00 66.81           O  
HETATM 3751  O   HOH A 784      23.882  24.916  30.196  1.00 43.40           O  
HETATM 3752  O   HOH A 785      24.706  13.234  22.908  1.00 41.89           O  
HETATM 3753  O   HOH A 786      20.644  44.190  15.755  1.00 48.48           O  
HETATM 3754  O   HOH A 787      -3.580  25.497  21.935  1.00 66.95           O  
HETATM 3755  O   HOH A 788      58.892  25.170 -13.465  1.00 47.18           O  
HETATM 3756  O   HOH A 789      74.645  11.681   5.869  1.00 66.41           O  
HETATM 3757  O   HOH A 790      26.739  41.359  27.692  1.00 51.83           O  
HETATM 3758  O   HOH A 791      72.015  31.848  -0.196  1.00 59.14           O  
HETATM 3759  O   HOH A 792      17.155  44.644   9.834  1.00 47.70           O  
HETATM 3760  O   HOH A 793      19.832  30.459  37.006  1.00 57.76           O  
HETATM 3761  O   HOH A 794      28.553  -5.781  23.757  1.00 53.11           O  
HETATM 3762  O   HOH A 795      31.678   6.417  35.247  1.00 47.50           O  
HETATM 3763  O   HOH A 796      43.243  23.686  12.478  1.00 46.80           O  
HETATM 3764  O   HOH A 797      69.993  29.046   5.494  1.00 37.39           O  
HETATM 3765  O   HOH A 798      54.005  17.931  -2.186  1.00 42.84           O  
HETATM 3766  O   HOH A 799      34.654  17.823   5.663  1.00 38.55           O  
HETATM 3767  O   HOH A 800      23.472  14.790  33.755  1.00 45.76           O  
HETATM 3768  O   HOH A 801      37.712  22.210  12.419  1.00 58.49           O  
HETATM 3769  O   HOH A 802      16.586   4.896  -0.087  1.00 53.84           O  
HETATM 3770  O   HOH A 803      32.098  23.547  29.907  1.00 43.18           O  
HETATM 3771  O   HOH A 804      42.826  20.456   9.187  1.00 49.04           O  
HETATM 3772  O   HOH A 805      15.199  45.048  24.319  1.00 38.14           O  
HETATM 3773  O   HOH A 806      66.871  20.259   6.060  1.00 38.64           O  
HETATM 3774  O   HOH A 807      20.554  16.430  28.759  1.00 39.27           O  
HETATM 3775  O   HOH A 808      14.811  25.383  34.413  1.00 45.76           O  
HETATM 3776  O   HOH A 809      37.267  -4.375  23.063  1.00 49.19           O  
HETATM 3777  O   HOH A 810      15.357  19.774  49.182  1.00 42.43           O  
HETATM 3778  O   HOH A 811      22.285  45.841  38.622  1.00 66.16           O  
HETATM 3779  O   HOH A 812      -4.019  29.138  23.345  1.00 66.50           O  
HETATM 3780  O   HOH A 813      43.550  -0.677   9.084  1.00 35.28           O  
HETATM 3781  O   HOH A 814      39.718   0.589   7.494  1.00 39.17           O  
HETATM 3782  O   HOH A 815      62.233   6.400   7.036  1.00 40.90           O  
HETATM 3783  O   HOH A 816      28.449  -8.177   6.279  1.00 46.58           O  
HETATM 3784  O   HOH A 817      11.850  26.956  32.368  1.00 34.05           O  
HETATM 3785  O   HOH A 818      41.418   5.452  32.255  1.00 35.70           O  
HETATM 3786  O   HOH A 819      23.578  30.252  15.409  1.00 40.16           O  
HETATM 3787  O   HOH A 820      -6.900  27.846  20.504  1.00 53.81           O  
HETATM 3788  O   HOH A 821      26.325  16.036  21.901  1.00 37.09           O  
HETATM 3789  O   HOH A 822      41.871  23.517  16.873  1.00 45.94           O  
HETATM 3790  O   HOH A 823      42.620  -1.025   2.618  1.00 40.95           O  
HETATM 3791  O   HOH A 824      29.189  28.640   9.232  1.00 46.04           O  
HETATM 3792  O   HOH A 825      66.924  36.747  -6.672  1.00 44.57           O  
HETATM 3793  O   HOH A 826      39.524   8.388  33.559  1.00 45.25           O  
HETATM 3794  O   HOH A 827      12.190  23.926  32.100  1.00 67.77           O  
HETATM 3795  O   HOH A 828      -5.015  23.528  19.819  1.00 58.22           O  
HETATM 3796  O   HOH A 829      14.554  47.063  25.987  1.00 41.97           O  
HETATM 3797  O   HOH A 830      78.061  29.103  -4.383  1.00 43.16           O  
HETATM 3798  O   HOH A 831      24.141  20.767  16.875  1.00 25.28           O  
HETATM 3799  O   HOH A 832      -3.066  27.674  16.602  1.00 37.37           O  
