HEADER    MEMBRANE PROTEIN                        21-JUL-23   8K5D              
TITLE     CRYO-EM STRUCTURE OF GSK256073 BOUND HUMAN HYDROXY-CARBOXYLIC ACID    
TITLE    2 RECEPTOR 2 (LOCAL REFINEMENT)                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN HYDROXYCARBOXYLIC ACID RECEPTOR 2;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 109A,G-PROTEIN COUPLED RECEPTOR  
COMPND   5 HM74A,NIACIN RECEPTOR 1,NICOTINIC ACID RECEPTOR;                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HCAR2, HCA2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR, G-PROTEIN, MEMBRANE PROTEIN, SIGNALING                          
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.H.PARK,N.ISHIMOTO,S.Y.PARK                                          
REVDAT   1   22-NOV-23 8K5D    0                                                
JRNL        AUTH   J.H.PARK,K.KAWAKAMI,N.ISHIMOTO,T.IKUTA,M.OHKI,T.EKIMOTO,     
JRNL        AUTH 2 M.IKEGUCHI,D.S.LEE,Y.H.LEE,J.R.H.TAME,A.INOUE,S.Y.PARK       
JRNL        TITL   STRUCTURAL BASIS FOR LIGAND RECOGNITION AND SIGNALING OF     
JRNL        TITL 2 HYDROXY-CARBOXYLIC ACID RECEPTOR 2                           
JRNL        REF    NAT COMMUN                    V.  14  7150 2023              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        DOI    10.1038/S41467-023-42764-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CRYOSPARC, EPU, CRYOSPARC, UCSF           
REMARK   3                            CHIMERAX, COOT, PHENIX, CRYOSPARC,        
REMARK   3                            CRYOSPARC, CRYOSPARC, CRYOSPARC           
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : AB INITIO MODEL                     
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.740                          
REMARK   3   NUMBER OF PARTICLES               : 153633                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 8K5D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUL-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300039565.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : GSK256073 BOUND HUMAN HYDROXY     
REMARK 245                                    -CARBOXYLIC ACID RECEPTOR 2       
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K3 (6K X 4K)             
REMARK 245   MINIMUM DEFOCUS (NM)              : 800.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 1800.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 5000.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 105000                         
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  -112                                                      
REMARK 465     PRO A  -111                                                      
REMARK 465     GLY A  -110                                                      
REMARK 465     ALA A  -109                                                      
REMARK 465     PRO A  -108                                                      
REMARK 465     ALA A  -107                                                      
REMARK 465     ASP A  -106                                                      
REMARK 465     LEU A  -105                                                      
REMARK 465     GLU A  -104                                                      
REMARK 465     ASP A  -103                                                      
REMARK 465     ASN A  -102                                                      
REMARK 465     TRP A  -101                                                      
REMARK 465     GLU A  -100                                                      
REMARK 465     THR A   -99                                                      
REMARK 465     LEU A   -98                                                      
REMARK 465     ASN A   -97                                                      
REMARK 465     ASP A   -96                                                      
REMARK 465     ASN A   -95                                                      
REMARK 465     LEU A   -94                                                      
REMARK 465     LYS A   -93                                                      
REMARK 465     VAL A   -92                                                      
REMARK 465     ILE A   -91                                                      
REMARK 465     GLU A   -90                                                      
REMARK 465     LYS A   -89                                                      
REMARK 465     ALA A   -88                                                      
REMARK 465     ASP A   -87                                                      
REMARK 465     ASN A   -86                                                      
REMARK 465     ALA A   -85                                                      
REMARK 465     ALA A   -84                                                      
REMARK 465     GLN A   -83                                                      
REMARK 465     VAL A   -82                                                      
REMARK 465     LYS A   -81                                                      
REMARK 465     ASP A   -80                                                      
REMARK 465     ALA A   -79                                                      
REMARK 465     LEU A   -78                                                      
REMARK 465     THR A   -77                                                      
REMARK 465     LYS A   -76                                                      
REMARK 465     MET A   -75                                                      
REMARK 465     ARG A   -74                                                      
REMARK 465     ALA A   -73                                                      
REMARK 465     ALA A   -72                                                      
REMARK 465     ALA A   -71                                                      
REMARK 465     LEU A   -70                                                      
REMARK 465     ASP A   -69                                                      
REMARK 465     ALA A   -68                                                      
REMARK 465     GLN A   -67                                                      
REMARK 465     LYS A   -66                                                      
REMARK 465     ALA A   -65                                                      
REMARK 465     THR A   -64                                                      
REMARK 465     PRO A   -63                                                      
REMARK 465     PRO A   -62                                                      
REMARK 465     LYS A   -61                                                      
REMARK 465     LEU A   -60                                                      
REMARK 465     GLU A   -59                                                      
REMARK 465     ASP A   -58                                                      
REMARK 465     LYS A   -57                                                      
REMARK 465     SER A   -56                                                      
REMARK 465     PRO A   -55                                                      
REMARK 465     ASP A   -54                                                      
REMARK 465     SER A   -53                                                      
REMARK 465     PRO A   -52                                                      
REMARK 465     GLU A   -51                                                      
REMARK 465     MET A   -50                                                      
REMARK 465     LYS A   -49                                                      
REMARK 465     ASP A   -48                                                      
REMARK 465     PHE A   -47                                                      
REMARK 465     ARG A   -46                                                      
REMARK 465     HIS A   -45                                                      
REMARK 465     GLY A   -44                                                      
REMARK 465     PHE A   -43                                                      
REMARK 465     ASP A   -42                                                      
REMARK 465     ILE A   -41                                                      
REMARK 465     LEU A   -40                                                      
REMARK 465     VAL A   -39                                                      
REMARK 465     GLY A   -38                                                      
REMARK 465     GLN A   -37                                                      
REMARK 465     ILE A   -36                                                      
REMARK 465     ASP A   -35                                                      
REMARK 465     ASP A   -34                                                      
REMARK 465     ALA A   -33                                                      
REMARK 465     LEU A   -32                                                      
REMARK 465     LYS A   -31                                                      
REMARK 465     LEU A   -30                                                      
REMARK 465     ALA A   -29                                                      
REMARK 465     ASN A   -28                                                      
REMARK 465     GLU A   -27                                                      
REMARK 465     GLY A   -26                                                      
REMARK 465     LYS A   -25                                                      
REMARK 465     VAL A   -24                                                      
REMARK 465     LYS A   -23                                                      
REMARK 465     GLU A   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     GLN A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     ALA A   -18                                                      
REMARK 465     ALA A   -17                                                      
REMARK 465     GLU A   -16                                                      
REMARK 465     GLN A   -15                                                      
REMARK 465     LEU A   -14                                                      
REMARK 465     LYS A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     THR A   -11                                                      
REMARK 465     ARG A   -10                                                      
REMARK 465     ASN A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A   300                                                      
REMARK 465     PHE A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     ASN A   303                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     PHE A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     ILE A   309                                                      
REMARK 465     ASN A   310                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     CYS A   312                                                      
REMARK 465     LEU A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     ARG A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 465     MET A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     ASP A   322                                                      
REMARK 465     ASN A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     ARG A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     THR A   327                                                      
REMARK 465     SER A   328                                                      
REMARK 465     VAL A   329                                                      
REMARK 465     GLU A   330                                                      
REMARK 465     LEU A   331                                                      
REMARK 465     THR A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     ASN A   336                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     ARG A   339                                                      
REMARK 465     GLY A   340                                                      
REMARK 465     ALA A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     GLU A   343                                                      
REMARK 465     ALA A   344                                                      
REMARK 465     LEU A   345                                                      
REMARK 465     MET A   346                                                      
REMARK 465     ALA A   347                                                      
REMARK 465     ASN A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     GLY A   350                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     PRO A   352                                                      
REMARK 465     TRP A   353                                                      
REMARK 465     SER A   354                                                      
REMARK 465     PRO A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     TYR A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     THR A   361                                                      
REMARK 465     SER A   362                                                      
REMARK 465     PRO A   363                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  15    CG   CD   CE   NZ                                   
REMARK 470     CYS A  19    SG                                                  
REMARK 470     ASP A  23    CG   OD1  OD2                                       
REMARK 470     PHE A  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     LEU A  56    CG   CD1  CD2                                       
REMARK 470     LYS A  60    CG   CD   CE   NZ                                   
REMARK 470     PRO A  81    CG   CD                                             
REMARK 470     MET A  84    CG   SD   CE                                        
REMARK 470     ASP A  85    CG   OD1  OD2                                       
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     MET A 106    CG   SD   CE                                        
REMARK 470     LYS A 166    CG   CD   CE   NZ                                   
REMARK 470     PHE A 186    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 225    CE   NZ                                             
REMARK 470     CYS A 266    SG                                                  
REMARK 470     ARG A 270    CG   CD   NE   CZ   NH1  NH2                        
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    SER A  58      111.23   -162.37                                   
REMARK 500    HIS A 131       68.71   -118.61                                   
REMARK 500    PHE A 180       51.29    -92.84                                   
REMARK 500    SER A 261     -128.00     59.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-36902   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF GSK256073 BOUND HUMAN HYDROXY-CARBOXYLIC ACID   
REMARK 900 RECEPTOR 2 (LOCAL REFINEMENT)                                        
DBREF  8K5D A -112     0  PDB    8K5D     8K5D          -112      0             
DBREF  8K5D A    1   363  UNP    Q8TDS4   HCAR2_HUMAN      1    363             
SEQRES   1 A  476  GLY PRO GLY ALA PRO ALA ASP LEU GLU ASP ASN TRP GLU          
SEQRES   2 A  476  THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP          
SEQRES   3 A  476  ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG          
SEQRES   4 A  476  ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS          
SEQRES   5 A  476  LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP          
SEQRES   6 A  476  PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP          
SEQRES   7 A  476  ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU          
SEQRES   8 A  476  ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN          
SEQRES   9 A  476  ALA TYR ILE GLN LYS TYR LEU GLU PHE MET ASN ARG HIS          
SEQRES  10 A  476  HIS LEU GLN ASP HIS PHE LEU GLU ILE ASP LYS LYS ASN          
SEQRES  11 A  476  CYS CYS VAL PHE ARG ASP ASP PHE ILE VAL LYS VAL LEU          
SEQRES  12 A  476  PRO PRO VAL LEU GLY LEU GLU PHE ILE PHE GLY LEU LEU          
SEQRES  13 A  476  GLY ASN GLY LEU ALA LEU TRP ILE PHE CYS PHE HIS LEU          
SEQRES  14 A  476  LYS SER TRP LYS SER SER ARG ILE PHE LEU PHE ASN LEU          
SEQRES  15 A  476  ALA VAL ALA ASP PHE LEU LEU ILE ILE CYS LEU PRO PHE          
SEQRES  16 A  476  LEU MET ASP ASN TYR VAL ARG ARG TRP ASP TRP LYS PHE          
SEQRES  17 A  476  GLY ASP ILE PRO CYS ARG LEU MET LEU PHE MET LEU ALA          
SEQRES  18 A  476  MET ASN ARG GLN GLY SER ILE ILE PHE LEU THR VAL VAL          
SEQRES  19 A  476  ALA VAL ASP ARG TYR PHE ARG VAL VAL HIS PRO HIS HIS          
SEQRES  20 A  476  ALA LEU ASN LYS ILE SER ASN ARG THR ALA ALA ILE ILE          
SEQRES  21 A  476  SER CYS LEU LEU TRP GLY ILE THR ILE GLY LEU THR VAL          
SEQRES  22 A  476  HIS LEU LEU LYS LYS LYS MET PRO ILE GLN ASN GLY GLY          
SEQRES  23 A  476  ALA ASN LEU CYS SER SER PHE SER ILE CYS HIS THR PHE          
SEQRES  24 A  476  GLN TRP HIS GLU ALA MET PHE LEU LEU GLU PHE PHE LEU          
SEQRES  25 A  476  PRO LEU GLY ILE ILE LEU PHE CYS SER ALA ARG ILE ILE          
SEQRES  26 A  476  TRP SER LEU ARG GLN ARG GLN MET ASP ARG HIS ALA LYS          
SEQRES  27 A  476  ILE LYS ARG ALA ILE THR PHE ILE MET VAL VAL ALA ILE          
SEQRES  28 A  476  VAL PHE VAL ILE CYS PHE LEU PRO SER VAL VAL VAL ARG          
SEQRES  29 A  476  ILE ARG ILE PHE TRP LEU LEU HIS THR SER GLY THR GLN          
SEQRES  30 A  476  ASN CYS GLU VAL TYR ARG SER VAL ASP LEU ALA PHE PHE          
SEQRES  31 A  476  ILE THR LEU SER PHE THR TYR MET ASN SER MET LEU ASP          
SEQRES  32 A  476  PRO VAL VAL TYR TYR PHE SER SER PRO SER PHE PRO ASN          
SEQRES  33 A  476  PHE PHE SER THR LEU ILE ASN ARG CYS LEU GLN ARG LYS          
SEQRES  34 A  476  MET THR GLY GLU PRO ASP ASN ASN ARG SER THR SER VAL          
SEQRES  35 A  476  GLU LEU THR GLY ASP PRO ASN LYS THR ARG GLY ALA PRO          
SEQRES  36 A  476  GLU ALA LEU MET ALA ASN SER GLY GLU PRO TRP SER PRO          
SEQRES  37 A  476  SER TYR LEU GLY PRO THR SER PRO                              
HET    OKL  A 401      17                                                       
HETNAM     OKL 8-CHLORANYL-3-PENTYL-7H-PURINE-2,6-DIONE                         
FORMUL   2  OKL    C10 H13 CL N4 O2                                             
HELIX    1 AA1 VAL A   29  PHE A   54  1                                  26    
HELIX    2 AA2 LYS A   60  ARG A   89  1                                  30    
HELIX    3 AA3 ASP A   97  VAL A  130  1                                  34    
HELIX    4 AA4 HIS A  134  LYS A  138  5                                   5    
HELIX    5 AA5 SER A  140  LYS A  166  1                                  27    
HELIX    6 AA6 GLN A  187  ARG A  218  1                                  32    
HELIX    7 AA7 HIS A  223  THR A  260  1                                  38    
HELIX    8 AA8 CYS A  266  TYR A  294  1                                  29    
SHEET    1 AA1 2 PHE A  10  GLU A  12  0                                        
SHEET    2 AA1 2 ASN A  17  CYS A  19 -1  O  CYS A  18   N  LEU A  11           
SHEET    1 AA2 2 ILE A 169  ASN A 171  0                                        
SHEET    2 AA2 2 ALA A 174  LEU A 176 -1  O  ALA A 174   N  ASN A 171           
SSBOND   1 CYS A   18    CYS A  183                          1555   1555  2.03  