HETATM 3800  O   HOH A 833      23.303  18.681  32.377  1.00 43.83           O  
HETATM 3801  O   HOH A 834      -0.978  12.671  11.843  1.00 43.44           O  
HETATM 3802  O   HOH A 835      22.475  -3.891  -1.069  1.00 57.88           O  
HETATM 3803  O   HOH A 836      21.930  31.262  18.892  1.00 47.59           O  
HETATM 3804  O   HOH A 837      64.125  28.230   0.171  1.00 32.80           O  
HETATM 3805  O   HOH A 838      34.517  -2.183   8.927  1.00 35.87           O  
HETATM 3806  O   HOH A 839      71.057   6.926   2.740  1.00 52.70           O  
HETATM 3807  O   HOH A 840      10.352  21.018  33.526  1.00 45.00           O  
HETATM 3808  O   HOH A 841      36.169  -1.802   5.765  1.00 53.09           O  
HETATM 3809  O   HOH A 842       9.854  51.118  16.932  1.00 45.55           O  
HETATM 3810  O   HOH A 843      15.094  31.507   5.783  1.00 45.48           O  
HETATM 3811  O   HOH A 844      16.372  31.824  34.653  1.00 53.32           O  
HETATM 3812  O   HOH A 845      17.980  16.374  16.242  1.00 35.47           O  
HETATM 3813  O   HOH A 846      -4.959  22.696   7.906  1.00 51.19           O  
HETATM 3814  O   HOH A 847       0.498  33.257  39.428  1.00 62.73           O  
HETATM 3815  O   HOH A 848       9.095  18.705   1.717  1.00 44.87           O  
HETATM 3816  O   HOH A 849      66.613   1.164  -4.088  1.00 64.38           O  
HETATM 3817  O   HOH A 850      58.133  23.690  -5.896  1.00 37.57           O  
HETATM 3818  O   HOH A 851      25.695   3.277  29.926  1.00 44.67           O  
HETATM 3819  O   HOH A 852      23.550  39.835  16.522  1.00 48.68           O  
HETATM 3820  O   HOH A 853      26.351  29.733  45.741  1.00 57.77           O  
HETATM 3821  O   HOH A 854      70.896  10.839  -2.786  1.00 37.03           O  
HETATM 3822  O   HOH A 855      41.559  -1.014  15.459  1.00 61.51           O  
HETATM 3823  O   HOH A 856      67.562  30.329   5.867  1.00 51.59           O  
HETATM 3824  O   HOH A 857      30.957   5.165  38.038  1.00 53.66           O  
HETATM 3825  O   HOH A 858      -2.040  29.524  10.327  1.00 46.03           O  
HETATM 3826  O   HOH A 859      25.998  36.105  24.359  1.00 50.67           O  
HETATM 3827  O   HOH A 860      30.053  10.020   8.164  1.00 41.99           O  
HETATM 3828  O   HOH A 861      -6.709  15.579  44.452  1.00 58.46           O  
HETATM 3829  O   HOH A 862      -1.837  13.751  29.769  1.00 52.94           O  
HETATM 3830  O   HOH A 863      25.906  -2.173  19.506  1.00 34.42           O  
HETATM 3831  O   HOH A 864      30.893  25.158  24.848  1.00 48.95           O  
HETATM 3832  O   HOH A 865      23.568  15.892  16.525  1.00 51.84           O  
HETATM 3833  O   HOH A 866      19.998  19.093  57.987  1.00 61.51           O  
HETATM 3834  O   HOH A 867       6.582  42.245  22.415  1.00 61.65           O  
HETATM 3835  O   HOH A 868      20.534  28.958  28.291  1.00 45.41           O  
HETATM 3836  O   HOH A 869      45.244  19.311  28.580  1.00 46.62           O  
HETATM 3837  O   HOH A 870      51.899  15.434   2.747  1.00 42.44           O  
HETATM 3838  O   HOH A 871      45.066  20.634   5.928  1.00 46.03           O  
HETATM 3839  O   HOH A 872      19.426  26.975  30.107  1.00 47.96           O  
HETATM 3840  O   HOH A 873      29.306  27.140  24.196  1.00 53.15           O  
HETATM 3841  O   HOH A 874      26.761  41.285  49.700  1.00 59.30           O  
HETATM 3842  O   HOH A 875      -3.941  27.998  19.131  1.00 45.52           O  
HETATM 3843  O   HOH A 876      50.352   5.454  25.668  1.00 61.14           O  
HETATM 3844  O   HOH A 877      11.214   0.622   7.116  1.00 60.84           O  
HETATM 3845  O   HOH A 878      25.564  29.811  16.846  1.00 56.51           O  
HETATM 3846  O   HOH A 879      36.953  -2.497  24.681  1.00 57.07           O  
HETATM 3847  O   HOH A 880      45.590   0.365  17.251  1.00 51.00           O  
HETATM 3848  O   HOH A 881      25.479  11.476  29.077  1.00 54.56           O  