SSBOND   2 CYS A  100    CYS A  177                          1555   1555  2.03  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   HIS A   9     113.783 114.225  82.520  1.00102.45           N  
ATOM      2  CA  HIS A   9     114.365 115.546  82.318  1.00102.45           C  
ATOM      3  C   HIS A   9     113.393 116.652  82.720  1.00102.45           C  
ATOM      4  O   HIS A   9     113.272 116.984  83.899  1.00102.45           O  
ATOM      5  CB  HIS A   9     114.798 115.721  80.859  1.00102.45           C  
ATOM      6  CG  HIS A   9     114.000 114.906  79.889  1.00102.45           C  
ATOM      7  ND1 HIS A   9     112.666 115.141  79.636  1.00102.45           N  
ATOM      8  CD2 HIS A   9     114.352 113.858  79.107  1.00102.45           C  
ATOM      9  CE1 HIS A   9     112.229 114.273  78.741  1.00102.45           C  
ATOM     10  NE2 HIS A   9     113.232 113.483  78.404  1.00102.45           N  
ATOM     11  N   PHE A  10     112.705 117.223  81.734  1.00103.45           N  
ATOM     12  CA  PHE A  10     111.764 118.301  82.007  1.00103.45           C  
ATOM     13  C   PHE A  10     110.554 117.779  82.773  1.00103.45           C  
ATOM     14  O   PHE A  10     110.100 116.652  82.561  1.00103.45           O  
ATOM     15  CB  PHE A  10     111.318 118.958  80.701  1.00103.45           C  
ATOM     16  CG  PHE A  10     112.356 118.921  79.616  1.00103.45           C  
ATOM     17  CD1 PHE A  10     113.530 119.646  79.738  1.00103.45           C  
ATOM     18  CD2 PHE A  10     112.157 118.165  78.474  1.00103.45           C  
ATOM     19  CE1 PHE A  10     114.486 119.615  78.741  1.00103.45           C  
ATOM     20  CE2 PHE A  10     113.110 118.130  77.473  1.00103.45           C  
ATOM     21  CZ  PHE A  10     114.276 118.857  77.607  1.00103.45           C  
ATOM     22  N   LEU A  11     110.033 118.613  83.670  1.00 99.52           N  
ATOM     23  CA  LEU A  11     108.871 118.255  84.471  1.00 99.52           C  
ATOM     24  C   LEU A  11     108.197 119.533  84.947  1.00 99.52           C  
ATOM     25  O   LEU A  11     108.801 120.610  84.954  1.00 99.52           O  
ATOM     26  CB  LEU A  11     109.261 117.367  85.659  1.00 99.52           C  
ATOM     27  CG  LEU A  11     108.147 116.572  86.345  1.00 99.52           C  
ATOM     28  CD1 LEU A  11     107.227 115.929  85.320  1.00 99.52           C  
ATOM     29  CD2 LEU A  11     108.735 115.523  87.274  1.00 99.52           C  
ATOM     30  N   GLU A  12     106.933 119.401  85.343  1.00102.42           N  
ATOM     31  CA  GLU A  12     106.152 120.512  85.872  1.00102.42           C  
ATOM     32  C   GLU A  12     105.679 120.159  87.275  1.00102.42           C  
ATOM     33  O   GLU A  12     105.039 119.121  87.476  1.00102.42           O  
ATOM     34  CB  GLU A  12     104.963 120.833  84.963  1.00102.42           C  
ATOM     35  CG  GLU A  12     104.087 121.976  85.457  1.00102.42           C  
ATOM     36  CD  GLU A  12     102.951 121.502  86.343  1.00102.42           C  
ATOM     37  OE1 GLU A  12     102.032 120.833  85.825  1.00102.42           O  
ATOM     38  OE2 GLU A  12     102.980 121.793  87.557  1.00102.42           O  
ATOM     39  N   ILE A  13     105.994 121.023  88.236  1.00 99.27           N  
ATOM     40  CA  ILE A  13     105.571 120.875  89.623  1.00 99.27           C  
ATOM     41  C   ILE A  13     104.909 122.178  90.046  1.00 99.27           C  
ATOM     42  O   ILE A  13     105.566 123.226  90.080  1.00 99.27           O  
ATOM     43  CB  ILE A  13     106.750 120.540  90.552  1.00 99.27           C  
ATOM     44  CG1 ILE A  13     107.295 119.145  90.241  1.00 99.27           C  
ATOM     45  CG2 ILE A  13     106.327 120.636  92.007  1.00 99.27           C  
ATOM     46  CD1 ILE A  13     108.545 119.157  89.391  1.00 99.27           C  
ATOM     47  N   ASP A  14     103.617 122.112  90.371  1.00102.00           N  
ATOM     48  CA  ASP A  14     102.838 123.281  90.784  1.00102.00           C  
ATOM     49  C   ASP A  14     102.965 124.417  89.771  1.00102.00           C  
ATOM     50  O   ASP A  14     103.256 125.564  90.117  1.00102.00           O  
ATOM     51  CB  ASP A  14     103.248 123.745  92.183  1.00102.00           C  
ATOM     52  CG  ASP A  14     103.228 122.621  93.197  1.00102.00           C  
ATOM     53  OD1 ASP A  14     103.305 121.445  92.783  1.00102.00           O  
ATOM     54  OD2 ASP A  14     103.136 122.913  94.408  1.00102.00           O  
ATOM     55  N   LYS A  15     102.743 124.079  88.498  1.00 97.58           N  
ATOM     56  CA  LYS A  15     102.873 125.027  87.389  1.00 97.58           C  
ATOM     57  C   LYS A  15     104.259 125.668  87.375  1.00 97.58           C  
ATOM     58  O   LYS A  15     104.415 126.852  87.070  1.00 97.58           O  
ATOM     59  CB  LYS A  15     101.777 126.094  87.439  1.00 97.58           C  
ATOM     60  N   LYS A  16     105.274 124.874  87.707  1.00 92.95           N  
ATOM     61  CA  LYS A  16     106.650 125.341  87.797  1.00 92.95           C  
ATOM     62  C   LYS A  16     107.531 124.421  86.967  1.00 92.95           C  
ATOM     63  O   LYS A  16     107.502 123.203  87.153  1.00 92.95           O  
ATOM     64  CB  LYS A  16     107.121 125.361  89.255  1.00 92.95           C  
ATOM     65  CG  LYS A  16     108.363 126.188  89.508  1.00 92.95           C  
ATOM     66  CD  LYS A  16     108.303 126.854  90.873  1.00 92.95           C  
ATOM     67  CE  LYS A  16     107.089 127.759  90.995  1.00 92.95           C  
ATOM     68  NZ  LYS A  16     107.064 128.478  92.298  1.00 92.95           N  
ATOM     69  N   ASN A  17     108.313 124.999  86.059  1.00 90.81           N  
ATOM     70  CA  ASN A  17     109.169 124.209  85.179  1.00 90.81           C  
ATOM     71  C   ASN A  17     110.438 123.821  85.930  1.00 90.81           C  
ATOM     72  O   ASN A  17     111.247 124.683  86.287  1.00 90.81           O  
ATOM     73  CB  ASN A  17     109.485 124.989  83.906  1.00 90.81           C  
ATOM     74  CG  ASN A  17     109.655 126.474  84.156  1.00 90.81           C  
ATOM     75  OD1 ASN A  17     109.835 126.908  85.293  1.00 90.81           O  
ATOM     76  ND2 ASN A  17     109.592 127.264  83.090  1.00 90.81           N  
ATOM     77  N   CYS A  18     110.614 122.521  86.169  1.00 92.41           N  
ATOM     78  CA  CYS A  18     111.755 121.999  86.904  1.00 92.41           C  
ATOM     79  C   CYS A  18     112.414 120.891  86.096  1.00 92.41           C  
ATOM     80  O   CYS A  18     111.814 120.317  85.184  1.00 92.41           O  
ATOM     81  CB  CYS A  18     111.343 121.464  88.282  1.00 92.41           C  
ATOM     82  SG  CYS A  18     110.208 122.531  89.194  1.00 92.41           S  
ATOM     83  N   CYS A  19     113.666 120.593  86.443  1.00 86.47           N  
ATOM     84  CA  CYS A  19     114.463 119.577  85.755  1.00 86.47           C  
ATOM     85  C   CYS A  19     115.042 118.625  86.798  1.00 86.47           C  
ATOM     86  O   CYS A  19     116.152 118.833  87.292  1.00 86.47           O  
ATOM     87  CB  CYS A  19     115.559 120.223  84.914  1.00 86.47           C  
ATOM     88  N   VAL A  20     114.289 117.577  87.127  1.00 87.15           N  
ATOM     89  CA  VAL A  20     114.758 116.552  88.053  1.00 87.15           C  
ATOM     90  C   VAL A  20     115.690 115.610  87.305  1.00 87.15           C  
ATOM     91  O   VAL A  20     115.744 115.628  86.070  1.00 87.15           O  
ATOM     92  CB  VAL A  20     113.582 115.785  88.684  1.00 87.15           C  
ATOM     93  CG1 VAL A  20     112.474 116.746  89.076  1.00 87.15           C  
ATOM     94  CG2 VAL A  20     113.062 114.728  87.724  1.00 87.15           C  
ATOM     95  N   PHE A  21     116.433 114.785  88.039  1.00 81.87           N  
ATOM     96  CA  PHE A  21     117.368 113.858  87.411  1.00 81.87           C  
ATOM     97  C   PHE A  21     117.570 112.646  88.306  1.00 81.87           C  
ATOM     98  O   PHE A  21     118.020 112.781  89.447  1.00 81.87           O  
ATOM     99  CB  PHE A  21     118.704 114.539  87.120  1.00 81.87           C  
ATOM    100  CG  PHE A  21     118.847 114.994  85.700  1.00 81.87           C  
ATOM    101  CD1 PHE A  21     118.459 114.169  84.657  1.00 81.87           C  
ATOM    102  CD2 PHE A  21     119.365 116.241  85.405  1.00 81.87           C  
ATOM    103  CE1 PHE A  21     118.585 114.580  83.346  1.00 81.87           C  
ATOM    104  CE2 PHE A  21     119.495 116.658  84.096  1.00 81.87           C  
ATOM    105  CZ  PHE A  21     119.104 115.826  83.064  1.00 81.87           C  
ATOM    106  N   ARG A  22     117.238 111.470  87.780  1.00 75.96           N  
ATOM    107  CA  ARG A  22     117.473 110.189  88.439  1.00 75.96           C  
ATOM    108  C   ARG A  22     118.572 109.479  87.654  1.00 75.96           C  
ATOM    109  O   ARG A  22     118.301 108.764  86.688  1.00 75.96           O  
ATOM    110  CB  ARG A  22     116.199 109.354  88.490  1.00 75.96           C  
ATOM    111  CG  ARG A  22     115.404 109.489  89.773  1.00 75.96           C  
ATOM    112  CD  ARG A  22     114.502 108.283  89.959  1.00 75.96           C  
ATOM    113  NE  ARG A  22     115.161 107.055  89.531  1.00 75.96           N  
ATOM    114  CZ  ARG A  22     114.528 105.988  89.064  1.00 75.96           C  
ATOM    115  NH1 ARG A  22     113.213 105.969  88.930  1.00 75.96           N  
ATOM    116  NH2 ARG A  22     115.233 104.916  88.716  1.00 75.96           N  
ATOM    117  N   ASP A  23     119.815 109.679  88.075  1.00 73.95           N  
ATOM    118  CA  ASP A  23     120.972 109.142  87.376  1.00 73.95           C  
ATOM    119  C   ASP A  23     121.698 108.135  88.257  1.00 73.95           C  
ATOM    120  O   ASP A  23     121.286 107.841  89.382  1.00 73.95           O  
ATOM    121  CB  ASP A  23     121.929 110.264  86.953  1.00 73.95           C  
ATOM    122  N   ASP A  24     122.785 107.592  87.721  1.00 71.29           N  
ATOM    123  CA  ASP A  24     123.637 106.684  88.474  1.00 71.29           C  
ATOM    124  C   ASP A  24     124.699 107.500  89.208  1.00 71.29           C  
ATOM    125  O   ASP A  24     124.627 108.730  89.282  1.00 71.29           O  
ATOM    126  CB  ASP A  24     124.243 105.632  87.549  1.00 71.29           C  
ATOM    127  CG  ASP A  24     124.587 104.347  88.276  1.00 71.29           C  
ATOM    128  OD1 ASP A  24     123.820 103.950  89.178  1.00 71.29           O  
ATOM    129  OD2 ASP A  24     125.625 103.734  87.948  1.00 71.29           O  
ATOM    130  N   PHE A  25     125.688 106.809  89.782  1.00 69.10           N  
ATOM    131  CA  PHE A  25     126.748 107.410  90.589  1.00 69.10           C  
ATOM    132  C   PHE A  25     126.183 108.026  91.864  1.00 69.10           C  
ATOM    133  O   PHE A  25     126.927 108.598  92.667  1.00 69.10           O  
ATOM    134  CB  PHE A  25     127.531 108.453  89.786  1.00 69.10           C  
ATOM    135  N   ILE A  26     124.869 107.909  92.060  1.00 66.44           N  
ATOM    136  CA  ILE A  26     124.235 108.311  93.308  1.00 66.44           C  
ATOM    137  C   ILE A  26     124.176 107.160  94.305  1.00 66.44           C  
ATOM    138  O   ILE A  26     124.144 107.410  95.520  1.00 66.44           O  
ATOM    139  CB  ILE A  26     122.816 108.862  93.058  1.00 66.44           C  
ATOM    140  CG1 ILE A  26     122.751 109.611  91.728  1.00 66.44           C  
ATOM    141  CG2 ILE A  26     122.382 109.768  94.193  1.00 66.44           C  
ATOM    142  CD1 ILE A  26     121.407 110.250  91.458  1.00 66.44           C  
ATOM    143  N   VAL A  27     124.170 105.916  93.834  1.00 65.97           N  
ATOM    144  CA  VAL A  27     124.115 104.750  94.705  1.00 65.97           C  
ATOM    145  C   VAL A  27     125.527 104.224  94.906  1.00 65.97           C  
ATOM    146  O   VAL A  27     125.723 103.073  95.311  1.00 65.97           O  
ATOM    147  CB  VAL A  27     123.196 103.665  94.119  1.00 65.97           C  
ATOM    148  CG1 VAL A  27     121.767 104.168  94.049  1.00 65.97           C  
ATOM    149  CG2 VAL A  27     123.685 103.248  92.744  1.00 65.97           C  
ATOM    150  N   LYS A  28     126.520 105.063  94.622  1.00 74.38           N  
ATOM    151  CA  LYS A  28     127.914 104.657  94.737  1.00 74.38           C  
ATOM    152  C   LYS A  28     128.616 105.406  95.862  1.00 74.38           C  
ATOM    153  O   LYS A  28     129.313 104.797  96.679  1.00 74.38           O  
ATOM    154  CB  LYS A  28     128.646 104.885  93.412  1.00 74.38           C  
ATOM    155  N   VAL A  29     128.447 106.726  95.909  1.00 67.43           N  
ATOM    156  CA  VAL A  29     129.136 107.550  96.895  1.00 67.43           C  
ATOM    157  C   VAL A  29     128.235 107.849  98.089  1.00 67.43           C  
ATOM    158  O   VAL A  29     128.634 107.644  99.240  1.00 67.43           O  
ATOM    159  CB  VAL A  29     129.665 108.846  96.251  1.00 67.43           C  
ATOM    160  CG1 VAL A  29     128.571 109.551  95.461  1.00 67.43           C  
ATOM    161  CG2 VAL A  29     130.231 109.770  97.316  1.00 67.43           C  
ATOM    162  N   LEU A  30     127.015 108.315  97.824  1.00 66.27           N  
ATOM    163  CA  LEU A  30     126.121 108.790  98.881  1.00 66.27           C  
ATOM    164  C   LEU A  30     125.767 107.748  99.937  1.00 66.27           C  
ATOM    165  O   LEU A  30     125.825 108.078 101.132  1.00 66.27           O  
ATOM    166  CB  LEU A  30     124.861 109.374  98.230  1.00 66.27           C  
ATOM    167  CG  LEU A  30     124.999 110.872  97.966  1.00 66.27           C  
ATOM    168  CD1 LEU A  30     124.033 111.342  96.907  1.00 66.27           C  
ATOM    169  CD2 LEU A  30     124.763 111.624  99.259  1.00 66.27           C  
ATOM    170  N   PRO A  31     125.393 106.516  99.605  1.00 66.20           N  
ATOM    171  CA  PRO A  31     125.076 105.541 100.670  1.00 66.20           C  
ATOM    172  C   PRO A  31     126.275 105.093 101.500  1.00 66.20           C  
ATOM    173  O   PRO A  31     126.128 104.983 102.728  1.00 66.20           O  
ATOM    174  CB  PRO A  31     124.391 104.385  99.917  1.00 66.20           C  
ATOM    175  CG  PRO A  31     124.493 104.710  98.456  1.00 66.20           C  
ATOM    176  CD  PRO A  31     125.386 105.879  98.275  1.00 66.20           C  
ATOM    177  N   PRO A  32     127.486 104.815 100.924  1.00 70.08           N  
ATOM    178  CA  PRO A  32     128.618 104.540 101.824  1.00 70.08           C  
ATOM    179  C   PRO A  32     128.953 105.661 102.796  1.00 70.08           C  
ATOM    180  O   PRO A  32     129.264 105.383 103.958  1.00 70.08           O  
ATOM    181  CB  PRO A  32     129.782 104.280 100.862  1.00 70.08           C  
ATOM    182  CG  PRO A  32     129.152 103.729  99.685  1.00 70.08           C  
ATOM    183  CD  PRO A  32     127.844 104.441  99.543  1.00 70.08           C  
ATOM    184  N   VAL A  33     128.904 106.922 102.360  1.00 68.33           N  
ATOM    185  CA  VAL A  33     129.218 108.004 103.290  1.00 68.33           C  
ATOM    186  C   VAL A  33     128.097 108.168 104.310  1.00 68.33           C  
ATOM    187  O   VAL A  33     128.354 108.381 105.500  1.00 68.33           O  
ATOM    188  CB  VAL A  33     129.517 109.321 102.544  1.00 68.33           C  
ATOM    189  CG1 VAL A  33     128.418 109.671 101.571  1.00 68.33           C  
ATOM    190  CG2 VAL A  33     129.736 110.457 103.533  1.00 68.33           C  
ATOM    191  N   LEU A  34     126.840 108.057 103.868  1.00 68.26           N  
ATOM    192  CA  LEU A  34     125.718 108.232 104.786  1.00 68.26           C  
ATOM    193  C   LEU A  34     125.695 107.149 105.858  1.00 68.26           C  
ATOM    194  O   LEU A  34     125.378 107.430 107.019  1.00 68.26           O  
ATOM    195  CB  LEU A  34     124.399 108.250 104.016  1.00 68.26           C  
ATOM    196  CG  LEU A  34     124.023 109.559 103.321  1.00 68.26           C  
ATOM    197  CD1 LEU A  34     122.536 109.586 103.014  1.00 68.26           C  
ATOM    198  CD2 LEU A  34     124.419 110.754 104.170  1.00 68.26           C  
ATOM    199  N   GLY A  35     126.017 105.907 105.492  1.00 70.71           N  
ATOM    200  CA  GLY A  35     126.017 104.840 106.482  1.00 70.71           C  
ATOM    201  C   GLY A  35     127.041 105.063 107.578  1.00 70.71           C  
ATOM    202  O   GLY A  35     126.741 104.917 108.768  1.00 70.71           O  
ATOM    203  N   LEU A  36     128.268 105.422 107.193  1.00 70.90           N  
ATOM    204  CA  LEU A  36     129.292 105.700 108.192  1.00 70.90           C  
ATOM    205  C   LEU A  36     128.944 106.939 109.005  1.00 70.90           C  
ATOM    206  O   LEU A  36     129.199 106.975 110.216  1.00 70.90           O  
ATOM    207  CB  LEU A  36     130.662 105.832 107.516  1.00 70.90           C  
ATOM    208  CG  LEU A  36     131.164 107.136 106.885  1.00 70.90           C  
ATOM    209  CD1 LEU A  36     131.785 108.083 107.909  1.00 70.90           C  
ATOM    210  CD2 LEU A  36     132.155 106.832 105.771  1.00 70.90           C  
ATOM    211  N   GLU A  37     128.348 107.950 108.367  1.00 67.15           N  
ATOM    212  CA  GLU A  37     127.881 109.118 109.103  1.00 67.15           C  
ATOM    213  C   GLU A  37     126.889 108.717 110.182  1.00 67.15           C  
ATOM    214  O   GLU A  37     126.993 109.159 111.330  1.00 67.15           O  
ATOM    215  CB  GLU A  37     127.240 110.116 108.140  1.00 67.15           C  
ATOM    216  CG  GLU A  37     128.226 110.937 107.334  1.00 67.15           C  
ATOM    217  CD  GLU A  37     128.357 112.353 107.840  1.00 67.15           C  
ATOM    218  OE1 GLU A  37     128.599 113.253 107.010  1.00 67.15           O  
ATOM    219  OE2 GLU A  37     128.216 112.568 109.061  1.00 67.15           O  
ATOM    220  N   PHE A  38     125.924 107.869 109.828  1.00 72.54           N  
ATOM    221  CA  PHE A  38     124.922 107.422 110.787  1.00 72.54           C  
ATOM    222  C   PHE A  38     125.555 106.626 111.922  1.00 72.54           C  
ATOM    223  O   PHE A  38     125.274 106.884 113.098  1.00 72.54           O  
ATOM    224  CB  PHE A  38     123.863 106.595 110.061  1.00 72.54           C  
ATOM    225  CG  PHE A  38     122.914 105.878 110.971  1.00 72.54           C  
ATOM    226  CD1 PHE A  38     122.043 106.583 111.781  1.00 72.54           C  
ATOM    227  CD2 PHE A  38     122.877 104.496 110.998  1.00 72.54           C  
ATOM    228  CE1 PHE A  38     121.160 105.921 112.611  1.00 72.54           C  
ATOM    229  CE2 PHE A  38     121.997 103.829 111.826  1.00 72.54           C  
ATOM    230  CZ  PHE A  38     121.136 104.542 112.631  1.00 72.54           C  
ATOM    231  N   ILE A  39     126.429 105.671 111.593  1.00 76.24           N  
ATOM    232  CA  ILE A  39     126.986 104.802 112.627  1.00 76.24           C  
ATOM    233  C   ILE A  39     128.032 105.498 113.489  1.00 76.24           C  
ATOM    234  O   ILE A  39     128.359 104.994 114.570  1.00 76.24           O  
ATOM    235  CB  ILE A  39     127.586 103.518 112.029  1.00 76.24           C  
ATOM    236  CG1 ILE A  39     128.922 103.813 111.343  1.00 76.24           C  
ATOM    237  CG2 ILE A  39     126.595 102.842 111.093  1.00 76.24           C  
ATOM    238  CD1 ILE A  39     129.556 102.602 110.696  1.00 76.24           C  
ATOM    239  N   PHE A  40     128.574 106.635 113.053  1.00 75.75           N  
ATOM    240  CA  PHE A  40     129.443 107.412 113.929  1.00 75.75           C  
ATOM    241  C   PHE A  40     128.672 108.445 114.736  1.00 75.75           C  
ATOM    242  O   PHE A  40     128.973 108.653 115.923  1.00 75.75           O  
ATOM    243  CB  PHE A  40     130.537 108.111 113.115  1.00 75.75           C  
ATOM    244  CG  PHE A  40     131.699 107.222 112.756  1.00 75.75           C  
ATOM    245  CD1 PHE A  40     132.964 107.756 112.580  1.00 75.75           C  
ATOM    246  CD2 PHE A  40     131.528 105.857 112.593  1.00 75.75           C  
ATOM    247  CE1 PHE A  40     134.035 106.948 112.249  1.00 75.75           C  
ATOM    248  CE2 PHE A  40     132.596 105.044 112.262  1.00 75.75           C  
ATOM    249  CZ  PHE A  40     133.850 105.590 112.090  1.00 75.75           C  
ATOM    250  N   GLY A  41     127.682 109.093 114.118  1.00 73.45           N  
ATOM    251  CA  GLY A  41     126.862 110.043 114.842  1.00 73.45           C  
ATOM    252  C   GLY A  41     126.054 109.388 115.941  1.00 73.45           C  
ATOM    253  O   GLY A  41     125.841 109.986 116.996  1.00 73.45           O  
ATOM    254  N   LEU A  42     125.599 108.151 115.718  1.00 74.16           N  
ATOM    255  CA  LEU A  42     124.897 107.435 116.777  1.00 74.16           C  
ATOM    256  C   LEU A  42     125.747 107.359 118.035  1.00 74.16           C  
ATOM    257  O   LEU A  42     125.312 107.772 119.113  1.00 74.16           O  
ATOM    258  CB  LEU A  42     124.518 106.030 116.312  1.00 74.16           C  
ATOM    259  CG  LEU A  42     123.243 105.846 115.496  1.00 74.16           C  
ATOM    260  CD1 LEU A  42     122.773 104.409 115.627  1.00 74.16           C  
ATOM    261  CD2 LEU A  42     122.161 106.811 115.950  1.00 74.16           C  
ATOM    262  N   LEU A  43     126.981 106.869 117.907  1.00 75.26           N  
ATOM    263  CA  LEU A  43     127.839 106.721 119.077  1.00 75.26           C  
ATOM    264  C   LEU A  43     128.188 108.074 119.685  1.00 75.26           C  
ATOM    265  O   LEU A  43     128.096 108.254 120.907  1.00 75.26           O  
ATOM    266  CB  LEU A  43     129.106 105.955 118.701  1.00 75.26           C  
ATOM    267  CG  LEU A  43     128.894 104.749 117.785  1.00 75.26           C  
ATOM    268  CD1 LEU A  43     130.226 104.188 117.309  1.00 75.26           C  
ATOM    269  CD2 LEU A  43     128.078 103.679 118.492  1.00 75.26           C  
ATOM    270  N   GLY A  44     128.582 109.041 118.850  1.00 76.19           N  
ATOM    271  CA  GLY A  44     128.970 110.337 119.383  1.00 76.19           C  
ATOM    272  C   GLY A  44     127.842 111.035 120.121  1.00 76.19           C  
ATOM    273  O   GLY A  44     128.015 111.487 121.258  1.00 76.19           O  
ATOM    274  N   ASN A  45     126.663 111.105 119.501  1.00 68.92           N  
ATOM    275  CA  ASN A  45     125.535 111.781 120.118  1.00 68.92           C  
ATOM    276  C   ASN A  45     124.974 110.995 121.292  1.00 68.92           C  
ATOM    277  O   ASN A  45     124.481 111.601 122.247  1.00 68.92           O  
ATOM    278  CB  ASN A  45     124.449 112.033 119.073  1.00 68.92           C  
ATOM    279  CG  ASN A  45     124.696 113.294 118.277  1.00 68.92           C  
ATOM    280  OD1 ASN A  45     123.785 113.848 117.667  1.00 68.92           O  
ATOM    281  ND2 ASN A  45     125.937 113.755 118.275  1.00 68.92           N  
ATOM    282  N   GLY A  46     125.047 109.663 121.258  1.00 71.34           N  
ATOM    283  CA  GLY A  46     124.638 108.889 122.415  1.00 71.34           C  
ATOM    284  C   GLY A  46     125.523 109.147 123.616  1.00 71.34           C  
ATOM    285  O   GLY A  46     125.031 109.320 124.732  1.00 71.34           O  
ATOM    286  N   LEU A  47     126.841 109.196 123.402  1.00 73.90           N  
ATOM    287  CA  LEU A  47     127.739 109.536 124.500  1.00 73.90           C  
ATOM    288  C   LEU A  47     127.507 110.959 124.992  1.00 73.90           C  
ATOM    289  O   LEU A  47     127.533 111.206 126.204  1.00 73.90           O  
ATOM    290  CB  LEU A  47     129.194 109.351 124.072  1.00 73.90           C  
ATOM    291  CG  LEU A  47     130.237 109.597 125.164  1.00 73.90           C  
ATOM    292  CD1 LEU A  47     129.895 108.811 126.418  1.00 73.90           C  
ATOM    293  CD2 LEU A  47     131.628 109.236 124.667  1.00 73.90           C  
ATOM    294  N   ALA A  48     127.272 111.903 124.074  1.00 73.57           N  
ATOM    295  CA  ALA A  48     126.998 113.276 124.487  1.00 73.57           C  
ATOM    296  C   ALA A  48     125.729 113.363 125.327  1.00 73.57           C  
ATOM    297  O   ALA A  48     125.717 114.003 126.384  1.00 73.57           O  
ATOM    298  CB  ALA A  48     126.892 114.181 123.260  1.00 73.57           C  
ATOM    299  N   LEU A  49     124.655 112.707 124.885  1.00 68.30           N  
ATOM    300  CA  LEU A  49     123.404 112.753 125.632  1.00 68.30           C  
ATOM    301  C   LEU A  49     123.512 112.007 126.954  1.00 68.30           C  
ATOM    302  O   LEU A  49     122.869 112.395 127.935  1.00 68.30           O  
ATOM    303  CB  LEU A  49     122.267 112.186 124.783  1.00 68.30           C  
ATOM    304  CG  LEU A  49     121.627 113.179 123.811  1.00 68.30           C  
ATOM    305  CD1 LEU A  49     120.720 112.462 122.826  1.00 68.30           C  
ATOM    306  CD2 LEU A  49     120.860 114.252 124.562  1.00 68.30           C  
ATOM    307  N   TRP A  50     124.314 110.941 127.004  1.00 78.98           N  
ATOM    308  CA  TRP A  50     124.544 110.244 128.265  1.00 78.98           C  
ATOM    309  C   TRP A  50     125.272 111.144 129.254  1.00 78.98           C  
ATOM    310  O   TRP A  50     124.875 111.255 130.420  1.00 78.98           O  
ATOM    311  CB  TRP A  50     125.334 108.959 128.006  1.00 78.98           C  
ATOM    312  CG  TRP A  50     125.647 108.141 129.229  1.00 78.98           C  
ATOM    313  CD1 TRP A  50     125.100 108.271 130.473  1.00 78.98           C  
ATOM    314  CD2 TRP A  50     126.584 107.061 129.315  1.00 78.98           C  
ATOM    315  NE1 TRP A  50     125.640 107.342 131.327  1.00 78.98           N  
ATOM    316  CE2 TRP A  50     126.553 106.585 130.640  1.00 78.98           C  
ATOM    317  CE3 TRP A  50     127.445 106.449 128.399  1.00 78.98           C  
ATOM    318  CZ2 TRP A  50     127.350 105.528 131.072  1.00 78.98           C  
ATOM    319  CZ3 TRP A  50     128.235 105.400 128.830  1.00 78.98           C  
ATOM    320  CH2 TRP A  50     128.183 104.950 130.154  1.00 78.98           C  
ATOM    321  N   ILE A  51     126.339 111.809 128.804  1.00 78.65           N  
ATOM    322  CA  ILE A  51     127.072 112.712 129.684  1.00 78.65           C  
ATOM    323  C   ILE A  51     126.283 113.967 130.017  1.00 78.65           C  
ATOM    324  O   ILE A  51     126.617 114.657 130.986  1.00 78.65           O  
ATOM    325  CB  ILE A  51     128.437 113.087 129.068  1.00 78.65           C  
ATOM    326  CG1 ILE A  51     129.484 113.270 130.168  1.00 78.65           C  
ATOM    327  CG2 ILE A  51     128.331 114.350 128.230  1.00 78.65           C  
ATOM    328  CD1 ILE A  51     130.131 111.980 130.619  1.00 78.65           C  
ATOM    329  N   PHE A  52     125.245 114.282 129.243  1.00 73.70           N  
ATOM    330  CA  PHE A  52     124.434 115.465 129.514  1.00 73.70           C  
ATOM    331  C   PHE A  52     123.284 115.167 130.474  1.00 73.70           C  
ATOM    332  O   PHE A  52     123.208 115.748 131.561  1.00 73.70           O  
ATOM    333  CB  PHE A  52     123.891 116.037 128.199  1.00 73.70           C  
ATOM    334  CG  PHE A  52     124.690 117.186 127.660  1.00 73.70           C  
ATOM    335  CD1 PHE A  52     126.014 117.016 127.296  1.00 73.70           C  
ATOM    336  CD2 PHE A  52     124.117 118.436 127.517  1.00 73.70           C  
ATOM    337  CE1 PHE A  52     126.751 118.072 126.801  1.00 73.70           C  
ATOM    338  CE2 PHE A  52     124.849 119.495 127.022  1.00 73.70           C  
ATOM    339  CZ  PHE A  52     126.168 119.313 126.664  1.00 73.70           C  
ATOM    340  N   CYS A  53     122.383 114.265 130.082  1.00 81.69           N  
ATOM    341  CA  CYS A  53     121.156 114.059 130.847  1.00 81.69           C  
ATOM    342  C   CYS A  53     121.418 113.314 132.152  1.00 81.69           C  
ATOM    343  O   CYS A  53     120.925 113.713 133.213  1.00 81.69           O  
ATOM    344  CB  CYS A  53     120.132 113.307 129.998  1.00 81.69           C  
ATOM    345  SG  CYS A  53     118.959 114.368 129.125  1.00 81.69           S  
ATOM    346  N   PHE A  54     122.192 112.230 132.096  1.00 86.57           N  
ATOM    347  CA  PHE A  54     122.297 111.302 133.220  1.00 86.57           C  
ATOM    348  C   PHE A  54     123.558 111.512 134.052  1.00 86.57           C  
ATOM    349  O   PHE A  54     123.473 111.784 135.252  1.00 86.57           O  
ATOM    350  CB  PHE A  54     122.242 109.851 132.714  1.00 86.57           C  
ATOM    351  CG  PHE A  54     120.973 109.496 131.984  1.00 86.57           C  
ATOM    352  CD1 PHE A  54     119.869 110.332 132.014  1.00 86.57           C  
ATOM    353  CD2 PHE A  54     120.891 108.317 131.262  1.00 86.57           C  
ATOM    354  CE1 PHE A  54     118.709 109.998 131.342  1.00 86.57           C  
ATOM    355  CE2 PHE A  54     119.734 107.978 130.587  1.00 86.57           C  
ATOM    356  CZ  PHE A  54     118.642 108.820 130.628  1.00 86.57           C  
ATOM    357  N   HIS A  55     124.734 111.393 133.431  1.00 83.44           N  
ATOM    358  CA  HIS A  55     125.971 111.320 134.202  1.00 83.44           C  
ATOM    359  C   HIS A  55     126.365 112.652 134.825  1.00 83.44           C  
ATOM    360  O   HIS A  55     127.187 112.666 135.746  1.00 83.44           O  
ATOM    361  CB  HIS A  55     127.111 110.807 133.324  1.00 83.44           C  
ATOM    362  CG  HIS A  55     128.219 110.160 134.095  1.00 83.44           C  
ATOM    363  ND1 HIS A  55     129.374 110.828 134.441  1.00 83.44           N  
ATOM    364  CD2 HIS A  55     128.346 108.907 134.591  1.00 83.44           C  
ATOM    365  CE1 HIS A  55     130.166 110.013 135.114  1.00 83.44           C  
ATOM    366  NE2 HIS A  55     129.566 108.841 135.220  1.00 83.44           N  
ATOM    367  N   LEU A  56     125.809 113.762 134.351  1.00 79.51           N  
ATOM    368  CA  LEU A  56     126.118 115.075 134.898  1.00 79.51           C  
ATOM    369  C   LEU A  56     124.831 115.770 135.309  1.00 79.51           C  
ATOM    370  O   LEU A  56     123.832 115.726 134.585  1.00 79.51           O  
ATOM    371  CB  LEU A  56     126.878 115.941 133.886  1.00 79.51           C  
ATOM    372  N   LYS A  57     124.859 116.413 136.480  1.00 75.98           N  
ATOM    373  CA  LYS A  57     123.722 117.184 136.988  1.00 75.98           C  
ATOM    374  C   LYS A  57     124.225 118.586 137.330  1.00 75.98           C  
ATOM    375  O   LYS A  57     124.531 118.891 138.485  1.00 75.98           O  
ATOM    376  CB  LYS A  57     123.087 116.489 138.193  1.00 75.98           C  
ATOM    377  CG  LYS A  57     124.069 115.680 139.025  1.00 75.98           C  
ATOM    378  CD  LYS A  57     123.403 115.092 140.258  1.00 75.98           C  
ATOM    379  CE  LYS A  57     124.434 114.624 141.272  1.00 75.98           C  
ATOM    380  NZ  LYS A  57     125.388 115.709 141.637  1.00 75.98           N  
ATOM    381  N   SER A  58     124.308 119.435 136.308  1.00 70.15           N  
ATOM    382  CA  SER A  58     124.612 120.853 136.491  1.00 70.15           C  
ATOM    383  C   SER A  58     124.192 121.562 135.211  1.00 70.15           C  
ATOM    384  O   SER A  58     124.819 121.364 134.166  1.00 70.15           O  
ATOM    385  CB  SER A  58     126.091 121.066 136.787  1.00 70.15           C  
ATOM    386  OG  SER A  58     126.896 120.622 135.710  1.00 70.15           O  
ATOM    387  N   TRP A  59     123.147 122.379 135.288  1.00 71.13           N  
ATOM    388  CA  TRP A  59     122.577 123.034 134.113  1.00 71.13           C  
ATOM    389  C   TRP A  59     122.931 124.517 134.148  1.00 71.13           C  
ATOM    390  O   TRP A  59     122.307 125.299 134.871  1.00 71.13           O  
ATOM    391  CB  TRP A  59     121.068 122.822 134.051  1.00 71.13           C  
ATOM    392  CG  TRP A  59     120.651 121.822 133.014  1.00 71.13           C  
ATOM    393  CD1 TRP A  59     121.407 120.806 132.505  1.00 71.13           C  
ATOM    394  CD2 TRP A  59     119.378 121.742 132.358  1.00 71.13           C  
ATOM    395  NE1 TRP A  59     120.685 120.100 131.573  1.00 71.13           N  
ATOM    396  CE2 TRP A  59     119.437 120.654 131.465  1.00 71.13           C  
ATOM    397  CE3 TRP A  59     118.195 122.484 132.440  1.00 71.13           C  
ATOM    398  CZ2 TRP A  59     118.359 120.291 130.660  1.00 71.13           C  
ATOM    399  CZ3 TRP A  59     117.126 122.121 131.639  1.00 71.13           C  
ATOM    400  CH2 TRP A  59     117.215 121.035 130.761  1.00 71.13           C  
ATOM    401  N   LYS A  60     123.933 124.897 133.363  1.00 65.59           N  
ATOM    402  CA  LYS A  60     124.298 126.289 133.156  1.00 65.59           C  
ATOM    403  C   LYS A  60     123.741 126.774 131.823  1.00 65.59           C  
ATOM    404  O   LYS A  60     123.401 125.981 130.941  1.00 65.59           O  
ATOM    405  CB  LYS A  60     125.817 126.469 133.194  1.00 65.59           C  
ATOM    406  N   SER A  61     123.667 128.102 131.683  1.00 62.79           N  
ATOM    407  CA  SER A  61     122.971 128.695 130.545  1.00 62.79           C  
ATOM    408  C   SER A  61     123.586 128.281 129.216  1.00 62.79           C  
ATOM    409  O   SER A  61     122.855 127.965 128.271  1.00 62.79           O  
ATOM    410  CB  SER A  61     122.963 130.216 130.669  1.00 62.79           C  
ATOM    411  OG  SER A  61     122.000 130.783 129.801  1.00 62.79           O  
ATOM    412  N   SER A  62     124.915 128.279 129.116  1.00 60.44           N  
ATOM    413  CA  SER A  62     125.556 127.803 127.896  1.00 60.44           C  
ATOM    414  C   SER A  62     125.329 126.312 127.687  1.00 60.44           C  
ATOM    415  O   SER A  62     125.218 125.855 126.540  1.00 60.44           O  
ATOM    416  CB  SER A  62     127.054 128.107 127.935  1.00 60.44           C  
ATOM    417  OG  SER A  62     127.605 128.109 126.630  1.00 60.44           O  
ATOM    418  N   ARG A  63     125.251 125.543 128.775  1.00 61.42           N  
ATOM    419  CA  ARG A  63     125.007 124.114 128.643  1.00 61.42           C  
ATOM    420  C   ARG A  63     123.607 123.825 128.120  1.00 61.42           C  
ATOM    421  O   ARG A  63     123.408 122.817 127.440  1.00 61.42           O  
ATOM    422  CB  ARG A  63     125.236 123.407 129.977  1.00 61.42           C  
ATOM    423  CG  ARG A  63     125.666 121.957 129.820  1.00 61.42           C  
ATOM    424  CD  ARG A  63     126.714 121.554 130.844  1.00 61.42           C  
ATOM    425  NE  ARG A  63     126.478 122.150 132.153  1.00 61.42           N  
ATOM    426  CZ  ARG A  63     127.299 123.008 132.743  1.00 61.42           C  
ATOM    427  NH1 ARG A  63     128.421 123.401 132.162  1.00 61.42           N  
ATOM    428  NH2 ARG A  63     126.989 123.480 133.946  1.00 61.42           N  
ATOM    429  N   ILE A  64     122.627 124.685 128.413  1.00 58.16           N  
ATOM    430  CA  ILE A  64     121.303 124.490 127.821  1.00 58.16           C  
ATOM    431  C   ILE A  64     121.364 124.632 126.306  1.00 58.16           C  
ATOM    432  O   ILE A  64     120.764 123.841 125.569  1.00 58.16           O  
ATOM    433  CB  ILE A  64     120.266 125.450 128.433  1.00 58.16           C  
ATOM    434  CG1 ILE A  64     120.618 125.785 129.876  1.00 58.16           C  
ATOM    435  CG2 ILE A  64     118.874 124.853 128.344  1.00 58.16           C  
ATOM    436  CD1 ILE A  64     119.801 126.906 130.455  1.00 58.16           C  
ATOM    437  N   PHE A  65     122.076 125.649 125.815  1.00 54.51           N  
ATOM    438  CA  PHE A  65     122.220 125.814 124.372  1.00 54.51           C  
ATOM    439  C   PHE A  65     122.968 124.637 123.757  1.00 54.51           C  
ATOM    440  O   PHE A  65     122.601 124.147 122.679  1.00 54.51           O  
ATOM    441  CB  PHE A  65     122.937 127.127 124.065  1.00 54.51           C  
ATOM    442  CG  PHE A  65     122.181 128.344 124.506  1.00 54.51           C  
ATOM    443  CD1 PHE A  65     120.882 128.559 124.084  1.00 54.51           C  
ATOM    444  CD2 PHE A  65     122.769 129.275 125.343  1.00 54.51           C  
ATOM    445  CE1 PHE A  65     120.186 129.679 124.488  1.00 54.51           C  
ATOM    446  CE2 PHE A  65     122.077 130.396 125.750  1.00 54.51           C  
ATOM    447  CZ  PHE A  65     120.784 130.598 125.322  1.00 54.51           C  
ATOM    448  N   LEU A  66     124.022 124.168 124.430  1.00 57.29           N  
ATOM    449  CA  LEU A  66     124.749 123.004 123.934  1.00 57.29           C  
ATOM    450  C   LEU A  66     123.849 121.775 123.884  1.00 57.29           C  
ATOM    451  O   LEU A  66     123.910 120.990 122.932  1.00 57.29           O  
ATOM    452  CB  LEU A  66     125.977 122.738 124.803  1.00 57.29           C  
ATOM    453  CG  LEU A  66     127.136 123.722 124.641  1.00 57.29           C  
ATOM    454  CD1 LEU A  66     128.417 123.141 125.214  1.00 57.29           C  
ATOM    455  CD2 LEU A  66     127.322 124.092 123.181  1.00 57.29           C  
ATOM    456  N   PHE A  67     123.007 121.592 124.902  1.00 59.62           N  
ATOM    457  CA  PHE A  67     122.077 120.469 124.911  1.00 59.62           C  
ATOM    458  C   PHE A  67     121.056 120.588 123.789  1.00 59.62           C  
ATOM    459  O   PHE A  67     120.667 119.581 123.191  1.00 59.62           O  
ATOM    460  CB  PHE A  67     121.373 120.377 126.265  1.00 59.62           C  
ATOM    461  CG  PHE A  67     120.344 119.287 126.338  1.00 59.62           C  
ATOM    462  CD1 PHE A  67     120.717 117.984 126.608  1.00 59.62           C  
ATOM    463  CD2 PHE A  67     119.004 119.566 126.133  1.00 59.62           C  
ATOM    464  CE1 PHE A  67     119.774 116.979 126.672  1.00 59.62           C  
ATOM    465  CE2 PHE A  67     118.058 118.565 126.196  1.00 59.62           C  
ATOM    466  CZ  PHE A  67     118.443 117.270 126.466  1.00 59.62           C  
ATOM    467  N   ASN A  68     120.589 121.805 123.511  1.00 55.99           N  
ATOM    468  CA  ASN A  68     119.672 121.997 122.392  1.00 55.99           C  
ATOM    469  C   ASN A  68     120.334 121.615 121.075  1.00 55.99           C  
ATOM    470  O   ASN A  68     119.727 120.937 120.232  1.00 55.99           O  
ATOM    471  CB  ASN A  68     119.194 123.446 122.354  1.00 55.99           C  
ATOM    472  CG  ASN A  68     117.810 123.617 122.938  1.00 55.99           C  
ATOM    473  OD1 ASN A  68     116.828 123.123 122.389  1.00 55.99           O  
ATOM    474  ND2 ASN A  68     117.725 124.320 124.060  1.00 55.99           N  
ATOM    475  N   LEU A  69     121.588 122.032 120.888  1.00 56.71           N  
ATOM    476  CA  LEU A  69     122.320 121.646 119.686  1.00 56.71           C  
ATOM    477  C   LEU A  69     122.478 120.133 119.607  1.00 56.71           C  
ATOM    478  O   LEU A  69     122.341 119.541 118.529  1.00 56.71           O  
ATOM    479  CB  LEU A  69     123.685 122.331 119.657  1.00 56.71           C  
ATOM    480  CG  LEU A  69     124.396 122.383 118.304  1.00 56.71           C  
ATOM    481  CD1 LEU A  69     124.954 123.770 118.054  1.00 56.71           C  
ATOM    482  CD2 LEU A  69     125.500 121.347 118.241  1.00 56.71           C  
ATOM    483  N   ALA A  70     122.764 119.492 120.742  1.00 59.12           N  
ATOM    484  CA  ALA A  70     122.912 118.041 120.765  1.00 59.12           C  
ATOM    485  C   ALA A  70     121.605 117.344 120.416  1.00 59.12           C  
ATOM    486  O   ALA A  70     121.603 116.335 119.705  1.00 59.12           O  
ATOM    487  CB  ALA A  70     123.412 117.587 122.135  1.00 59.12           C  
ATOM    488  N   VAL A  71     120.484 117.861 120.919  1.00 58.96           N  