HETATM 3849  O   HOH A 882      12.061  49.540  18.246  1.00 56.07           O  
HETATM 3850  O   HOH A 883      71.351  13.646  -3.262  1.00 48.99           O  
HETATM 3851  O   HOH A 884      23.023 -10.063   7.700  1.00 57.18           O  
HETATM 3852  O   HOH A 885      -0.479   7.694  18.529  1.00 58.80           O  
HETATM 3853  O   HOH A 886      41.399  -2.202  19.455  1.00 54.04           O  
HETATM 3854  O   HOH A 887      58.388   4.893   8.711  1.00 41.76           O  
HETATM 3855  O   HOH A 888       0.289  27.594  37.462  1.00 44.96           O  
HETATM 3856  O   HOH A 889       7.429  20.562  60.915  1.00 57.73           O  
HETATM 3857  O   HOH A 890       0.281   6.332  36.561  1.00 50.06           O  
HETATM 3858  O   HOH A 891      38.406  21.895  31.288  1.00 53.37           O  
HETATM 3859  O   HOH A 892      17.390  15.110  25.553  1.00 46.27           O  
HETATM 3860  O   HOH A 893      29.702   1.722  29.414  1.00 44.13           O  
HETATM 3861  O   HOH A 894      13.571   0.424  13.303  1.00 60.58           O  
HETATM 3862  O   HOH A 895       0.072  24.563  51.069  1.00 58.87           O  
HETATM 3863  O   HOH A 896      52.232  13.901  12.100  1.00 49.14           O  
HETATM 3864  O   HOH A 897      25.760  17.408  16.388  1.00 50.24           O  
HETATM 3865  O   HOH A 898      29.920  40.298  36.665  1.00 65.84           O  
HETATM 3866  O   HOH A 899      73.640  27.973   8.182  1.00 53.55           O  
HETATM 3867  O   HOH A 900      32.555  37.464  33.393  1.00 55.22           O  
HETATM 3868  O   HOH A 901      25.536  12.716  33.614  1.00 55.39           O  
HETATM 3869  O   HOH A 902      26.584  30.031  21.110  1.00 50.48           O  
HETATM 3870  O   HOH A 903      18.991   5.015  16.253  1.00 52.57           O  
HETATM 3871  O   HOH A 904      24.126  33.788  27.953  1.00 57.95           O  
HETATM 3872  O   HOH A 905      36.873  22.238  26.410  1.00 53.83           O  
CONECT  480 3566                                                                
CONECT  496 3566                                                                
CONECT  836 3566                                                                
CONECT 1290 3568                                                                
CONECT 3128 3567                                                                
CONECT 3160 3567                                                                
CONECT 3161 3567                                                                
CONECT 3561 3562 3563 3564                                                      
CONECT 3562 3561 3565                                                           
CONECT 3563 3561 3565 3568                                                      
CONECT 3564 3561                                                                
CONECT 3565 3562 3563 3598 3648                                                 
CONECT 3565 3832                                                                
CONECT 3566  480  496  836                                                      
CONECT 3567 3128 3160 3161 3574                                                 
CONECT 3567 3686                                                                
CONECT 3568 1290 3563 3752 3788                                                 
CONECT 3574 3567                                                                
CONECT 3598 3565                                                                
CONECT 3648 3565                                                                
CONECT 3686 3567                                                                
CONECT 3752 3568                                                                
CONECT 3788 3568                                                                
CONECT 3832 3565                                                                
MASTER      380    0    5   18   15    0    7    6 3871    1   24   34          
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.