ATOM    489  CA  VAL A  71     119.182 117.276 120.609  1.00 58.96           C  
ATOM    490  C   VAL A  71     118.897 117.389 119.118  1.00 58.96           C  
ATOM    491  O   VAL A  71     118.445 116.430 118.476  1.00 58.96           O  
ATOM    492  CB  VAL A  71     118.080 117.947 121.448  1.00 58.96           C  
ATOM    493  CG1 VAL A  71     116.732 117.837 120.754  1.00 58.96           C  
ATOM    494  CG2 VAL A  71     118.021 117.328 122.831  1.00 58.96           C  
ATOM    495  N   ALA A  72     119.160 118.567 118.544  1.00 57.38           N  
ATOM    496  CA  ALA A  72     118.947 118.744 117.111  1.00 57.38           C  
ATOM    497  C   ALA A  72     119.827 117.797 116.304  1.00 57.38           C  
ATOM    498  O   ALA A  72     119.363 117.168 115.344  1.00 57.38           O  
ATOM    499  CB  ALA A  72     119.215 120.195 116.717  1.00 57.38           C  
ATOM    500  N   ASP A  73     121.097 117.670 116.693  1.00 60.46           N  
ATOM    501  CA  ASP A  73     122.009 116.779 115.984  1.00 60.46           C  
ATOM    502  C   ASP A  73     121.560 115.327 116.090  1.00 60.46           C  
ATOM    503  O   ASP A  73     121.625 114.578 115.109  1.00 60.46           O  
ATOM    504  CB  ASP A  73     123.425 116.945 116.531  1.00 60.46           C  
ATOM    505  CG  ASP A  73     124.202 118.025 115.813  1.00 60.46           C  
ATOM    506  OD1 ASP A  73     125.448 117.961 115.810  1.00 60.46           O  
ATOM    507  OD2 ASP A  73     123.565 118.939 115.250  1.00 60.46           O  
ATOM    508  N   PHE A  74     121.111 114.907 117.274  1.00 60.74           N  
ATOM    509  CA  PHE A  74     120.658 113.532 117.448  1.00 60.74           C  
ATOM    510  C   PHE A  74     119.425 113.247 116.607  1.00 60.74           C  
ATOM    511  O   PHE A  74     119.322 112.183 115.987  1.00 60.74           O  
ATOM    512  CB  PHE A  74     120.374 113.248 118.922  1.00 60.74           C  
ATOM    513  CG  PHE A  74     120.162 111.792 119.227  1.00 60.74           C  
ATOM    514  CD1 PHE A  74     121.230 110.976 119.549  1.00 60.74           C  
ATOM    515  CD2 PHE A  74     118.892 111.242 119.192  1.00 60.74           C  
ATOM    516  CE1 PHE A  74     121.040 109.639 119.827  1.00 60.74           C  
ATOM    517  CE2 PHE A  74     118.695 109.905 119.470  1.00 60.74           C  
ATOM    518  CZ  PHE A  74     119.771 109.103 119.788  1.00 60.74           C  
ATOM    519  N   LEU A  75     118.471 114.178 116.580  1.00 59.47           N  
ATOM    520  CA  LEU A  75     117.279 113.966 115.768  1.00 59.47           C  
ATOM    521  C   LEU A  75     117.632 113.907 114.287  1.00 59.47           C  
ATOM    522  O   LEU A  75     117.085 113.085 113.541  1.00 59.47           O  
ATOM    523  CB  LEU A  75     116.255 115.061 116.043  1.00 59.47           C  
ATOM    524  CG  LEU A  75     115.107 114.682 116.977  1.00 59.47           C  
ATOM    525  CD1 LEU A  75     115.618 114.503 118.396  1.00 59.47           C  
ATOM    526  CD2 LEU A  75     114.011 115.731 116.926  1.00 59.47           C  
ATOM    527  N   LEU A  76     118.557 114.764 113.844  1.00 58.26           N  
ATOM    528  CA  LEU A  76     119.000 114.715 112.454  1.00 58.26           C  
ATOM    529  C   LEU A  76     119.683 113.388 112.136  1.00 58.26           C  
ATOM    530  O   LEU A  76     119.464 112.806 111.066  1.00 58.26           O  
ATOM    531  CB  LEU A  76     119.934 115.889 112.168  1.00 58.26           C  
ATOM    532  CG  LEU A  76     120.489 116.009 110.752  1.00 58.26           C  
ATOM    533  CD1 LEU A  76     119.362 115.956 109.744  1.00 58.26           C  
ATOM    534  CD2 LEU A  76     121.278 117.296 110.609  1.00 58.26           C  
ATOM    535  N   ILE A  77     120.511 112.890 113.057  1.00 63.12           N  
ATOM    536  CA  ILE A  77     121.188 111.616 112.840  1.00 63.12           C  
ATOM    537  C   ILE A  77     120.177 110.479 112.763  1.00 63.12           C  
ATOM    538  O   ILE A  77     120.302 109.575 111.928  1.00 63.12           O  
ATOM    539  CB  ILE A  77     122.237 111.379 113.942  1.00 63.12           C  
ATOM    540  CG1 ILE A  77     123.484 112.221 113.677  1.00 63.12           C  
ATOM    541  CG2 ILE A  77     122.610 109.910 114.026  1.00 63.12           C  
ATOM    542  CD1 ILE A  77     123.988 112.136 112.255  1.00 63.12           C  
ATOM    543  N   ILE A  78     119.160 110.504 113.626  1.00 61.38           N  
ATOM    544  CA  ILE A  78     118.105 109.497 113.555  1.00 61.38           C  
ATOM    545  C   ILE A  78     117.397 109.567 112.210  1.00 61.38           C  
ATOM    546  O   ILE A  78     117.113 108.537 111.586  1.00 61.38           O  
ATOM    547  CB  ILE A  78     117.117 109.665 114.724  1.00 61.38           C  
ATOM    548  CG1 ILE A  78     117.821 109.422 116.059  1.00 61.38           C  
ATOM    549  CG2 ILE A  78     115.934 108.726 114.562  1.00 61.38           C  
ATOM    550  CD1 ILE A  78     118.511 108.083 116.152  1.00 61.38           C  
ATOM    551  N   CYS A  79     117.106 110.782 111.739  1.00 62.52           N  
ATOM    552  CA  CYS A  79     116.475 110.937 110.432  1.00 62.52           C  
ATOM    553  C   CYS A  79     117.368 110.423 109.309  1.00 62.52           C  
ATOM    554  O   CYS A  79     116.866 109.990 108.266  1.00 62.52           O  
ATOM    555  CB  CYS A  79     116.121 112.404 110.196  1.00 62.52           C  
ATOM    556  SG  CYS A  79     114.568 112.932 110.952  1.00 62.52           S  
ATOM    557  N   LEU A  80     118.686 110.471 109.506  1.00 62.27           N  
ATOM    558  CA  LEU A  80     119.619 110.075 108.452  1.00 62.27           C  
ATOM    559  C   LEU A  80     119.411 108.657 107.933  1.00 62.27           C  
ATOM    560  O   LEU A  80     119.591 108.444 106.720  1.00 62.27           O  
ATOM    561  CB  LEU A  80     121.058 110.253 108.951  1.00 62.27           C  
ATOM    562  CG  LEU A  80     122.144 110.326 107.878  1.00 62.27           C  
ATOM    563  CD1 LEU A  80     121.644 111.083 106.661  1.00 62.27           C  
ATOM    564  CD2 LEU A  80     123.396 110.975 108.436  1.00 62.27           C  
ATOM    565  N   PRO A  81     119.089 107.657 108.762  1.00 55.39           N  
ATOM    566  CA  PRO A  81     118.928 106.295 108.220  1.00 55.39           C  
ATOM    567  C   PRO A  81     117.883 106.198 107.121  1.00 55.39           C  
ATOM    568  O   PRO A  81     118.070 105.451 106.150  1.00 55.39           O  
ATOM    569  CB  PRO A  81     118.534 105.478 109.457  1.00 55.39           C  
ATOM    570  N   PHE A  82     116.785 106.944 107.241  1.00 59.48           N  
ATOM    571  CA  PHE A  82     115.786 106.952 106.178  1.00 59.48           C  
ATOM    572  C   PHE A  82     116.346 107.574 104.906  1.00 59.48           C  
ATOM    573  O   PHE A  82     116.020 107.134 103.799  1.00 59.48           O  
ATOM    574  CB  PHE A  82     114.529 107.686 106.641  1.00 59.48           C  
ATOM    575  CG  PHE A  82     113.782 106.974 107.733  1.00 59.48           C  
ATOM    576  CD1 PHE A  82     114.009 105.631 107.985  1.00 59.48           C  
ATOM    577  CD2 PHE A  82     112.852 107.645 108.506  1.00 59.48           C  
ATOM    578  CE1 PHE A  82     113.324 104.975 108.987  1.00 59.48           C  
ATOM    579  CE2 PHE A  82     112.164 106.994 109.509  1.00 59.48           C  
ATOM    580  CZ  PHE A  82     112.400 105.657 109.750  1.00 59.48           C  
ATOM    581  N   LEU A  83     117.195 108.595 105.042  1.00 59.35           N  
ATOM    582  CA  LEU A  83     117.867 109.150 103.870  1.00 59.35           C  
ATOM    583  C   LEU A  83     118.762 108.111 103.206  1.00 59.35           C  
ATOM    584  O   LEU A  83     118.804 108.011 101.974  1.00 59.35           O  
ATOM    585  CB  LEU A  83     118.686 110.380 104.258  1.00 59.35           C  
ATOM    586  CG  LEU A  83     117.942 111.701 104.440  1.00 59.35           C  
ATOM    587  CD1 LEU A  83     117.711 111.985 105.909  1.00 59.35           C  
ATOM    588  CD2 LEU A  83     118.717 112.832 103.793  1.00 59.35           C  
ATOM    589  N   MET A  84     119.503 107.343 104.006  1.00 57.66           N  
ATOM    590  CA  MET A  84     120.342 106.296 103.434  1.00 57.66           C  
ATOM    591  C   MET A  84     119.497 105.271 102.692  1.00 57.66           C  
ATOM    592  O   MET A  84     119.847 104.847 101.584  1.00 57.66           O  
ATOM    593  CB  MET A  84     121.168 105.623 104.529  1.00 57.66           C  
ATOM    594  N   ASP A  85     118.364 104.882 103.282  1.00 59.27           N  
ATOM    595  CA  ASP A  85     117.465 103.946 102.614  1.00 59.27           C  
ATOM    596  C   ASP A  85     116.918 104.532 101.317  1.00 59.27           C  
ATOM    597  O   ASP A  85     116.745 103.812 100.326  1.00 59.27           O  
ATOM    598  CB  ASP A  85     116.322 103.558 103.552  1.00 59.27           C  
ATOM    599  N   ASN A  86     116.630 105.834 101.308  1.00 60.73           N  
ATOM    600  CA  ASN A  86     116.093 106.471 100.110  1.00 60.73           C  
ATOM    601  C   ASN A  86     117.120 106.492  98.984  1.00 60.73           C  
ATOM    602  O   ASN A  86     116.824 106.085  97.855  1.00 60.73           O  
ATOM    603  CB  ASN A  86     115.625 107.889 100.439  1.00 60.73           C  
ATOM    604  CG  ASN A  86     115.301 108.699  99.201  1.00 60.73           C  
ATOM    605  OD1 ASN A  86     114.805 108.169  98.207  1.00 60.73           O  
ATOM    606  ND2 ASN A  86     115.580 109.995  99.256  1.00 60.73           N  
ATOM    607  N   TYR A  87     118.336 106.967  99.269  1.00 56.64           N  
ATOM    608  CA  TYR A  87     119.362 106.997  98.228  1.00 56.64           C  
ATOM    609  C   TYR A  87     119.813 105.608  97.800  1.00 56.64           C  
ATOM    610  O   TYR A  87     120.292 105.454  96.672  1.00 56.64           O  
ATOM    611  CB  TYR A  87     120.584 107.812  98.654  1.00 56.64           C  
ATOM    612  CG  TYR A  87     120.355 109.300  98.819  1.00 56.64           C  
ATOM    613  CD1 TYR A  87     119.600 109.805  99.863  1.00 56.64           C  
ATOM    614  CD2 TYR A  87     120.902 110.200  97.919  1.00 56.64           C  
ATOM    615  CE1 TYR A  87     119.403 111.162 100.010  1.00 56.64           C  
ATOM    616  CE2 TYR A  87     120.709 111.556  98.056  1.00 56.64           C  
ATOM    617  CZ  TYR A  87     119.959 112.032  99.102  1.00 56.64           C  
ATOM    618  OH  TYR A  87     119.764 113.384  99.242  1.00 56.64           O  
ATOM    619  N   VAL A  88     119.686 104.597  98.661  1.00 59.36           N  
ATOM    620  CA  VAL A  88     120.016 103.239  98.235  1.00 59.36           C  
ATOM    621  C   VAL A  88     119.086 102.795  97.113  1.00 59.36           C  
ATOM    622  O   VAL A  88     119.520 102.174  96.134  1.00 59.36           O  
ATOM    623  CB  VAL A  88     119.970 102.272  99.433  1.00 59.36           C  
ATOM    624  CG1 VAL A  88     119.664 100.855  98.970  1.00 59.36           C  
ATOM    625  CG2 VAL A  88     121.290 102.306 100.186  1.00 59.36           C  
ATOM    626  N   ARG A  89     117.802 103.122  97.223  1.00 65.86           N  
ATOM    627  CA  ARG A  89     116.803 102.726  96.238  1.00 65.86           C  
ATOM    628  C   ARG A  89     116.860 103.549  94.954  1.00 65.86           C  
ATOM    629  O   ARG A  89     115.946 103.435  94.130  1.00 65.86           O  
ATOM    630  CB  ARG A  89     115.401 102.822  96.847  1.00 65.86           C  
ATOM    631  CG  ARG A  89     115.123 101.797  97.931  1.00 65.86           C  
ATOM    632  CD  ARG A  89     114.239 100.676  97.413  1.00 65.86           C  
ATOM    633  NE  ARG A  89     113.490 100.032  98.485  1.00 65.86           N  
ATOM    634  CZ  ARG A  89     113.461  98.724  98.697  1.00 65.86           C  
ATOM    635  NH1 ARG A  89     114.132  97.885  97.926  1.00 65.86           N  
ATOM    636  NH2 ARG A  89     112.741  98.246  99.708  1.00 65.86           N  
ATOM    637  N   ARG A  90     117.899 104.367  94.772  1.00 67.77           N  
ATOM    638  CA  ARG A  90     118.063 105.212  93.587  1.00 67.77           C  
ATOM    639  C   ARG A  90     116.866 106.149  93.410  1.00 67.77           C  
ATOM    640  O   ARG A  90     116.168 106.131  92.395  1.00 67.77           O  
ATOM    641  CB  ARG A  90     118.293 104.362  92.333  1.00 67.77           C  
ATOM    642  CG  ARG A  90     119.334 104.928  91.384  1.00 67.77           C  
ATOM    643  CD  ARG A  90     119.451 104.085  90.125  1.00 67.77           C  
ATOM    644  NE  ARG A  90     118.658 104.622  89.025  1.00 67.77           N  
ATOM    645  CZ  ARG A  90     118.366 103.955  87.917  1.00 67.77           C  
ATOM    646  NH1 ARG A  90     118.782 102.713  87.728  1.00 67.77           N  
ATOM    647  NH2 ARG A  90     117.641 104.549  86.974  1.00 67.77           N  
ATOM    648  N   TRP A  91     116.645 106.975  94.434  1.00 66.00           N  
ATOM    649  CA  TRP A  91     115.579 107.977  94.447  1.00 66.00           C  
ATOM    650  C   TRP A  91     114.208 107.329  94.240  1.00 66.00           C  
ATOM    651  O   TRP A  91     113.509 107.580  93.258  1.00 66.00           O  
ATOM    652  CB  TRP A  91     115.840 109.066  93.401  1.00 66.00           C  
ATOM    653  CG  TRP A  91     116.972 109.973  93.759  1.00 66.00           C  
ATOM    654  CD1 TRP A  91     118.268 109.864  93.351  1.00 66.00           C  
ATOM    655  CD2 TRP A  91     116.913 111.127  94.604  1.00 66.00           C  
ATOM    656  NE1 TRP A  91     119.020 110.880  93.887  1.00 66.00           N  
ATOM    657  CE2 TRP A  91     118.210 111.669  94.661  1.00 66.00           C  
ATOM    658  CE3 TRP A  91     115.888 111.754  95.317  1.00 66.00           C  
ATOM    659  CZ2 TRP A  91     118.510 112.807  95.403  1.00 66.00           C  
ATOM    660  CZ3 TRP A  91     116.188 112.884  96.052  1.00 66.00           C  
ATOM    661  CH2 TRP A  91     117.487 113.399  96.089  1.00 66.00           C  
ATOM    662  N   ASP A  92     113.835 106.479  95.195  1.00 70.68           N  
ATOM    663  CA  ASP A  92     112.527 105.823  95.189  1.00 70.68           C  
ATOM    664  C   ASP A  92     112.050 105.718  96.634  1.00 70.68           C  
ATOM    665  O   ASP A  92     112.431 104.790  97.353  1.00 70.68           O  
ATOM    666  CB  ASP A  92     112.592 104.454  94.525  1.00 70.68           C  
ATOM    667  CG  ASP A  92     111.254 103.742  94.532  1.00 70.68           C  
ATOM    668  OD1 ASP A  92     110.351 104.164  93.780  1.00 70.68           O  
ATOM    669  OD2 ASP A  92     111.104 102.761  95.290  1.00 70.68           O  
ATOM    670  N   TRP A  93     111.217 106.666  97.052  1.00 65.52           N  
ATOM    671  CA  TRP A  93     110.677 106.683  98.407  1.00 65.52           C  
ATOM    672  C   TRP A  93     109.585 105.627  98.516  1.00 65.52           C  
ATOM    673  O   TRP A  93     108.506 105.776  97.934  1.00 65.52           O  
ATOM    674  CB  TRP A  93     110.139 108.071  98.739  1.00 65.52           C  
ATOM    675  CG  TRP A  93     109.842 108.284 100.187  1.00 65.52           C  
ATOM    676  CD1 TRP A  93     108.612 108.334 100.770  1.00 65.52           C  
ATOM    677  CD2 TRP A  93     110.793 108.490 101.237  1.00 65.52           C  
ATOM    678  NE1 TRP A  93     108.737 108.554 102.119  1.00 65.52           N  
ATOM    679  CE2 TRP A  93     110.066 108.653 102.431  1.00 65.52           C  
ATOM    680  CE3 TRP A  93     112.188 108.549 101.284  1.00 65.52           C  
ATOM    681  CZ2 TRP A  93     110.686 108.872 103.657  1.00 65.52           C  
ATOM    682  CZ3 TRP A  93     112.800 108.767 102.502  1.00 65.52           C  
ATOM    683  CH2 TRP A  93     112.051 108.925 103.671  1.00 65.52           C  
ATOM    684  N   LYS A  94     109.856 104.562  99.266  1.00 65.32           N  
ATOM    685  CA  LYS A  94     108.934 103.442  99.420  1.00 65.32           C  
ATOM    686  C   LYS A  94     108.332 103.403 100.821  1.00 65.32           C  
ATOM    687  O   LYS A  94     108.160 102.336 101.411  1.00 65.32           O  
ATOM    688  CB  LYS A  94     109.632 102.122  99.103  1.00 65.32           C  
ATOM    689  N   PHE A  95     108.010 104.574 101.370  1.00 68.89           N  
ATOM    690  CA  PHE A  95     107.464 104.679 102.716  1.00 68.89           C  
ATOM    691  C   PHE A  95     106.019 105.162 102.711  1.00 68.89           C  
ATOM    692  O   PHE A  95     105.141 104.497 103.266  1.00 68.89           O  
ATOM    693  CB  PHE A  95     108.335 105.615 103.567  1.00 68.89           C  
ATOM    694  CG  PHE A  95     109.571 104.962 104.125  1.00 68.89           C  
ATOM    695  CD1 PHE A  95     110.364 104.147 103.334  1.00 68.89           C  
ATOM    696  CD2 PHE A  95     109.943 105.173 105.441  1.00 68.89           C  
ATOM    697  CE1 PHE A  95     111.499 103.551 103.846  1.00 68.89           C  
ATOM    698  CE2 PHE A  95     111.077 104.580 105.959  1.00 68.89           C  
ATOM    699  CZ  PHE A  95     111.856 103.768 105.160  1.00 68.89           C  
ATOM    700  N   GLY A  96     105.749 106.303 102.094  1.00 71.19           N  
ATOM    701  CA  GLY A  96     104.408 106.848 102.076  1.00 71.19           C  
ATOM    702  C   GLY A  96     104.450 108.344 101.830  1.00 71.19           C  
ATOM    703  O   GLY A  96     105.479 108.902 101.453  1.00 71.19           O  
ATOM    704  N   ASP A  97     103.301 108.979 102.058  1.00 74.45           N  
ATOM    705  CA  ASP A  97     103.159 110.415 101.848  1.00 74.45           C  
ATOM    706  C   ASP A  97     103.332 111.219 103.132  1.00 74.45           C  
ATOM    707  O   ASP A  97     104.062 112.213 103.143  1.00 74.45           O  
ATOM    708  CB  ASP A  97     101.801 110.722 101.197  1.00 74.45           C  
ATOM    709  CG  ASP A  97     100.638 110.563 102.155  1.00 74.45           C  
ATOM    710  OD1 ASP A  97     100.588 109.537 102.865  1.00 74.45           O  
ATOM    711  OD2 ASP A  97      99.776 111.465 102.199  1.00 74.45           O  
ATOM    712  N   ILE A  98     102.673 110.813 104.217  1.00 74.01           N  
ATOM    713  CA  ILE A  98     102.897 111.469 105.506  1.00 74.01           C  
ATOM    714  C   ILE A  98     104.344 111.325 105.970  1.00 74.01           C  
ATOM    715  O   ILE A  98     104.935 112.332 106.393  1.00 74.01           O  
ATOM    716  CB  ILE A  98     101.882 110.959 106.542  1.00 74.01           C  
ATOM    717  CG1 ILE A  98     100.612 111.812 106.503  1.00 74.01           C  
ATOM    718  CG2 ILE A  98     102.483 110.963 107.941  1.00 74.01           C  
ATOM    719  CD1 ILE A  98     100.800 113.212 107.042  1.00 74.01           C  
ATOM    720  N   PRO A  99     104.966 110.139 105.929  1.00 69.82           N  
ATOM    721  CA  PRO A  99     106.379 110.062 106.332  1.00 69.82           C  
ATOM    722  C   PRO A  99     107.295 110.923 105.488  1.00 69.82           C  
ATOM    723  O   PRO A  99     108.273 111.455 106.018  1.00 69.82           O  
ATOM    724  CB  PRO A  99     106.710 108.570 106.181  1.00 69.82           C  
ATOM    725  CG  PRO A  99     105.674 108.037 105.265  1.00 69.82           C  
ATOM    726  CD  PRO A  99     104.440 108.804 105.594  1.00 69.82           C  
ATOM    727  N   CYS A 100     107.008 111.094 104.196  1.00 69.77           N  
ATOM    728  CA  CYS A 100     107.876 111.910 103.351  1.00 69.77           C  
ATOM    729  C   CYS A 100     107.839 113.376 103.765  1.00 69.77           C  
ATOM    730  O   CYS A 100     108.888 114.013 103.932  1.00 69.77           O  
ATOM    731  CB  CYS A 100     107.473 111.762 101.886  1.00 69.77           C  
ATOM    732  SG  CYS A 100     108.033 113.123 100.846  1.00 69.77           S  
ATOM    733  N   ARG A 101     106.637 113.935 103.915  1.00 66.95           N  
ATOM    734  CA  ARG A 101     106.523 115.322 104.350  1.00 66.95           C  
ATOM    735  C   ARG A 101     107.102 115.502 105.746  1.00 66.95           C  
ATOM    736  O   ARG A 101     107.785 116.496 106.020  1.00 66.95           O  
ATOM    737  CB  ARG A 101     105.063 115.771 104.308  1.00 66.95           C  
ATOM    738  CG  ARG A 101     104.347 115.439 103.010  1.00 66.95           C  
ATOM    739  CD  ARG A 101     102.847 115.637 103.143  1.00 66.95           C  
ATOM    740  NE  ARG A 101     102.467 117.032 102.962  1.00 66.95           N  
ATOM    741  CZ  ARG A 101     101.304 117.545 103.337  1.00 66.95           C  
ATOM    742  NH1 ARG A 101     100.375 116.803 103.917  1.00 66.95           N  
ATOM    743  NH2 ARG A 101     101.066 118.836 103.125  1.00 66.95           N  
ATOM    744  N   LEU A 102     106.849 114.543 106.638  1.00 65.65           N  
ATOM    745  CA  LEU A 102     107.418 114.614 107.978  1.00 65.65           C  
ATOM    746  C   LEU A 102     108.940 114.605 107.930  1.00 65.65           C  
ATOM    747  O   LEU A 102     109.597 115.349 108.666  1.00 65.65           O  
ATOM    748  CB  LEU A 102     106.898 113.452 108.823  1.00 65.65           C  
ATOM    749  CG  LEU A 102     107.442 113.330 110.245  1.00 65.65           C  
ATOM    750  CD1 LEU A 102     107.215 114.619 111.016  1.00 65.65           C  
ATOM    751  CD2 LEU A 102     106.799 112.152 110.954  1.00 65.65           C  
ATOM    752  N   MET A 103     109.518 113.773 107.063  1.00 63.43           N  
ATOM    753  CA  MET A 103     110.968 113.677 106.960  1.00 63.43           C  
ATOM    754  C   MET A 103     111.568 114.962 106.411  1.00 63.43           C  
ATOM    755  O   MET A 103     112.598 115.434 106.903  1.00 63.43           O  
ATOM    756  CB  MET A 103     111.347 112.482 106.083  1.00 63.43           C  
ATOM    757  CG  MET A 103     112.811 112.073 106.146  1.00 63.43           C  
ATOM    758  SD  MET A 103     113.516 111.767 107.785  1.00 63.43           S  
ATOM    759  CE  MET A 103     112.154 111.018 108.684  1.00 63.43           C  
ATOM    760  N   LEU A 104     110.944 115.539 105.382  1.00 59.46           N  
ATOM    761  CA  LEU A 104     111.442 116.805 104.848  1.00 59.46           C  
ATOM    762  C   LEU A 104     111.354 117.907 105.896  1.00 59.46           C  
ATOM    763  O   LEU A 104     112.291 118.706 106.060  1.00 59.46           O  
ATOM    764  CB  LEU A 104     110.658 117.193 103.595  1.00 59.46           C  
ATOM    765  CG  LEU A 104     110.688 116.251 102.390  1.00 59.46           C  
ATOM    766  CD1 LEU A 104     110.515 117.038 101.105  1.00 59.46           C  
ATOM    767  CD2 LEU A 104     111.970 115.439 102.345  1.00 59.46           C  
ATOM    768  N   PHE A 105     110.236 117.952 106.625  1.00 61.77           N  
ATOM    769  CA  PHE A 105     110.063 118.938 107.683  1.00 61.77           C  
ATOM    770  C   PHE A 105     111.130 118.784 108.755  1.00 61.77           C  
ATOM    771  O   PHE A 105     111.730 119.773 109.187  1.00 61.77           O  
ATOM    772  CB  PHE A 105     108.661 118.797 108.279  1.00 61.77           C  
ATOM    773  CG  PHE A 105     108.502 119.418 109.634  1.00 61.77           C  
ATOM    774  CD1 PHE A 105     108.320 120.780 109.769  1.00 61.77           C  
ATOM    775  CD2 PHE A 105     108.519 118.635 110.774  1.00 61.77           C  
ATOM    776  CE1 PHE A 105     108.165 121.350 111.016  1.00 61.77           C  
ATOM    777  CE2 PHE A 105     108.369 119.202 112.022  1.00 61.77           C  
ATOM    778  CZ  PHE A 105     108.192 120.561 112.142  1.00 61.77           C  
ATOM    779  N   MET A 106     111.392 117.548 109.186  1.00 59.25           N  
ATOM    780  CA  MET A 106     112.414 117.313 110.201  1.00 59.25           C  
ATOM    781  C   MET A 106     113.796 117.698 109.687  1.00 59.25           C  
ATOM    782  O   MET A 106     114.576 118.344 110.393  1.00 59.25           O  
ATOM    783  CB  MET A 106     112.390 115.850 110.641  1.00 59.25           C  
ATOM    784  N   LEU A 107     114.116 117.319 108.450  1.00 56.10           N  
ATOM    785  CA  LEU A 107     115.421 117.658 107.896  1.00 56.10           C  
ATOM    786  C   LEU A 107     115.643 119.163 107.926  1.00 56.10           C  
ATOM    787  O   LEU A 107     116.631 119.648 108.496  1.00 56.10           O  
ATOM    788  CB  LEU A 107     115.534 117.128 106.468  1.00 56.10           C  
ATOM    789  CG  LEU A 107     116.278 115.810 106.277  1.00 56.10           C  
ATOM    790  CD1 LEU A 107     117.759 116.028 106.475  1.00 56.10           C  
ATOM    791  CD2 LEU A 107     115.763 114.758 107.234  1.00 56.10           C  
ATOM    792  N   ALA A 108     114.700 119.921 107.362  1.00 56.91           N  
ATOM    793  CA  ALA A 108     114.852 121.371 107.319  1.00 56.91           C  
ATOM    794  C   ALA A 108     114.887 121.964 108.723  1.00 56.91           C  
ATOM    795  O   ALA A 108     115.728 122.821 109.030  1.00 56.91           O  
ATOM    796  CB  ALA A 108     113.723 121.991 106.499  1.00 56.91           C  
ATOM    797  N   MET A 109     113.988 121.503 109.598  1.00 59.98           N  
ATOM    798  CA  MET A 109     113.849 122.118 110.911  1.00 59.98           C  
ATOM    799  C   MET A 109     115.094 121.906 111.758  1.00 59.98           C  
ATOM    800  O   MET A 109     115.611 122.859 112.343  1.00 59.98           O  
ATOM    801  CB  MET A 109     112.608 121.570 111.616  1.00 59.98           C  
ATOM    802  CG  MET A 109     112.473 121.986 113.071  1.00 59.98           C  
ATOM    803  SD  MET A 109     113.130 120.795 114.250  1.00 59.98           S  
ATOM    804  CE  MET A 109     111.667 119.826 114.603  1.00 59.98           C  
ATOM    805  N   ASN A 110     115.609 120.678 111.830  1.00 56.95           N  
ATOM    806  CA  ASN A 110     116.819 120.486 112.622  1.00 56.95           C  
ATOM    807  C   ASN A 110     118.085 120.991 111.941  1.00 56.95           C  
ATOM    808  O   ASN A 110     119.030 121.350 112.646  1.00 56.95           O  
ATOM    809  CB  ASN A 110     116.972 119.030 113.060  1.00 56.95           C  
ATOM    810  CG  ASN A 110     115.665 118.415 113.504  1.00 56.95           C  
ATOM    811  OD1 ASN A 110     114.637 118.556 112.858  1.00 56.95           O  
ATOM    812  ND2 ASN A 110     115.696 117.760 114.653  1.00 56.95           N  
ATOM    813  N   ARG A 111     118.146 121.085 110.609  1.00 51.91           N  
ATOM    814  CA  ARG A 111     119.293 121.778 110.023  1.00 51.91           C  
ATOM    815  C   ARG A 111     119.308 123.244 110.443  1.00 51.91           C  
ATOM    816  O   ARG A 111     120.333 123.766 110.909  1.00 51.91           O  
ATOM    817  CB  ARG A 111     119.284 121.660 108.499  1.00 51.91           C  
ATOM    818  CG  ARG A 111     120.677 121.754 107.894  1.00 51.91           C  
ATOM    819  CD  ARG A 111     120.807 120.936 106.626  1.00 51.91           C  
ATOM    820  NE  ARG A 111     119.740 121.237 105.681  1.00 51.91           N  
ATOM    821  CZ  ARG A 111     119.257 120.374 104.798  1.00 51.91           C  
ATOM    822  NH1 ARG A 111     119.727 119.141 104.709  1.00 51.91           N  
ATOM    823  NH2 ARG A 111     118.280 120.759 103.983  1.00 51.91           N  
ATOM    824  N   GLN A 112     118.164 123.920 110.305  1.00 55.33           N  
ATOM    825  CA  GLN A 112     118.096 125.319 110.707  1.00 55.33           C  
ATOM    826  C   GLN A 112     118.310 125.471 112.206  1.00 55.33           C  
ATOM    827  O   GLN A 112     118.922 126.445 112.652  1.00 55.33           O  
ATOM    828  CB  GLN A 112     116.761 125.927 110.287  1.00 55.33           C  
ATOM    829  CG  GLN A 112     116.735 127.442 110.363  1.00 55.33           C  
ATOM    830  CD  GLN A 112     116.193 128.078 109.103  1.00 55.33           C  
ATOM    831  OE1 GLN A 112     115.774 127.386 108.175  1.00 55.33           O  
ATOM    832  NE2 GLN A 112     116.198 129.404 109.061  1.00 55.33           N  
ATOM    833  N   GLY A 113     117.820 124.517 112.999  1.00 54.27           N  
ATOM    834  CA  GLY A 113     118.031 124.579 114.434  1.00 54.27           C  
ATOM    835  C   GLY A 113     119.487 124.409 114.818  1.00 54.27           C  
ATOM    836  O   GLY A 113     119.986 125.104 115.705  1.00 54.27           O  
ATOM    837  N   SER A 114     120.188 123.485 114.158  1.00 49.86           N  
ATOM    838  CA  SER A 114     121.615 123.330 114.406  1.00 49.86           C  
ATOM    839  C   SER A 114     122.365 124.608 114.069  1.00 49.86           C  
ATOM    840  O   SER A 114     123.212 125.062 114.847  1.00 49.86           O  
ATOM    841  CB  SER A 114     122.163 122.155 113.597  1.00 49.86           C  
ATOM    842  OG  SER A 114     123.454 121.788 114.047  1.00 49.86           O  
ATOM    843  N   ILE A 115     122.049 125.220 112.925  1.00 49.31           N  
ATOM    844  CA  ILE A 115     122.735 126.457 112.552  1.00 49.31           C  
ATOM    845  C   ILE A 115     122.416 127.575 113.541  1.00 49.31           C  
ATOM    846  O   ILE A 115     123.306 128.326 113.962  1.00 49.31           O  
ATOM    847  CB  ILE A 115     122.379 126.856 111.110  1.00 49.31           C  
ATOM    848  CG1 ILE A 115     122.841 125.777 110.135  1.00 49.31           C  
ATOM    849  CG2 ILE A 115     123.024 128.174 110.757  1.00 49.31           C  
ATOM    850  CD1 ILE A 115     122.535 126.099 108.698  1.00 49.31           C  
ATOM    851  N   ILE A 116     121.146 127.699 113.933  1.00 51.89           N  
ATOM    852  CA  ILE A 116     120.735 128.768 114.839  1.00 51.89           C  
ATOM    853  C   ILE A 116     121.394 128.602 116.201  1.00 51.89           C  
ATOM    854  O   ILE A 116     121.862 129.574 116.801  1.00 51.89           O  
ATOM    855  CB  ILE A 116     119.200 128.808 114.954  1.00 51.89           C  
ATOM    856  CG1 ILE A 116     118.589 129.451 113.710  1.00 51.89           C  
ATOM    857  CG2 ILE A 116     118.773 129.567 116.193  1.00 51.89           C  
ATOM    858  CD1 ILE A 116     117.081 129.481 113.725  1.00 51.89           C  
ATOM    859  N   PHE A 117     121.446 127.371 116.713  1.00 50.76           N  
ATOM    860  CA  PHE A 117     122.055 127.156 118.019  1.00 50.76           C  
ATOM    861  C   PHE A 117     123.570 127.296 117.962  1.00 50.76           C  
ATOM    862  O   PHE A 117     124.182 127.731 118.942  1.00 50.76           O  
ATOM    863  CB  PHE A 117     121.647 125.792 118.567  1.00 50.76           C  
ATOM    864  CG  PHE A 117     120.255 125.766 119.123  1.00 50.76           C  
ATOM    865  CD1 PHE A 117     119.866 126.684 120.081  1.00 50.76           C  
ATOM    866  CD2 PHE A 117     119.332 124.838 118.679  1.00 50.76           C  
ATOM    867  CE1 PHE A 117     118.587 126.672 120.591  1.00 50.76           C  
ATOM    868  CE2 PHE A 117     118.050 124.821 119.185  1.00 50.76           C  
ATOM    869  CZ  PHE A 117     117.678 125.740 120.143  1.00 50.76           C  
ATOM    870  N   LEU A 118     124.190 126.957 116.830  1.00 47.98           N  
ATOM    871  CA  LEU A 118     125.606 127.259 116.655  1.00 47.98           C  
ATOM    872  C   LEU A 118     125.848 128.763 116.706  1.00 47.98           C  
ATOM    873  O   LEU A 118     126.789 129.231 117.361  1.00 47.98           O  
ATOM    874  CB  LEU A 118     126.093 126.664 115.334  1.00 47.98           C  
ATOM    875  CG  LEU A 118     127.525 126.144 115.213  1.00 47.98           C  
ATOM    876  CD1 LEU A 118     127.723 125.504 113.855  1.00 47.98           C  
ATOM    877  CD2 LEU A 118     128.519 127.270 115.394  1.00 47.98           C  
ATOM    878  N   THR A 119     124.990 129.537 116.038  1.00 44.57           N  
ATOM    879  CA  THR A 119     125.099 130.991 116.100  1.00 44.57           C  
ATOM    880  C   THR A 119     124.896 131.499 117.522  1.00 44.57           C  
ATOM    881  O   THR A 119     125.591 132.419 117.965  1.00 44.57           O  
ATOM    882  CB  THR A 119     124.085 131.630 115.153  1.00 44.57           C  
ATOM    883  OG1 THR A 119     124.500 131.417 113.801  1.00 44.57           O  
ATOM    884  CG2 THR A 119     123.969 133.123 115.409  1.00 44.57           C  
ATOM    885  N   VAL A 120     123.941 130.915 118.247  1.00 47.92           N  
ATOM    886  CA  VAL A 120     123.663 131.345 119.614  1.00 47.92           C  
ATOM    887  C   VAL A 120     124.851 131.056 120.523  1.00 47.92           C  
ATOM    888  O   VAL A 120     125.217 131.880 121.367  1.00 47.92           O  
ATOM    889  CB  VAL A 120     122.375 130.680 120.130  1.00 47.92           C  
ATOM    890  CG1 VAL A 120     122.274 130.811 121.637  1.00 47.92           C  
ATOM    891  CG2 VAL A 120     121.162 131.299 119.465  1.00 47.92           C  
ATOM    892  N   VAL A 121     125.471 129.885 120.369  1.00 48.45           N  
ATOM    893  CA  VAL A 121     126.664 129.566 121.148  1.00 48.45           C  
ATOM    894  C   VAL A 121     127.793 130.532 120.813  1.00 48.45           C  
ATOM    895  O   VAL A 121     128.516 131.000 121.704  1.00 48.45           O  
ATOM    896  CB  VAL A 121     127.078 128.101 120.916  1.00 48.45           C  
ATOM    897  CG1 VAL A 121     128.425 127.822 121.559  1.00 48.45           C  
ATOM    898  CG2 VAL A 121     126.023 127.161 121.469  1.00 48.45           C  
ATOM    899  N   ALA A 122     127.968 130.845 119.526  1.00 50.12           N  
ATOM    900  CA  ALA A 122     129.007 131.794 119.138  1.00 50.12           C  
ATOM    901  C   ALA A 122     128.755 133.173 119.739  1.00 50.12           C  
ATOM    902  O   ALA A 122     129.686 133.827 120.222  1.00 50.12           O  
ATOM    903  CB  ALA A 122     129.096 131.879 117.616  1.00 50.12           C  
ATOM    904  N   VAL A 123     127.501 133.630 119.718  1.00 48.47           N  
ATOM    905  CA  VAL A 123     127.162 134.927 120.297  1.00 48.47           C  
ATOM    906  C   VAL A 123     127.388 134.915 121.803  1.00 48.47           C  
ATOM    907  O   VAL A 123     127.860 135.899 122.384  1.00 48.47           O  
ATOM    908  CB  VAL A 123     125.712 135.305 119.946  1.00 48.47           C  
ATOM    909  CG1 VAL A 123     125.252 136.492 120.772  1.00 48.47           C  
ATOM    910  CG2 VAL A 123     125.591 135.613 118.469  1.00 48.47           C  
ATOM    911  N   ASP A 124     127.045 133.806 122.459  1.00 54.61           N  
ATOM    912  CA  ASP A 124     127.284 133.697 123.892  1.00 54.61           C  
ATOM    913  C   ASP A 124     128.771 133.790 124.201  1.00 54.61           C  
ATOM    914  O   ASP A 124     129.170 134.479 125.144  1.00 54.61           O  
ATOM    915  CB  ASP A 124     126.704 132.388 124.424  1.00 54.61           C  
ATOM    916  CG  ASP A 124     126.946 132.203 125.910  1.00 54.61           C  
ATOM    917  OD1 ASP A 124     127.107 133.215 126.623  1.00 54.61           O  
ATOM    918  OD2 ASP A 124     126.979 131.041 126.366  1.00 54.61           O  
ATOM    919  N   ARG A 125     129.608 133.113 123.411  1.00 55.13           N  
ATOM    920  CA  ARG A 125     131.051 133.211 123.621  1.00 55.13           C  
ATOM    921  C   ARG A 125     131.549 134.628 123.369  1.00 55.13           C  
ATOM    922  O   ARG A 125     132.428 135.124 124.085  1.00 55.13           O  
ATOM    923  CB  ARG A 125     131.787 132.220 122.722  1.00 55.13           C  
ATOM    924  CG  ARG A 125     131.829 130.806 123.262  1.00 55.13           C  
ATOM    925  CD  ARG A 125     132.057 129.809 122.144  1.00 55.13           C  
ATOM    926  NE  ARG A 125     132.179 128.445 122.644  1.00 55.13           N  
ATOM    927  CZ  ARG A 125     132.359 127.384 121.872  1.00 55.13           C  
ATOM    928  NH1 ARG A 125     132.459 127.495 120.559  1.00 55.13           N  
ATOM    929  NH2 ARG A 125     132.448 126.182 122.433  1.00 55.13           N  
ATOM    930  N   TYR A 126     131.003 135.289 122.347  1.00 52.29           N  
ATOM    931  CA  TYR A 126     131.368 136.675 122.071  1.00 52.29           C  
ATOM    932  C   TYR A 126     131.053 137.565 123.264  1.00 52.29           C  
ATOM    933  O   TYR A 126     131.873 138.400 123.661  1.00 52.29           O  
ATOM    934  CB  TYR A 126     130.635 137.153 120.815  1.00 52.29           C  
ATOM    935  CG  TYR A 126     130.598 138.652 120.589  1.00 52.29           C  
ATOM    936  CD1 TYR A 126     131.726 139.438 120.772  1.00 52.29           C  
ATOM    937  CD2 TYR A 126     129.430 139.274 120.174  1.00 52.29           C  
ATOM    938  CE1 TYR A 126     131.685 140.801 120.560  1.00 52.29           C  
ATOM    939  CE2 TYR A 126     129.381 140.635 119.959  1.00 52.29           C  
ATOM    940  CZ  TYR A 126     130.511 141.393 120.153  1.00 52.29           C  
ATOM    941  OH  TYR A 126     130.465 142.750 119.939  1.00 52.29           O  
ATOM    942  N   PHE A 127     129.874 137.388 123.859  1.00 53.46           N  
ATOM    943  CA  PHE A 127     129.516 138.181 125.030  1.00 53.46           C  
ATOM    944  C   PHE A 127     130.370 137.819 126.239  1.00 53.46           C  
ATOM    945  O   PHE A 127     130.711 138.698 127.036  1.00 53.46           O  
ATOM    946  CB  PHE A 127     128.032 138.008 125.349  1.00 53.46           C  
ATOM    947  CG  PHE A 127     127.141 138.957 124.604  1.00 53.46           C  
ATOM    948  CD1 PHE A 127     127.415 140.313 124.586  1.00 53.46           C  
ATOM    949  CD2 PHE A 127     126.033 138.494 123.916  1.00 53.46           C  
ATOM    950  CE1 PHE A 127     126.600 141.189 123.901  1.00 53.46           C  
ATOM    951  CE2 PHE A 127     125.214 139.367 123.229  1.00 53.46           C  
ATOM    952  CZ  PHE A 127     125.498 140.715 123.222  1.00 53.46           C  
ATOM    953  N   ARG A 128     130.721 136.542 126.397  1.00 52.85           N  
ATOM    954  CA  ARG A 128     131.561 136.142 127.522  1.00 52.85           C  
ATOM    955  C   ARG A 128     132.951 136.755 127.421  1.00 52.85           C  
ATOM    956  O   ARG A 128     133.521 137.181 128.431  1.00 52.85           O  
ATOM    957  CB  ARG A 128     131.666 134.619 127.595  1.00 52.85           C  
ATOM    958  CG  ARG A 128     130.362 133.884 127.854  1.00 52.85           C  
ATOM    959  CD  ARG A 128     129.991 133.845 129.323  1.00 52.85           C  
ATOM    960  NE  ARG A 128     128.714 133.171 129.523  1.00 52.85           N  
ATOM    961  CZ  ARG A 128     128.161 132.943 130.706  1.00 52.85           C  
ATOM    962  NH1 ARG A 128     128.747 133.325 131.828  1.00 52.85           N  
ATOM    963  NH2 ARG A 128     126.990 132.314 130.764  1.00 52.85           N  
ATOM    964  N   VAL A 129     133.514 136.805 126.218  1.00 52.82           N  
ATOM    965  CA  VAL A 129     134.917 137.181 126.056  1.00 52.82           C  
ATOM    966  C   VAL A 129     135.083 138.684 125.868  1.00 52.82           C  
ATOM    967  O   VAL A 129     135.947 139.304 126.493  1.00 52.82           O  
ATOM    968  CB  VAL A 129     135.538 136.394 124.884  1.00 52.82           C  
ATOM    969  CG1 VAL A 129     136.869 136.998 124.487  1.00 52.82           C  
ATOM    970  CG2 VAL A 129     135.705 134.935 125.262  1.00 52.82           C  
ATOM    971  N   VAL A 130     134.273 139.302 125.015  1.00 55.24           N  
ATOM    972  CA  VAL A 130     134.469 140.712 124.689  1.00 55.24           C  
ATOM    973  C   VAL A 130     133.720 141.626 125.651  1.00 55.24           C  
ATOM    974  O   VAL A 130     134.235 142.678 126.038  1.00 55.24           O  
ATOM    975  CB  VAL A 130     134.057 140.973 123.228  1.00 55.24           C  
ATOM    976  CG1 VAL A 130     134.346 142.414 122.846  1.00 55.24           C  
ATOM    977  CG2 VAL A 130     134.790 140.024 122.302  1.00 55.24           C  
ATOM    978  N   HIS A 131     132.506 141.253 126.057  1.00 58.28           N  
ATOM    979  CA  HIS A 131     131.658 142.081 126.913  1.00 58.28           C  
ATOM    980  C   HIS A 131     131.383 141.345 128.220  1.00 58.28           C  
ATOM    981  O   HIS A 131     130.244 140.943 128.491  1.00 58.28           O  
ATOM    982  CB  HIS A 131     130.347 142.432 126.211  1.00 58.28           C  
ATOM    983  CG  HIS A 131     130.487 143.483 125.157  1.00 58.28           C  
ATOM    984  ND1 HIS A 131     131.674 143.730 124.503  1.00 58.28           N  
ATOM    985  CD2 HIS A 131     129.584 144.347 124.635  1.00 58.28           C  
ATOM    986  CE1 HIS A 131     131.498 144.704 123.628  1.00 58.28           C  
ATOM    987  NE2 HIS A 131     130.238 145.096 123.688  1.00 58.28           N  
ATOM    988  N   PRO A 132     132.402 141.170 129.064  1.00 55.01           N  
ATOM    989  CA  PRO A 132     132.219 140.340 130.265  1.00 55.01           C  
ATOM    990  C   PRO A 132     131.236 140.914 131.268  1.00 55.01           C  
ATOM    991  O   PRO A 132     130.714 140.157 132.095  1.00 55.01           O  
ATOM    992  CB  PRO A 132     133.632 140.251 130.861  1.00 55.01           C  
ATOM    993  CG  PRO A 132     134.494 141.190 130.073  1.00 55.01           C  
ATOM    994  CD  PRO A 132     133.654 141.939 129.099  1.00 55.01           C  
ATOM    995  N   HIS A 133     130.959 142.214 131.223  1.00 61.59           N  
ATOM    996  CA  HIS A 133     130.121 142.865 132.219  1.00 61.59           C  
ATOM    997  C   HIS A 133     128.693 143.088 131.741  1.00 61.59           C  
ATOM    998  O   HIS A 133     127.933 143.797 132.407  1.00 61.59           O  
ATOM    999  CB  HIS A 133     130.746 144.196 132.636  1.00 61.59           C  
ATOM   1000  CG  HIS A 133     132.038 144.044 133.375  1.00 61.59           C  
ATOM   1001  ND1 HIS A 133     132.205 143.137 134.399  1.00 61.59           N  
ATOM   1002  CD2 HIS A 133     133.226 144.677 133.235  1.00 61.59           C  
ATOM   1003  CE1 HIS A 133     133.440 143.220 134.860  1.00 61.59           C  
ATOM   1004  NE2 HIS A 133     134.080 144.147 134.171  1.00 61.59           N  
ATOM   1005  N   HIS A 134     128.310 142.504 130.611  1.00 66.02           N  
ATOM   1006  CA  HIS A 134     126.955 142.672 130.118  1.00 66.02           C  
ATOM   1007  C   HIS A 134     125.993 141.765 130.881  1.00 66.02           C  
ATOM   1008  O   HIS A 134     126.391 140.807 131.549  1.00 66.02           O  
ATOM   1009  CB  HIS A 134     126.889 142.384 128.620  1.00 66.02           C  
ATOM   1010  CG  HIS A 134     125.804 143.131 127.913  1.00 66.02           C  
ATOM   1011  ND1 HIS A 134     125.817 144.501 127.768  1.00 66.02           N  
ATOM   1012  CD2 HIS A 134     124.670 142.700 127.312  1.00 66.02           C  
ATOM   1013  CE1 HIS A 134     124.738 144.882 127.107  1.00 66.02           C  
ATOM   1014  NE2 HIS A 134     124.026 143.808 126.819  1.00 66.02           N  
ATOM   1015  N   ALA A 135     124.702 142.086 130.779  1.00 67.99           N  
ATOM   1016  CA  ALA A 135     123.688 141.311 131.487  1.00 67.99           C  
ATOM   1017  C   ALA A 135     123.558 139.906 130.914  1.00 67.99           C  
ATOM   1018  O   ALA A 135     123.387 138.937 131.664  1.00 67.99           O  
ATOM   1019  CB  ALA A 135     122.344 142.037 131.437  1.00 67.99           C  
ATOM   1020  N   LEU A 136     123.658 139.770 129.591  1.00 65.57           N  
ATOM   1021  CA  LEU A 136     123.423 138.493 128.927  1.00 65.57           C  
ATOM   1022  C   LEU A 136     124.457 137.439 129.307  1.00 65.57           C  
ATOM   1023  O   LEU A 136     124.360 136.287 128.873  1.00 65.57           O  
ATOM   1024  CB  LEU A 136     123.403 138.674 127.408  1.00 65.57           C  
ATOM   1025  CG  LEU A 136     122.018 138.773 126.766  1.00 65.57           C  
ATOM   1026  CD1 LEU A 136     121.274 140.000 127.265  1.00 65.57           C  
ATOM   1027  CD2 LEU A 136     122.126 138.785 125.250  1.00 65.57           C  
ATOM   1028  N   ASN A 137     125.448 137.817 130.109  1.00 63.73           N  
ATOM   1029  CA  ASN A 137     126.445 136.871 130.584  1.00 63.73           C  
ATOM   1030  C   ASN A 137     126.061 136.210 131.901  1.00 63.73           C  
ATOM   1031  O   ASN A 137     126.760 135.288 132.337  1.00 63.73           O  
ATOM   1032  CB  ASN A 137     127.798 137.567 130.743  1.00 63.73           C  
ATOM   1033  CG  ASN A 137     128.460 137.851 129.414  1.00 63.73           C  
ATOM   1034  OD1 ASN A 137     128.656 136.950 128.602  1.00 63.73           O  
ATOM   1035  ND2 ASN A 137     128.811 139.110 129.185  1.00 63.73           N  
ATOM   1036  N   LYS A 138     124.982 136.651 132.544  1.00 71.08           N  
ATOM   1037  CA  LYS A 138     124.562 136.083 133.822  1.00 71.08           C  
ATOM   1038  C   LYS A 138     123.049 135.915 133.866  1.00 71.08           C  
ATOM   1039  O   LYS A 138     122.409 136.156 134.894  1.00 71.08           O  
ATOM   1040  CB  LYS A 138     125.048 136.941 134.990  1.00 71.08           C  
ATOM   1041  CG  LYS A 138     124.620 138.398 134.918  1.00 71.08           C  
ATOM   1042  CD  LYS A 138     125.486 139.272 135.809  1.00 71.08           C  
ATOM   1043  CE  LYS A 138     126.556 139.986 135.005  1.00 71.08           C  
ATOM   1044  NZ  LYS A 138     125.963 140.895 133.987  1.00 71.08           N  
ATOM   1045  N   ILE A 139     122.454 135.488 132.749  1.00 71.63           N  
ATOM   1046  CA  ILE A 139     121.003 135.343 132.705  1.00 71.63           C  
ATOM   1047  C   ILE A 139     120.562 134.159 133.559  1.00 71.63           C  
ATOM   1048  O   ILE A 139     121.351 133.283 133.931  1.00 71.63           O  
ATOM   1049  CB  ILE A 139     120.502 135.196 131.260  1.00 71.63           C  
ATOM   1050  CG1 ILE A 139     120.842 133.808 130.714  1.00 71.63           C  
ATOM   1051  CG2 ILE A 139     121.082 136.284 130.385  1.00 71.63           C  
ATOM   1052  CD1 ILE A 139     120.765 133.710 129.208  1.00 71.63           C  
ATOM   1053  N   SER A 140     119.272 134.143 133.874  1.00 75.94           N  
ATOM   1054  CA  SER A 140     118.666 133.072 134.647  1.00 75.94           C  
ATOM   1055  C   SER A 140     118.269 131.916 133.737  1.00 75.94           C  
ATOM   1056  O   SER A 140     118.214 132.045 132.512  1.00 75.94           O  
ATOM   1057  CB  SER A 140     117.444 133.586 135.408  1.00 75.94           C  
ATOM   1058  OG  SER A 140     117.692 134.865 135.965  1.00 75.94           O  
ATOM   1059  N   ASN A 141     117.991 130.769 134.359  1.00 76.03           N  
ATOM   1060  CA  ASN A 141     117.594 129.594 133.592  1.00 76.03           C  
ATOM   1061  C   ASN A 141     116.236 129.782 132.930  1.00 76.03           C  
ATOM   1062  O   ASN A 141     116.000 129.241 131.843  1.00 76.03           O  
ATOM   1063  CB  ASN A 141     117.579 128.363 134.493  1.00 76.03           C  
ATOM   1064  CG  ASN A 141     118.908 127.645 134.510  1.00 76.03           C  
ATOM   1065  OD1 ASN A 141     119.049 126.562 133.944  1.00 76.03           O  
ATOM   1066  ND2 ASN A 141     119.896 128.250 135.156  1.00 76.03           N  
ATOM   1067  N   ARG A 142     115.331 130.529 133.567  1.00 79.14           N  
ATOM   1068  CA  ARG A 142     114.021 130.778 132.974  1.00 79.14           C  
ATOM   1069  C   ARG A 142     114.153 131.510 131.646  1.00 79.14           C  
ATOM   1070  O   ARG A 142     113.528 131.133 130.648  1.00 79.14           O  
ATOM   1071  CB  ARG A 142     113.153 131.581 133.942  1.00 79.14           C  
ATOM   1072  CG  ARG A 142     111.656 131.435 133.723  1.00 79.14           C  
ATOM   1073  CD  ARG A 142     111.139 130.115 134.269  1.00 79.14           C  
ATOM   1074  NE  ARG A 142     109.771 130.231 134.762  1.00 79.14           N  
ATOM   1075  CZ  ARG A 142     109.225 129.418 135.656  1.00 79.14           C  
ATOM   1076  NH1 ARG A 142     109.904 128.412 136.182  1.00 79.14           N  
ATOM   1077  NH2 ARG A 142     107.965 129.621 136.033  1.00 79.14           N  
ATOM   1078  N   THR A 143     114.975 132.562 131.615  1.00 77.45           N  
ATOM   1079  CA  THR A 143     115.160 133.320 130.383  1.00 77.45           C  
ATOM   1080  C   THR A 143     115.817 132.468 129.305  1.00 77.45           C  
ATOM   1081  O   THR A 143     115.453 132.557 128.128  1.00 77.45           O  
ATOM   1082  CB  THR A 143     115.992 134.573 130.652  1.00 77.45           C  
ATOM   1083  OG1 THR A 143     117.372 134.211 130.780  1.00 77.45           O  
ATOM   1084  CG2 THR A 143     115.531 135.252 131.930  1.00 77.45           C  
ATOM   1085  N   ALA A 144     116.792 131.641 129.686  1.00 73.18           N  
ATOM   1086  CA  ALA A 144     117.452 130.783 128.708  1.00 73.18           C  
ATOM   1087  C   ALA A 144     116.482 129.765 128.123  1.00 73.18           C  
ATOM   1088  O   ALA A 144     116.488 129.515 126.912  1.00 73.18           O  
ATOM   1089  CB  ALA A 144     118.650 130.085 129.345  1.00 73.18           C  
ATOM   1090  N   ALA A 145     115.638 129.166 128.966  1.00 70.58           N  
ATOM   1091  CA  ALA A 145     114.643 128.224 128.465  1.00 70.58           C  
ATOM   1092  C   ALA A 145     113.629 128.919 127.565  1.00 70.58           C  
ATOM   1093  O   ALA A 145     113.208 128.359 126.545  1.00 70.58           O  
ATOM   1094  CB  ALA A 145     113.943 127.528 129.631  1.00 70.58           C  
ATOM   1095  N   ILE A 146     113.225 130.139 127.926  1.00 71.81           N  
ATOM   1096  CA  ILE A 146     112.299 130.894 127.087  1.00 71.81           C  
ATOM   1097  C   ILE A 146     112.929 131.190 125.732  1.00 71.81           C  
ATOM   1098  O   ILE A 146     112.276 131.074 124.689  1.00 71.81           O  
ATOM   1099  CB  ILE A 146     111.856 132.182 127.806  1.00 71.81           C  
ATOM   1100  CG1 ILE A 146     110.805 131.859 128.869  1.00 71.81           C  
ATOM   1101  CG2 ILE A 146     111.312 133.199 126.815  1.00 71.81           C  
ATOM   1102  CD1 ILE A 146     109.677 130.987 128.367  1.00 71.81           C  
ATOM   1103  N   ILE A 147     114.208 131.571 125.724  1.00 67.20           N  
ATOM   1104  CA  ILE A 147     114.900 131.842 124.466  1.00 67.20           C  
ATOM   1105  C   ILE A 147     115.005 130.573 123.629  1.00 67.20           C  
ATOM   1106  O   ILE A 147     114.834 130.603 122.405  1.00 67.20           O  
ATOM   1107  CB  ILE A 147     116.284 132.460 124.739  1.00 67.20           C  
ATOM   1108  CG1 ILE A 147     116.134 133.875 125.296  1.00 67.20           C  
ATOM   1109  CG2 ILE A 147     117.122 132.484 123.472  1.00 67.20           C  
ATOM   1110  CD1 ILE A 147     117.447 134.599 125.484  1.00 67.20           C  
ATOM   1111  N   SER A 148     115.298 129.440 124.272  1.00 62.75           N  
ATOM   1112  CA  SER A 148     115.378 128.175 123.547  1.00 62.75           C  
ATOM   1113  C   SER A 148     114.043 127.834 122.898  1.00 62.75           C  
ATOM   1114  O   SER A 148     113.985 127.459 121.719  1.00 62.75           O  
ATOM   1115  CB  SER A 148     115.813 127.059 124.496  1.00 62.75           C  
ATOM   1116  OG  SER A 148     117.218 126.889 124.475  1.00 62.75           O  
ATOM   1117  N   CYS A 149     112.954 127.968 123.658  1.00 65.33           N  
ATOM   1118  CA  CYS A 149     111.634 127.683 123.108  1.00 65.33           C  
ATOM   1119  C   CYS A 149     111.284 128.655 121.990  1.00 65.33           C  
ATOM   1120  O   CYS A 149     110.665 128.268 120.994  1.00 65.33           O  
ATOM   1121  CB  CYS A 149     110.582 127.728 124.215  1.00 65.33           C  
ATOM   1122  SG  CYS A 149     110.134 126.103 124.868  1.00 65.33           S  
ATOM   1123  N   LEU A 150     111.678 129.922 122.132  1.00 63.80           N  
ATOM   1124  CA  LEU A 150     111.409 130.908 121.091  1.00 63.80           C  
ATOM   1125  C   LEU A 150     112.158 130.566 119.808  1.00 63.80           C  
ATOM   1126  O   LEU A 150     111.607 130.688 118.709  1.00 63.80           O  
ATOM   1127  CB  LEU A 150     111.773 132.306 121.608  1.00 63.80           C  
ATOM   1128  CG  LEU A 150     111.633 133.620 120.823  1.00 63.80           C  
ATOM   1129  CD1 LEU A 150     111.928 134.776 121.761  1.00 63.80           C  
ATOM   1130  CD2 LEU A 150     112.548 133.725 119.613  1.00 63.80           C  
ATOM   1131  N   LEU A 151     113.419 130.146 119.926  1.00 58.34           N  
ATOM   1132  CA  LEU A 151     114.188 129.775 118.742  1.00 58.34           C  
ATOM   1133  C   LEU A 151     113.606 128.538 118.072  1.00 58.34           C  
ATOM   1134  O   LEU A 151     113.513 128.474 116.838  1.00 58.34           O  
ATOM   1135  CB  LEU A 151     115.651 129.549 119.115  1.00 58.34           C  
ATOM   1136  CG  LEU A 151     116.395 130.798 119.589  1.00 58.34           C  
ATOM   1137  CD1 LEU A 151     117.667 130.419 120.327  1.00 58.34           C  
ATOM   1138  CD2 LEU A 151     116.699 131.723 118.421  1.00 58.34           C  
ATOM   1139  N   TRP A 152     113.201 127.547 118.869  1.00 59.82           N  
ATOM   1140  CA  TRP A 152     112.543 126.380 118.291  1.00 59.82           C  
ATOM   1141  C   TRP A 152     111.255 126.780 117.583  1.00 59.82           C  
ATOM   1142  O   TRP A 152     110.971 126.300 116.478  1.00 59.82           O  
ATOM   1143  CB  TRP A 152     112.266 125.338 119.373  1.00 59.82           C  
ATOM   1144  CG  TRP A 152     113.461 124.509 119.710  1.00 59.82           C  
ATOM   1145  CD1 TRP A 152     114.210 124.576 120.845  1.00 59.82           C  
ATOM   1146  CD2 TRP A 152     114.053 123.492 118.897  1.00 59.82           C  
ATOM   1147  NE1 TRP A 152     115.230 123.661 120.793  1.00 59.82           N  
ATOM   1148  CE2 TRP A 152     115.156 122.983 119.606  1.00 59.82           C  
ATOM   1149  CE3 TRP A 152     113.757 122.962 117.640  1.00 59.82           C  
ATOM   1150  CZ2 TRP A 152     115.963 121.969 119.101  1.00 59.82           C  
ATOM   1151  CZ3 TRP A 152     114.558 121.956 117.141  1.00 59.82           C  
ATOM   1152  CH2 TRP A 152     115.648 121.470 117.869  1.00 59.82           C  
ATOM   1153  N   GLY A 153     110.475 127.672 118.196  1.00 63.02           N  
ATOM   1154  CA  GLY A 153     109.254 128.136 117.562  1.00 63.02           C  
ATOM   1155  C   GLY A 153     109.516 128.876 116.266  1.00 63.02           C  
ATOM   1156  O   GLY A 153     108.766 128.736 115.301  1.00 63.02           O  
ATOM   1157  N   ILE A 154     110.584 129.676 116.229  1.00 60.47           N  
ATOM   1158  CA  ILE A 154     110.960 130.360 114.994  1.00 60.47           C  
ATOM   1159  C   ILE A 154     111.297 129.346 113.912  1.00 60.47           C  
ATOM   1160  O   ILE A 154     110.900 129.497 112.749  1.00 60.47           O  
ATOM   1161  CB  ILE A 154     112.131 131.327 115.248  1.00 60.47           C  
ATOM   1162  CG1 ILE A 154     111.613 132.693 115.697  1.00 60.47           C  
ATOM   1163  CG2 ILE A 154     112.995 131.475 114.003  1.00 60.47           C  
ATOM   1164  CD1 ILE A 154     112.713 133.691 115.980  1.00 60.47           C  
ATOM   1165  N   THR A 155     112.034 128.295 114.275  1.00 62.43           N  
ATOM   1166  CA  THR A 155     112.371 127.267 113.295  1.00 62.43           C  
ATOM   1167  C   THR A 155     111.117 126.598 112.739  1.00 62.43           C  
ATOM   1168  O   THR A 155     110.958 126.460 111.517  1.00 62.43           O  
ATOM   1169  CB  THR A 155     113.297 126.228 113.922  1.00 62.43           C  
ATOM   1170  OG1 THR A 155     114.331 126.891 114.660  1.00 62.43           O  
ATOM   1171  CG2 THR A 155     113.920 125.380 112.843  1.00 62.43           C  
ATOM   1172  N   ILE A 156     110.204 126.186 113.622  1.00 65.67           N  
ATOM   1173  CA  ILE A 156     108.977 125.561 113.131  1.00 65.67           C  
ATOM   1174  C   ILE A 156     108.177 126.545 112.288  1.00 65.67           C  
ATOM   1175  O   ILE A 156     107.584 126.167 111.274  1.00 65.67           O  
ATOM   1176  CB  ILE A 156     108.130 124.981 114.279  1.00 65.67           C  
ATOM   1177  CG1 ILE A 156     109.011 124.446 115.401  1.00 65.67           C  
ATOM   1178  CG2 ILE A 156     107.219 123.885 113.757  1.00 65.67           C  
ATOM   1179  CD1 ILE A 156     109.659 123.119 115.088  1.00 65.67           C  
ATOM   1180  N   GLY A 157     108.146 127.818 112.686  1.00 67.96           N  
ATOM   1181  CA  GLY A 157     107.433 128.808 111.899  1.00 67.96           C  
ATOM   1182  C   GLY A 157     108.019 128.990 110.515  1.00 67.96           C  
ATOM   1183  O   GLY A 157     107.293 129.281 109.561  1.00 67.96           O  
ATOM   1184  N   LEU A 158     109.334 128.829 110.386  1.00 68.05           N  
ATOM   1185  CA  LEU A 158     109.966 128.926 109.079  1.00 68.05           C  
ATOM   1186  C   LEU A 158     109.849 127.646 108.261  1.00 68.05           C  
ATOM   1187  O   LEU A 158     110.092 127.687 107.050  1.00 68.05           O  
ATOM   1188  CB  LEU A 158     111.443 129.302 109.226  1.00 68.05           C  
ATOM   1189  CG  LEU A 158     111.757 130.643 109.889  1.00 68.05           C  
ATOM   1190  CD1 LEU A 158     113.257 130.879 109.937  1.00 68.05           C  
ATOM   1191  CD2 LEU A 158     111.060 131.775 109.156  1.00 68.05           C  
ATOM   1192  N   THR A 159     109.509 126.512 108.877  1.00 68.57           N  
ATOM   1193  CA  THR A 159     109.399 125.268 108.114  1.00 68.57           C  
ATOM   1194  C   THR A 159     107.998 124.656 108.032  1.00 68.57           C  
ATOM   1195  O   THR A 159     107.852 123.577 107.440  1.00 68.57           O  
ATOM   1196  CB  THR A 159     110.380 124.221 108.654  1.00 68.57           C  
ATOM   1197  OG1 THR A 159     109.782 123.514 109.745  1.00 68.57           O  
ATOM   1198  CG2 THR A 159     111.694 124.855 109.075  1.00 68.57           C  
ATOM   1199  N   VAL A 160     106.957 125.295 108.576  1.00 67.98           N  
ATOM   1200  CA  VAL A 160     105.616 124.767 108.299  1.00 67.98           C  
ATOM   1201  C   VAL A 160     105.302 124.831 106.810  1.00 67.98           C  
ATOM   1202  O   VAL A 160     104.521 124.017 106.300  1.00 67.98           O  
ATOM   1203  CB  VAL A 160     104.502 125.464 109.116  1.00 67.98           C  
ATOM   1204  CG1 VAL A 160     104.885 125.664 110.551  1.00 67.98           C  
ATOM   1205  CG2 VAL A 160     104.119 126.798 108.488  1.00 67.98           C  
ATOM   1206  N   HIS A 161     105.888 125.789 106.085  1.00 75.65           N  
ATOM   1207  CA  HIS A 161     105.621 125.856 104.652  1.00 75.65           C  
ATOM   1208  C   HIS A 161     106.205 124.654 103.924  1.00 75.65           C  
ATOM   1209  O   HIS A 161     105.607 124.170 102.960  1.00 75.65           O  
ATOM   1210  CB  HIS A 161     106.127 127.182 104.073  1.00 75.65           C  
ATOM   1211  CG  HIS A 161     107.617 127.290 103.971  1.00 75.65           C  
ATOM   1212  ND1 HIS A 161     108.372 126.513 103.119  1.00 75.65           N  
ATOM   1213  CD2 HIS A 161     108.491 128.104 104.609  1.00 75.65           C  
ATOM   1214  CE1 HIS A 161     109.647 126.836 103.244  1.00 75.65           C  
ATOM   1215  NE2 HIS A 161     109.746 127.797 104.144  1.00 75.65           N  
ATOM   1216  N   LEU A 162     107.358 124.151 104.372  1.00 71.59           N  
ATOM   1217  CA  LEU A 162     107.840 122.869 103.867  1.00 71.59           C  
ATOM   1218  C   LEU A 162     106.949 121.726 104.326  1.00 71.59           C  
ATOM   1219  O   LEU A 162     106.756 120.754 103.586  1.00 71.59           O  
ATOM   1220  CB  LEU A 162     109.281 122.626 104.315  1.00 71.59           C  
ATOM   1221  CG  LEU A 162     110.382 123.375 103.565  1.00 71.59           C  
ATOM   1222  CD1 LEU A 162     111.657 122.562 103.590  1.00 71.59           C  
ATOM   1223  CD2 LEU A 162     109.964 123.656 102.131  1.00 71.59           C  
ATOM   1224  N   LEU A 163     106.409 121.823 105.541  1.00 68.04           N  
ATOM   1225  CA  LEU A 163     105.505 120.787 106.030  1.00 68.04           C  
ATOM   1226  C   LEU A 163     104.242 120.687 105.180  1.00 68.04           C  
ATOM   1227  O   LEU A 163     103.650 119.608 105.076  1.00 68.04           O  
ATOM   1228  CB  LEU A 163     105.142 121.057 107.491  1.00 68.04           C  
ATOM   1229  CG  LEU A 163     104.271 120.028 108.214  1.00 68.04           C  
ATOM   1230  CD1 LEU A 163     104.987 118.695 108.339  1.00 68.04           C  
ATOM   1231  CD2 LEU A 163     103.857 120.552 109.582  1.00 68.04           C  
ATOM   1232  N   LYS A 164     103.819 121.790 104.561  1.00 70.49           N  
ATOM   1233  CA  LYS A 164     102.524 121.845 103.893  1.00 70.49           C  
ATOM   1234  C   LYS A 164     102.585 121.900 102.371  1.00 70.49           C  
ATOM   1235  O   LYS A 164     101.555 121.675 101.727  1.00 70.49           O  
ATOM   1236  CB  LYS A 164     101.733 123.067 104.383  1.00 70.49           C  
ATOM   1237  CG  LYS A 164     101.032 122.875 105.716  1.00 70.49           C  
ATOM   1238  CD  LYS A 164     100.129 124.058 106.029  1.00 70.49           C  
ATOM   1239  CE  LYS A 164      98.954 124.128 105.067  1.00 70.49           C  
ATOM   1240  NZ  LYS A 164      97.649 123.994 105.770  1.00 70.49           N  
ATOM   1241  N   LYS A 165     103.747 122.190 101.781  1.00 78.08           N  
ATOM   1242  CA  LYS A 165     103.772 122.619 100.383  1.00 78.08           C  
ATOM   1243  C   LYS A 165     103.419 121.488  99.416  1.00 78.08           C  
ATOM   1244  O   LYS A 165     102.632 121.698  98.485  1.00 78.08           O  
ATOM   1245  CB  LYS A 165     105.126 123.270 100.074  1.00 78.08           C  
ATOM   1246  CG  LYS A 165     105.729 123.099  98.681  1.00 78.08           C  
ATOM   1247  CD  LYS A 165     106.514 121.810  98.575  1.00 78.08           C  
ATOM   1248  CE  LYS A 165     107.633 121.777  99.601  1.00 78.08           C  
ATOM   1249  NZ  LYS A 165     108.302 120.453  99.631  1.00 78.08           N  
ATOM   1250  N   LYS A 166     103.960 120.284  99.613  1.00 82.76           N  
ATOM   1251  CA  LYS A 166     103.675 119.203  98.673  1.00 82.76           C  
ATOM   1252  C   LYS A 166     103.933 117.841  99.302  1.00 82.76           C  
ATOM   1253  O   LYS A 166     104.464 117.727 100.410  1.00 82.76           O  
ATOM   1254  CB  LYS A 166     104.498 119.331  97.383  1.00 82.76           C  
ATOM   1255  N   MET A 167     103.542 116.802  98.555  1.00 78.74           N  
ATOM   1256  CA  MET A 167     103.659 115.389  98.898  1.00 78.74           C  
ATOM   1257  C   MET A 167     104.653 114.720  97.953  1.00 78.74           C  
ATOM   1258  O   MET A 167     105.176 115.387  97.051  1.00 78.74           O  
ATOM   1259  CB  MET A 167     102.287 114.714  98.813  1.00 78.74           C  
ATOM   1260  CG  MET A 167     101.195 115.425  99.581  1.00 78.74           C  
ATOM   1261  SD  MET A 167      99.595 115.345  98.755  1.00 78.74           S  
ATOM   1262  CE  MET A 167      99.349 117.055  98.294  1.00 78.74           C  
ATOM   1263  N   PRO A 168     104.960 113.430  98.124  1.00 74.38           N  
ATOM   1264  CA  PRO A 168     105.804 112.746  97.133  1.00 74.38           C  
ATOM   1265  C   PRO A 168     105.216 112.854  95.735  1.00 74.38           C  
ATOM   1266  O   PRO A 168     103.999 112.799  95.546  1.00 74.38           O  
ATOM   1267  CB  PRO A 168     105.827 111.291  97.616  1.00 74.38           C  
ATOM   1268  CG  PRO A 168     105.368 111.306  99.018  1.00 74.38           C  
ATOM   1269  CD  PRO A 168     104.820 112.651  99.367  1.00 74.38           C  
ATOM   1270  N   ILE A 169     106.095 113.013  94.749  1.00 78.22           N  
ATOM   1271  CA  ILE A 169     105.694 113.288  93.375  1.00 78.22           C  
ATOM   1272  C   ILE A 169     106.078 112.103  92.499  1.00 78.22           C  
ATOM   1273  O   ILE A 169     107.239 111.680  92.489  1.00 78.22           O  
ATOM   1274  CB  ILE A 169     106.330 114.587  92.849  1.00 78.22           C  
ATOM   1275  CG1 ILE A 169     105.602 115.804  93.422  1.00 78.22           C  
ATOM   1276  CG2 ILE A 169     106.295 114.625  91.331  1.00 78.22           C  
ATOM   1277  CD1 ILE A 169     104.094 115.703  93.362  1.00 78.22           C  
ATOM   1278  N   GLN A 170     105.101 111.575  91.768  1.00 83.77           N  
ATOM   1279  CA  GLN A 170     105.343 110.505  90.815  1.00 83.77           C  
ATOM   1280  C   GLN A 170     106.094 111.044  89.601  1.00 83.77           C  
ATOM   1281  O   GLN A 170     105.791 112.125  89.089  1.00 83.77           O  
ATOM   1282  CB  GLN A 170     104.016 109.885  90.370  1.00 83.77           C  
ATOM   1283  CG  GLN A 170     104.085 108.456  89.833  1.00 83.77           C  
ATOM   1284  CD  GLN A 170     104.957 107.526  90.660  1.00 83.77           C  
ATOM   1285  OE1 GLN A 170     105.094 107.687  91.874  1.00 83.77           O  
ATOM   1286  NE2 GLN A 170     105.558 106.545  89.999  1.00 83.77           N  
ATOM   1287  N   ASN A 171     107.085 110.281  89.142  1.00 88.97           N  
ATOM   1288  CA  ASN A 171     107.814 110.633  87.932  1.00 88.97           C  
ATOM   1289  C   ASN A 171     108.389 109.365  87.319  1.00 88.97           C  
ATOM   1290  O   ASN A 171     108.875 108.479  88.029  1.00 88.97           O  
ATOM   1291  CB  ASN A 171     108.928 111.652  88.211  1.00 88.97           C  
ATOM   1292  CG  ASN A 171     110.133 111.031  88.884  1.00 88.97           C  
ATOM   1293  OD1 ASN A 171     110.003 110.297  89.863  1.00 88.97           O  
ATOM   1294  ND2 ASN A 171     111.318 111.321  88.361  1.00 88.97           N  
ATOM   1295  N   GLY A 172     108.326 109.287  85.992  1.00 95.48           N  
ATOM   1296  CA  GLY A 172     108.786 108.109  85.286  1.00 95.48           C  
ATOM   1297  C   GLY A 172     108.090 106.849  85.755  1.00 95.48           C  
ATOM   1298  O   GLY A 172     106.890 106.671  85.529  1.00 95.48           O  
ATOM   1299  N   GLY A 173     108.836 105.968  86.416  1.00 90.98           N  
ATOM   1300  CA  GLY A 173     108.261 104.765  86.982  1.00 90.98           C  
ATOM   1301  C   GLY A 173     108.369 104.714  88.492  1.00 90.98           C  
ATOM   1302  O   GLY A 173     107.960 103.730  89.116  1.00 90.98           O  
ATOM   1303  N   ALA A 174     108.915 105.771  89.093  1.00 86.14           N  
ATOM   1304  CA  ALA A 174     109.119 105.797  90.536  1.00 86.14           C  
ATOM   1305  C   ALA A 174     108.552 107.069  91.152  1.00 86.14           C  
ATOM   1306  O   ALA A 174     107.847 107.831  90.485  1.00 86.14           O  
ATOM   1307  CB  ALA A 174     110.606 105.667  90.869  1.00 86.14           C  
ATOM   1308  N   ASN A 175     108.846 107.301  92.428  1.00 76.12           N  
ATOM   1309  CA  ASN A 175     108.394 108.492  93.128  1.00 76.12           C  
ATOM   1310  C   ASN A 175     109.586 109.187  93.766  1.00 76.12           C  
ATOM   1311  O   ASN A 175     110.507 108.532  94.263  1.00 76.12           O  
ATOM   1312  CB  ASN A 175     107.347 108.150  94.193  1.00 76.12           C  
ATOM   1313  CG  ASN A 175     107.941 107.421  95.378  1.00 76.12           C  
ATOM   1314  OD1 ASN A 175     108.720 106.483  95.215  1.00 76.12           O  
ATOM   1315  ND2 ASN A 175     107.576 107.848  96.580  1.00 76.12           N  
ATOM   1316  N   LEU A 176     109.566 110.515  93.741  1.00 70.26           N  
ATOM   1317  CA  LEU A 176     110.610 111.330  94.339  1.00 70.26           C  
ATOM   1318  C   LEU A 176     110.025 112.113  95.504  1.00 70.26           C  
ATOM   1319  O   LEU A 176     108.918 112.654  95.412  1.00 70.26           O  
ATOM   1320  CB  LEU A 176     111.240 112.275  93.299  1.00 70.26           C  
ATOM   1321  CG  LEU A 176     110.514 113.544  92.835  1.00 70.26           C  
ATOM   1322  CD1 LEU A 176     110.886 114.753  93.686  1.00 70.26           C  
ATOM   1323  CD2 LEU A 176     110.795 113.817  91.366  1.00 70.26           C  
ATOM   1324  N   CYS A 177     110.768 112.148  96.609  1.00 60.56           N  
ATOM   1325  CA  CYS A 177     110.386 112.889  97.808  1.00 60.56           C  
ATOM   1326  C   CYS A 177     111.546 113.826  98.116  1.00 60.56           C  
ATOM   1327  O   CYS A 177     112.478 113.459  98.835  1.00 60.56           O  
ATOM   1328  CB  CYS A 177     110.085 111.952  98.971  1.00 60.56           C  
ATOM   1329  SG  CYS A 177     110.012 112.761 100.583  1.00 60.56           S  
ATOM   1330  N   SER A 178     111.492 115.033  97.560  1.00 55.23           N  
ATOM   1331  CA  SER A 178     112.582 115.982  97.713  1.00 55.23           C  
ATOM   1332  C   SER A 178     112.026 117.394  97.761  1.00 55.23           C  
ATOM   1333  O   SER A 178     110.951 117.675  97.225  1.00 55.23           O  
ATOM   1334  CB  SER A 178     113.595 115.863  96.571  1.00 55.23           C  
ATOM   1335  OG  SER A 178     114.230 117.106  96.335  1.00 55.23           O  
ATOM   1336  N   SER A 179     112.777 118.281  98.412  1.00 57.80           N  
ATOM   1337  CA  SER A 179     112.460 119.699  98.443  1.00 57.80           C  
ATOM   1338  C   SER A 179     113.527 120.571  97.805  1.00 57.80           C  
ATOM   1339  O   SER A 179     113.228 121.717  97.453  1.00 57.80           O  
ATOM   1340  CB  SER A 179     112.241 120.172  99.889  1.00 57.80           C  
ATOM   1341  OG  SER A 179     113.324 119.791 100.719  1.00 57.80           O  
ATOM   1342  N   PHE A 180     114.748 120.070  97.647  1.00 59.71           N  
ATOM   1343  CA  PHE A 180     115.839 120.836  97.047  1.00 59.71           C  
ATOM   1344  C   PHE A 180     115.935 120.590  95.546  1.00 59.71           C  
ATOM   1345  O   PHE A 180     116.998 120.279  95.014  1.00 59.71           O  
ATOM   1346  CB  PHE A 180     117.151 120.492  97.738  1.00 59.71           C  
ATOM   1347  CG  PHE A 180     117.499 121.416  98.859  1.00 59.71           C  
ATOM   1348  CD1 PHE A 180     116.678 122.484  99.172  1.00 59.71           C  
ATOM   1349  CD2 PHE A 180     118.646 121.218  99.604  1.00 59.71           C  
ATOM   1350  CE1 PHE A 180     116.994 123.337 100.206  1.00 59.71           C  
ATOM   1351  CE2 PHE A 180     118.967 122.068 100.641  1.00 59.71           C  
ATOM   1352  CZ  PHE A 180     118.139 123.128 100.942  1.00 59.71           C  
ATOM   1353  N   SER A 181     114.815 120.735  94.848  1.00 59.85           N  
ATOM   1354  CA  SER A 181     114.814 120.575  93.406  1.00 59.85           C  
ATOM   1355  C   SER A 181     115.389 121.830  92.752  1.00 59.85           C  
ATOM   1356  O   SER A 181     115.855 122.755  93.422  1.00 59.85           O  
ATOM   1357  CB  SER A 181     113.402 120.277  92.908  1.00 59.85           C  
ATOM   1358  OG  SER A 181     113.431 119.645  91.641  1.00 59.85           O  
ATOM   1359  N   ILE A 182     115.364 121.864  91.424  1.00 70.86           N  
ATOM   1360  CA  ILE A 182     115.817 123.018  90.659  1.00 70.86           C  
ATOM   1361  C   ILE A 182     114.676 123.445  89.746  1.00 70.86           C  
ATOM   1362  O   ILE A 182     114.271 122.697  88.847  1.00 70.86           O  
ATOM   1363  CB  ILE A 182     117.099 122.721  89.868  1.00 70.86           C  
ATOM   1364  CG1 ILE A 182     117.002 121.371  89.157  1.00 70.86           C  
ATOM   1365  CG2 ILE A 182     118.305 122.739  90.793  1.00 70.86           C  
ATOM   1366  CD1 ILE A 182     118.277 120.962  88.460  1.00 70.86           C  
ATOM   1367  N   CYS A 183     114.149 124.644  89.983  1.00 83.79           N  
ATOM   1368  CA  CYS A 183     113.028 125.173  89.224  1.00 83.79           C  
ATOM   1369  C   CYS A 183     113.294 126.634  88.899  1.00 83.79           C  
ATOM   1370  O   CYS A 183     114.046 127.319  89.596  1.00 83.79           O  
ATOM   1371  CB  CYS A 183     111.708 125.033  89.992  1.00 83.79           C  
ATOM   1372  SG  CYS A 183     111.372 123.377  90.626  1.00 83.79           S  
ATOM   1373  N   HIS A 184     112.657 127.113  87.829  1.00 85.72           N  
ATOM   1374  CA  HIS A 184     112.879 128.478  87.350  1.00 85.72           C  
ATOM   1375  C   HIS A 184     111.987 129.450  88.122  1.00 85.72           C  
ATOM   1376  O   HIS A 184     111.115 130.130  87.576  1.00 85.72           O  
ATOM   1377  CB  HIS A 184     112.637 128.569  85.850  1.00 85.72           C  
ATOM   1378  CG  HIS A 184     113.250 129.779  85.216  1.00 85.72           C  
ATOM   1379  ND1 HIS A 184     114.189 129.697  84.210  1.00 85.72           N  
ATOM   1380  CD2 HIS A 184     113.065 131.100  85.451  1.00 85.72           C  
ATOM   1381  CE1 HIS A 184     114.552 130.915  83.850  1.00 85.72           C  
ATOM   1382  NE2 HIS A 184     113.885 131.784  84.587  1.00 85.72           N  
ATOM   1383  N   THR A 185     112.217 129.498  89.432  1.00 88.04           N  
ATOM   1384  CA  THR A 185     111.575 130.477  90.299  1.00 88.04           C  
ATOM   1385  C   THR A 185     112.414 130.621  91.559  1.00 88.04           C  
ATOM   1386  O   THR A 185     113.153 129.710  91.942  1.00 88.04           O  
ATOM   1387  CB  THR A 185     110.134 130.083  90.657  1.00 88.04           C  
ATOM   1388  OG1 THR A 185     109.519 129.416  89.548  1.00 88.04           O  
ATOM   1389  CG2 THR A 185     109.315 131.318  91.006  1.00 88.04           C  
ATOM   1390  N   PHE A 186     112.292 131.779  92.196  1.00 88.03           N  
ATOM   1391  CA  PHE A 186     112.989 132.078  93.444  1.00 88.03           C  
ATOM   1392  C   PHE A 186     111.933 132.178  94.541  1.00 88.03           C  
ATOM   1393  O   PHE A 186     111.408 133.256  94.825  1.00 88.03           O  
ATOM   1394  CB  PHE A 186     113.808 133.360  93.328  1.00 88.03           C  
ATOM   1395  N   GLN A 187     111.624 131.041  95.155  1.00 85.59           N  
ATOM   1396  CA  GLN A 187     110.638 130.988  96.224  1.00 85.59           C  
ATOM   1397  C   GLN A 187     111.283 131.450  97.528  1.00 85.59           C  
ATOM   1398  O   GLN A 187     112.406 131.962  97.553  1.00 85.59           O  
ATOM   1399  CB  GLN A 187     110.065 129.579  96.346  1.00 85.59           C  
ATOM   1400  CG  GLN A 187     109.722 128.928  95.020  1.00 85.59           C  
ATOM   1401  CD  GLN A 187     110.007 127.439  95.017  1.00 85.59           C  
ATOM   1402  OE1 GLN A 187     109.315 126.662  95.673  1.00 85.59           O  
ATOM   1403  NE2 GLN A 187     111.035 127.035  94.280  1.00 85.59           N  
ATOM   1404  N   TRP A 188     110.568 131.278  98.638  1.00 85.34           N  
ATOM   1405  CA  TRP A 188     111.141 131.564  99.945  1.00 85.34           C  
ATOM   1406  C   TRP A 188     112.126 130.493 100.390  1.00 85.34           C  
ATOM   1407  O   TRP A 188     113.015 130.787 101.193  1.00 85.34           O  
ATOM   1408  CB  TRP A 188     110.026 131.713 100.984  1.00 85.34           C  
ATOM   1409  CG  TRP A 188     110.511 131.946 102.385  1.00 85.34           C  
ATOM   1410  CD1 TRP A 188     110.843 130.997 103.308  1.00 85.34           C  
ATOM   1411  CD2 TRP A 188     110.712 133.213 103.024  1.00 85.34           C  
ATOM   1412  NE1 TRP A 188     111.241 131.594 104.479  1.00 85.34           N  
ATOM   1413  CE2 TRP A 188     111.169 132.954 104.331  1.00 85.34           C  
ATOM   1414  CE3 TRP A 188     110.550 134.541 102.617  1.00 85.34           C  
ATOM   1415  CZ2 TRP A 188     111.466 133.973 105.234  1.00 85.34           C  
ATOM   1416  CZ3 TRP A 188     110.845 135.551 103.515  1.00 85.34           C  
ATOM   1417  CH2 TRP A 188     111.298 135.262 104.808  1.00 85.34           C  
ATOM   1418  N   HIS A 189     111.999 129.270  99.870  1.00 73.47           N  
ATOM   1419  CA  HIS A 189     112.822 128.163 100.347  1.00 73.47           C  
ATOM   1420  C   HIS A 189     114.297 128.379 100.028  1.00 73.47           C  
ATOM   1421  O   HIS A 189     115.155 128.275 100.913  1.00 73.47           O  
ATOM   1422  CB  HIS A 189     112.326 126.854  99.733  1.00 73.47           C  
ATOM   1423  CG  HIS A 189     112.866 125.629 100.400  1.00 73.47           C  
ATOM   1424  ND1 HIS A 189     113.700 125.683 101.496  1.00 73.47           N  
ATOM   1425  CD2 HIS A 189     112.701 124.315 100.119  1.00 73.47           C  
ATOM   1426  CE1 HIS A 189     114.020 124.456 101.864  1.00 73.47           C  
ATOM   1427  NE2 HIS A 189     113.427 123.607 101.044  1.00 73.47           N  
ATOM   1428  N   GLU A 190     114.613 128.678  98.767  1.00 70.01           N  
ATOM   1429  CA  GLU A 190     116.010 128.847  98.381  1.00 70.01           C  
ATOM   1430  C   GLU A 190     116.606 130.103  99.003  1.00 70.01           C  
ATOM   1431  O   GLU A 190     117.769 130.104  99.431  1.00 70.01           O  
ATOM   1432  CB  GLU A 190     116.129 128.887  96.860  1.00 70.01           C  
ATOM   1433  CG  GLU A 190     115.377 127.771  96.153  1.00 70.01           C  
ATOM   1434  CD  GLU A 190     115.561 126.426  96.825  1.00 70.01           C  
ATOM   1435  OE1 GLU A 190     116.609 125.787  96.606  1.00 70.01           O  
ATOM   1436  OE2 GLU A 190     114.653 126.004  97.570  1.00 70.01           O  
ATOM   1437  N   ALA A 191     115.825 131.182  99.058  1.00 69.41           N  
ATOM   1438  CA  ALA A 191     116.279 132.379  99.753  1.00 69.41           C  
ATOM   1439  C   ALA A 191     116.502 132.094 101.230  1.00 69.41           C  
ATOM   1440  O   ALA A 191     117.437 132.623 101.838  1.00 69.41           O  
ATOM   1441  CB  ALA A 191     115.271 133.511  99.566  1.00 69.41           C  
ATOM   1442  N   MET A 192     115.655 131.250 101.825  1.00 70.26           N  
ATOM   1443  CA  MET A 192     115.843 130.893 103.226  1.00 70.26           C  
ATOM   1444  C   MET A 192     117.114 130.075 103.416  1.00 70.26           C  
ATOM   1445  O   MET A 192     117.804 130.231 104.424  1.00 70.26           O  
ATOM   1446  CB  MET A 192     114.600 130.162 103.753  1.00 70.26           C  
ATOM   1447  CG  MET A 192     114.754 129.333 105.031  1.00 70.26           C  
ATOM   1448  SD  MET A 192     115.602 127.747 104.887  1.00 70.26           S  
ATOM   1449  CE  MET A 192     114.217 126.649 104.605  1.00 70.26           C  
ATOM   1450  N   PHE A 193     117.443 129.201 102.461  1.00 62.78           N  
ATOM   1451  CA  PHE A 193     118.710 128.472 102.532  1.00 62.78           C  
ATOM   1452  C   PHE A 193     119.897 129.428 102.450  1.00 62.78           C  
ATOM   1453  O   PHE A 193     120.848 129.342 103.243  1.00 62.78           O  
ATOM   1454  CB  PHE A 193     118.779 127.436 101.408  1.00 62.78           C  
ATOM   1455  CG  PHE A 193     119.865 126.411 101.586  1.00 62.78           C  
ATOM   1456  CD1 PHE A 193     120.468 126.218 102.818  1.00 62.78           C  
ATOM   1457  CD2 PHE A 193     120.291 125.647 100.515  1.00 62.78           C  
ATOM   1458  CE1 PHE A 193     121.468 125.276 102.978  1.00 62.78           C  
ATOM   1459  CE2 PHE A 193     121.288 124.705 100.669  1.00 62.78           C  
ATOM   1460  CZ  PHE A 193     121.877 124.520 101.902  1.00 62.78           C  
ATOM   1461  N   LEU A 194     119.854 130.357 101.494  1.00 63.04           N  
ATOM   1462  CA  LEU A 194     120.950 131.309 101.358  1.00 63.04           C  
ATOM   1463  C   LEU A 194     121.089 132.165 102.610  1.00 63.04           C  
ATOM   1464  O   LEU A 194     122.206 132.462 103.043  1.00 63.04           O  
ATOM   1465  CB  LEU A 194     120.747 132.184 100.122  1.00 63.04           C  
ATOM   1466  CG  LEU A 194     121.631 131.833  98.924  1.00 63.04           C  
ATOM   1467  CD1 LEU A 194     121.258 130.471  98.361  1.00 63.04           C  
ATOM   1468  CD2 LEU A 194     121.540 132.905  97.852  1.00 63.04           C  
ATOM   1469  N   LEU A 195     119.966 132.560 103.212  1.00 64.24           N  
ATOM   1470  CA  LEU A 195     120.016 133.347 104.440  1.00 64.24           C  
ATOM   1471  C   LEU A 195     120.556 132.523 105.603  1.00 64.24           C  
ATOM   1472  O   LEU A 195     121.452 132.972 106.329  1.00 64.24           O  
ATOM   1473  CB  LEU A 195     118.627 133.893 104.764  1.00 64.24           C  
ATOM   1474  CG  LEU A 195     118.562 135.026 105.787  1.00 64.24           C  
ATOM   1475  CD1 LEU A 195     117.738 136.185 105.249  1.00 64.24           C  
ATOM   1476  CD2 LEU A 195     117.994 134.525 107.106  1.00 64.24           C  
ATOM   1477  N   GLU A 196     120.043 131.298 105.774  1.00 64.50           N  
ATOM   1478  CA  GLU A 196     120.466 130.423 106.861  1.00 64.50           C  
ATOM   1479  C   GLU A 196     121.915 130.002 106.720  1.00 64.50           C  
ATOM   1480  O   GLU A 196     122.461 129.391 107.642  1.00 64.50           O  
ATOM   1481  CB  GLU A 196     119.589 129.168 106.925  1.00 64.50           C  
ATOM   1482  CG  GLU A 196     120.005 128.085 105.935  1.00 64.50           C  
ATOM   1483  CD  GLU A 196     119.395 126.727 106.229  1.00 64.50           C  
ATOM   1484  OE1 GLU A 196     118.170 126.569 106.060  1.00 64.50           O  
ATOM   1485  OE2 GLU A 196     120.145 125.808 106.614  1.00 64.50           O  
ATOM   1486  N   PHE A 197     122.529 130.241 105.564  1.00 58.47           N  
ATOM   1487  CA  PHE A 197     123.984 130.171 105.576  1.00 58.47           C  
ATOM   1488  C   PHE A 197     124.624 131.533 105.831  1.00 58.47           C  
ATOM   1489  O   PHE A 197     125.464 131.662 106.724  1.00 58.47           O  
ATOM   1490  CB  PHE A 197     124.534 129.593 104.273  1.00 58.47           C  
ATOM   1491  CG  PHE A 197     126.037 129.544 104.241  1.00 58.47           C  
ATOM   1492  CD1 PHE A 197     126.744 129.057 105.329  1.00 58.47           C  
ATOM   1493  CD2 PHE A 197     126.742 130.014 103.151  1.00 58.47           C  
ATOM   1494  CE1 PHE A 197     128.124 129.020 105.318  1.00 58.47           C  
ATOM   1495  CE2 PHE A 197     128.126 129.979 103.136  1.00 58.47           C  
ATOM   1496  CZ  PHE A 197     128.815 129.480 104.221  1.00 58.47           C  
ATOM   1497  N   PHE A 198     124.234 132.557 105.066  1.00 57.38           N  
ATOM   1498  CA  PHE A 198     125.007 133.796 105.021  1.00 57.38           C  
ATOM   1499  C   PHE A 198     124.906 134.588 106.321  1.00 57.38           C  
ATOM   1500  O   PHE A 198     125.925 135.033 106.861  1.00 57.38           O  
ATOM   1501  CB  PHE A 198     124.556 134.646 103.834  1.00 57.38           C  
ATOM   1502  CG  PHE A 198     125.378 134.436 102.596  1.00 57.38           C  
ATOM   1503  CD1 PHE A 198     125.941 133.202 102.328  1.00 57.38           C  
ATOM   1504  CD2 PHE A 198     125.592 135.471 101.704  1.00 57.38           C  
ATOM   1505  CE1 PHE A 198     126.700 133.002 101.192  1.00 57.38           C  
ATOM   1506  CE2 PHE A 198     126.350 135.277 100.565  1.00 57.38           C  
ATOM   1507  CZ  PHE A 198     126.904 134.041 100.310  1.00 57.38           C  
ATOM   1508  N   LEU A 199     123.690 134.800 106.832  1.00 53.99           N  
ATOM   1509  CA  LEU A 199     123.559 135.598 108.051  1.00 53.99           C  
ATOM   1510  C   LEU A 199     124.262 134.963 109.244  1.00 53.99           C  
ATOM   1511  O   LEU A 199     125.044 135.661 109.915  1.00 53.99           O  
ATOM   1512  CB  LEU A 199     122.081 135.874 108.346  1.00 53.99           C  
ATOM   1513  CG  LEU A 199     121.358 136.824 107.392  1.00 53.99           C  
ATOM   1514  CD1 LEU A 199     120.152 137.443 108.081  1.00 53.99           C  
ATOM   1515  CD2 LEU A 199     122.301 137.904 106.886  1.00 53.99           C  
ATOM   1516  N   PRO A 200     124.053 133.682 109.566  1.00 49.52           N  
ATOM   1517  CA  PRO A 200     124.884 133.070 110.610  1.00 49.52           C  
ATOM   1518  C   PRO A 200     126.351 133.044 110.251  1.00 49.52           C  
ATOM   1519  O   PRO A 200     127.189 133.102 111.154  1.00 49.52           O  
ATOM   1520  CB  PRO A 200     124.307 131.657 110.736  1.00 49.52           C  
ATOM   1521  CG  PRO A 200     123.683 131.404 109.451  1.00 49.52           C  
ATOM   1522  CD  PRO A 200     123.111 132.702 109.002  1.00 49.52           C  
ATOM   1523  N   LEU A 201     126.696 132.959 108.965  1.00 49.52           N  
ATOM   1524  CA  LEU A 201     128.100 133.059 108.580  1.00 49.52           C  
ATOM   1525  C   LEU A 201     128.683 134.392 109.020  1.00 49.52           C  
ATOM   1526  O   LEU A 201     129.755 134.444 109.633  1.00 49.52           O  
ATOM   1527  CB  LEU A 201     128.254 132.882 107.070  1.00 49.52           C  
ATOM   1528  CG  LEU A 201     129.675 133.023 106.525  1.00 49.52           C  
ATOM   1529  CD1 LEU A 201     130.585 131.983 107.149  1.00 49.52           C  
ATOM   1530  CD2 LEU A 201     129.684 132.909 105.010  1.00 49.52           C  
ATOM   1531  N   GLY A 202     127.971 135.484 108.737  1.00 49.70           N  
ATOM   1532  CA  GLY A 202     128.442 136.789 109.164  1.00 49.70           C  
ATOM   1533  C   GLY A 202     128.514 136.919 110.672  1.00 49.70           C  
ATOM   1534  O   GLY A 202     129.493 137.441 111.212  1.00 49.70           O  
ATOM   1535  N   ILE A 203     127.487 136.434 111.375  1.00 47.96           N  
ATOM   1536  CA  ILE A 203     127.465 136.560 112.831  1.00 47.96           C  
ATOM   1537  C   ILE A 203     128.608 135.766 113.454  1.00 47.96           C  
ATOM   1538  O   ILE A 203     129.322 136.259 114.336  1.00 47.96           O  
ATOM   1539  CB  ILE A 203     126.101 136.120 113.391  1.00 47.96           C  
ATOM   1540  CG1 ILE A 203     125.001 137.085 112.944  1.00 47.96           C  
ATOM   1541  CG2 ILE A 203     126.151 136.049 114.902  1.00 47.96           C  
ATOM   1542  CD1 ILE A 203     123.665 136.422 112.700  1.00 47.96           C  
ATOM   1543  N   ILE A 204     128.803 134.528 112.997  1.00 48.67           N  
ATOM   1544  CA  ILE A 204     129.862 133.681 113.533  1.00 48.67           C  
ATOM   1545  C   ILE A 204     131.230 134.266 113.217  1.00 48.67           C  
ATOM   1546  O   ILE A 204     132.120 134.279 114.073  1.00 48.67           O  
ATOM   1547  CB  ILE A 204     129.720 132.247 112.993  1.00 48.67           C  
ATOM   1548  CG1 ILE A 204     128.489 131.572 113.591  1.00 48.67           C  
ATOM   1549  CG2 ILE A 204     130.963 131.433 113.295  1.00 48.67           C  
ATOM   1550  CD1 ILE A 204     128.288 130.156 113.117  1.00 48.67           C  
ATOM   1551  N   LEU A 205     131.428 134.752 111.988  1.00 50.11           N  
ATOM   1552  CA  LEU A 205     132.717 135.335 111.635  1.00 50.11           C  
ATOM   1553  C   LEU A 205     133.010 136.573 112.470  1.00 50.11           C  
ATOM   1554  O   LEU A 205     134.127 136.739 112.971  1.00 50.11           O  
ATOM   1555  CB  LEU A 205     132.750 135.668 110.145  1.00 50.11           C  
ATOM   1556  CG  LEU A 205     133.563 134.706 109.280  1.00 50.11           C  
ATOM   1557  CD1 LEU A 205     135.043 134.835 109.595  1.00 50.11           C  
ATOM   1558  CD2 LEU A 205     133.094 133.277 109.483  1.00 50.11           C  
ATOM   1559  N   PHE A 206     132.015 137.445 112.647  1.00 52.50           N  
ATOM   1560  CA  PHE A 206     132.213 138.644 113.452  1.00 52.50           C  
ATOM   1561  C   PHE A 206     132.534 138.285 114.897  1.00 52.50           C  
ATOM   1562  O   PHE A 206     133.464 138.839 115.495  1.00 52.50           O  
ATOM   1563  CB  PHE A 206     130.966 139.526 113.375  1.00 52.50           C  
ATOM   1564  CG  PHE A 206     131.054 140.781 114.192  1.00 52.50           C  
ATOM   1565  CD1 PHE A 206     132.201 141.552 114.184  1.00 52.50           C  
ATOM   1566  CD2 PHE A 206     129.981 141.195 114.961  1.00 52.50           C  
ATOM   1567  CE1 PHE A 206     132.277 142.711 114.930  1.00 52.50           C  
ATOM   1568  CE2 PHE A 206     130.053 142.351 115.711  1.00 52.50           C  
ATOM   1569  CZ  PHE A 206     131.203 143.109 115.696  1.00 52.50           C  
ATOM   1570  N   CYS A 207     131.783 137.339 115.468  1.00 53.19           N  
ATOM   1571  CA  CYS A 207     132.013 136.948 116.854  1.00 53.19           C  
ATOM   1572  C   CYS A 207     133.387 136.316 117.031  1.00 53.19           C  
ATOM   1573  O   CYS A 207     134.106 136.639 117.982  1.00 53.19           O  
ATOM   1574  CB  CYS A 207     130.917 135.989 117.315  1.00 53.19           C  
ATOM   1575  SG  CYS A 207     129.302 136.765 117.536  1.00 53.19           S  
ATOM   1576  N   SER A 208     133.773 135.419 116.122  1.00 56.03           N  
ATOM   1577  CA  SER A 208     135.073 134.769 116.231  1.00 56.03           C  
ATOM   1578  C   SER A 208     136.207 135.771 116.067  1.00 56.03           C  
ATOM   1579  O   SER A 208     137.187 135.734 116.821  1.00 56.03           O  
ATOM   1580  CB  SER A 208     135.187 133.651 115.197  1.00 56.03           C  
ATOM   1581  OG  SER A 208     134.462 132.507 115.610  1.00 56.03           O  
ATOM   1582  N   ALA A 209     136.092 136.678 115.094  1.00 57.30           N  
ATOM   1583  CA  ALA A 209     137.135 137.676 114.899  1.00 57.30           C  
ATOM   1584  C   ALA A 209     137.261 138.580 116.115  1.00 57.30           C  
ATOM   1585  O   ALA A 209     138.375 138.888 116.552  1.00 57.30           O  
ATOM   1586  CB  ALA A 209     136.849 138.496 113.643  1.00 57.30           C  
ATOM   1587  N   ARG A 210     136.131 139.009 116.684  1.00 59.97           N  
ATOM   1588  CA  ARG A 210     136.191 139.862 117.865  1.00 59.97           C  
ATOM   1589  C   ARG A 210     136.774 139.118 119.058  1.00 59.97           C  
ATOM   1590  O   ARG A 210     137.547 139.691 119.831  1.00 59.97           O  
ATOM   1591  CB  ARG A 210     134.805 140.411 118.194  1.00 59.97           C  
ATOM   1592  CG  ARG A 210     134.421 141.627 117.372  1.00 59.97           C  
ATOM   1593  CD  ARG A 210     135.576 142.609 117.260  1.00 59.97           C  
ATOM   1594  NE  ARG A 210     135.905 143.220 118.542  1.00 59.97           N  
ATOM   1595  CZ  ARG A 210     135.308 144.297 119.036  1.00 59.97           C  
ATOM   1596  NH1 ARG A 210     134.343 144.915 118.376  1.00 59.97           N  
ATOM   1597  NH2 ARG A 210     135.690 144.764 120.221  1.00 59.97           N  
ATOM   1598  N   ILE A 211     136.421 137.841 119.225  1.00 55.12           N  
ATOM   1599  CA  ILE A 211     136.978 137.057 120.325  1.00 55.12           C  
ATOM   1600  C   ILE A 211     138.490 136.953 120.184  1.00 55.12           C  
ATOM   1601  O   ILE A 211     139.239 137.184 121.142  1.00 55.12           O  
ATOM   1602  CB  ILE A 211     136.322 135.666 120.380  1.00 55.12           C  
ATOM   1603  CG1 ILE A 211     134.898 135.764 120.923  1.00 55.12           C  
ATOM   1604  CG2 ILE A 211     137.144 134.720 121.234  1.00 55.12           C  
ATOM   1605  CD1 ILE A 211     134.054 134.552 120.622  1.00 55.12           C  
ATOM   1606  N   ILE A 212     138.962 136.618 118.980  1.00 57.83           N  
ATOM   1607  CA  ILE A 212     140.399 136.481 118.756  1.00 57.83           C  
ATOM   1608  C   ILE A 212     141.102 137.808 119.012  1.00 57.83           C  
ATOM   1609  O   ILE A 212     142.124 137.868 119.708  1.00 57.83           O  
ATOM   1610  CB  ILE A 212     140.675 135.965 117.333  1.00 57.83           C  
ATOM   1611  CG1 ILE A 212     140.046 134.588 117.125  1.00 57.83           C  
ATOM   1612  CG2 ILE A 212     142.169 135.914 117.065  1.00 57.83           C  
ATOM   1613  CD1 ILE A 212     140.621 133.519 118.006  1.00 57.83           C  
ATOM   1614  N   TRP A 213     140.554 138.894 118.460  1.00 67.21           N  
ATOM   1615  CA  TRP A 213     141.192 140.197 118.595  1.00 67.21           C  
ATOM   1616  C   TRP A 213     141.242 140.644 120.050  1.00 67.21           C  
ATOM   1617  O   TRP A 213     142.272 141.140 120.514  1.00 67.21           O  
ATOM   1618  CB  TRP A 213     140.458 141.230 117.741  1.00 67.21           C  
ATOM   1619  CG  TRP A 213     141.228 142.495 117.535  1.00 67.21           C  
ATOM   1620  CD1 TRP A 213     142.514 142.608 117.093  1.00 67.21           C  
ATOM   1621  CD2 TRP A 213     140.761 143.830 117.759  1.00 67.21           C  
ATOM   1622  NE1 TRP A 213     142.877 143.931 117.030  1.00 67.21           N  
ATOM   1623  CE2 TRP A 213     141.818 144.702 117.433  1.00 67.21           C  
ATOM   1624  CE3 TRP A 213     139.552 144.372 118.204  1.00 67.21           C  
ATOM   1625  CZ2 TRP A 213     141.703 146.086 117.539  1.00 67.21           C  
ATOM   1626  CZ3 TRP A 213     139.440 145.746 118.307  1.00 67.21           C  
ATOM   1627  CH2 TRP A 213     140.509 146.587 117.976  1.00 67.21           C  
ATOM   1628  N   SER A 214     140.144 140.467 120.788  1.00 64.39           N  
ATOM   1629  CA  SER A 214     140.113 140.884 122.185  1.00 64.39           C  
ATOM   1630  C   SER A 214     141.054 140.044 123.039  1.00 64.39           C  
ATOM   1631  O   SER A 214     141.774 140.583 123.889  1.00 64.39           O  
ATOM   1632  CB  SER A 214     138.686 140.802 122.720  1.00 64.39           C  
ATOM   1633  OG  SER A 214     138.050 139.621 122.268  1.00 64.39           O  
ATOM   1634  N   LEU A 215     141.066 138.725 122.829  1.00 61.65           N  
ATOM   1635  CA  LEU A 215     141.951 137.868 123.609  1.00 61.65           C  
ATOM   1636  C   LEU A 215     143.413 138.196 123.340  1.00 61.65           C  
ATOM   1637  O   LEU A 215     144.234 138.208 124.265  1.00 61.65           O  
ATOM   1638  CB  LEU A 215     141.662 136.399 123.305  1.00 61.65           C  
ATOM   1639  CG  LEU A 215     140.439 135.813 124.012  1.00 61.65           C  
ATOM   1640  CD1 LEU A 215     140.076 134.461 123.427  1.00 61.65           C  
ATOM   1641  CD2 LEU A 215     140.685 135.705 125.506  1.00 61.65           C  
ATOM   1642  N   ARG A 216     143.762 138.467 122.080  1.00 66.74           N  
ATOM   1643  CA  ARG A 216     145.146 138.805 121.770  1.00 66.74           C  
ATOM   1644  C   ARG A 216     145.510 140.204 122.254  1.00 66.74           C  
ATOM   1645  O   ARG A 216     146.651 140.435 122.668  1.00 66.74           O  
ATOM   1646  CB  ARG A 216     145.394 138.672 120.268  1.00 66.74           C  
ATOM   1647  CG  ARG A 216     145.589 137.235 119.810  1.00 66.74           C  
ATOM   1648  CD  ARG A 216     146.282 137.161 118.460  1.00 66.74           C  
ATOM   1649  NE  ARG A 216     147.244 136.067 118.405  1.00 66.74           N  
ATOM   1650  CZ  ARG A 216     146.923 134.791 118.240  1.00 66.74           C  
ATOM   1651  NH1 ARG A 216     145.665 134.408 118.100  1.00 66.74           N  
ATOM   1652  NH2 ARG A 216     147.888 133.877 118.216  1.00 66.74           N  
ATOM   1653  N   GLN A 217     144.562 141.145 122.217  1.00 72.64           N  
ATOM   1654  CA  GLN A 217     144.860 142.519 122.603  1.00 72.64           C  
ATOM   1655  C   GLN A 217     144.989 142.660 124.114  1.00 72.64           C  
ATOM   1656  O   GLN A 217     145.854 143.396 124.603  1.00 72.64           O  
ATOM   1657  CB  GLN A 217     143.779 143.455 122.062  1.00 72.64           C  
ATOM   1658  CG  GLN A 217     143.758 144.832 122.703  1.00 72.64           C  
ATOM   1659  CD  GLN A 217     144.616 145.833 121.956  1.00 72.64           C  
ATOM   1660  OE1 GLN A 217     144.967 145.622 120.795  1.00 72.64           O  
ATOM   1661  NE2 GLN A 217     144.961 146.930 122.620  1.00 72.64           N  
ATOM   1662  N   ARG A 218     144.149 141.959 124.872  1.00 70.42           N  
ATOM   1663  CA  ARG A 218     144.178 142.061 126.325  1.00 70.42           C  
ATOM   1664  C   ARG A 218     145.331 141.283 126.950  1.00 70.42           C  
ATOM   1665  O   ARG A 218     145.334 141.087 128.170  1.00 70.42           O  
ATOM   1666  CB  ARG A 218     142.845 141.585 126.911  1.00 70.42           C  
ATOM   1667  CG  ARG A 218     142.420 142.335 128.164  1.00 70.42           C  
ATOM   1668  CD  ARG A 218     141.217 141.687 128.824  1.00 70.42           C  
ATOM   1669  NE  ARG A 218     140.149 141.402 127.874  1.00 70.42           N  
ATOM   1670  CZ  ARG A 218     139.357 142.319 127.336  1.00 70.42           C  
ATOM   1671  NH1 ARG A 218     139.484 143.603 127.631  1.00 70.42           N  
ATOM   1672  NH2 ARG A 218     138.410 141.939 126.484  1.00 70.42           N  
ATOM   1673  N   GLN A 219     146.300 140.845 126.144  1.00 77.03           N  
ATOM   1674  CA  GLN A 219     147.463 140.097 126.618  1.00 77.03           C  
ATOM   1675  C   GLN A 219     147.019 138.853 127.391  1.00 77.03           C  
ATOM   1676  O   GLN A 219     147.226 138.718 128.599  1.00 77.03           O  
ATOM   1677  CB  GLN A 219     148.385 140.993 127.457  1.00 77.03           C  
ATOM   1678  CG  GLN A 219     149.680 140.332 127.922  1.00 77.03           C  
ATOM   1679  CD  GLN A 219     150.839 140.591 126.981  1.00 77.03           C  
ATOM   1680  OE1 GLN A 219     150.811 141.530 126.186  1.00 77.03           O  
ATOM   1681  NE2 GLN A 219     151.870 139.758 127.068  1.00 77.03           N  
ATOM   1682  N   MET A 220     146.361 137.949 126.666  1.00 79.71           N  
ATOM   1683  CA  MET A 220     145.901 136.694 127.234  1.00 79.71           C  
ATOM   1684  C   MET A 220     146.472 135.462 126.552  1.00 79.71           C  
ATOM   1685  O   MET A 220     146.295 134.358 127.075  1.00 79.71           O  
ATOM   1686  CB  MET A 220     144.367 136.614 127.200  1.00 79.71           C  
ATOM   1687  CG  MET A 220     143.748 136.208 128.528  1.00 79.71           C  
ATOM   1688  SD  MET A 220     142.074 136.829 128.758  1.00 79.71           S  
ATOM   1689  CE  MET A 220     142.412 138.378 129.586  1.00 79.71           C  
ATOM   1690  N   ASP A 221     147.170 135.614 125.424  1.00 80.90           N  
ATOM   1691  CA  ASP A 221     147.699 134.462 124.702  1.00 80.90           C  
ATOM   1692  C   ASP A 221     148.791 133.728 125.471  1.00 80.90           C  
ATOM   1693  O   ASP A 221     149.168 132.622 125.068  1.00 80.90           O  
ATOM   1694  CB  ASP A 221     148.237 134.901 123.339  1.00 80.90           C  
ATOM   1695  CG  ASP A 221     148.885 136.269 123.382  1.00 80.90           C  
ATOM   1696  OD1 ASP A 221     148.882 136.895 124.462  1.00 80.90           O  
ATOM   1697  OD2 ASP A 221     149.400 136.717 122.336  1.00 80.90           O  
ATOM   1698  N   ARG A 222     149.308 134.312 126.553  1.00 81.37           N  
ATOM   1699  CA  ARG A 222     150.305 133.622 127.365  1.00 81.37           C  
ATOM   1700  C   ARG A 222     149.719 132.376 128.019  1.00 81.37           C  
ATOM   1701  O   ARG A 222     150.403 131.352 128.141  1.00 81.37           O  
ATOM   1702  CB  ARG A 222     150.869 134.577 128.418  1.00 81.37           C  
ATOM   1703  CG  ARG A 222     151.384 133.907 129.686  1.00 81.37           C  
ATOM   1704  CD  ARG A 222     152.703 133.186 129.444  1.00 81.37           C  
ATOM   1705  NE  ARG A 222     152.512 131.750 129.281  1.00 81.37           N  
ATOM   1706  CZ  ARG A 222     153.482 130.890 129.003  1.00 81.37           C  
ATOM   1707  NH1 ARG A 222     154.735 131.288 128.848  1.00 81.37           N  
ATOM   1708  NH2 ARG A 222     153.189 129.600 128.875  1.00 81.37           N  
ATOM   1709  N   HIS A 223     148.456 132.438 128.437  1.00 77.16           N  
ATOM   1710  CA  HIS A 223     147.845 131.325 129.150  1.00 77.16           C  
ATOM   1711  C   HIS A 223     147.768 130.089 128.260  1.00 77.16           C  
ATOM   1712  O   HIS A 223     147.671 130.180 127.034  1.00 77.16           O  
ATOM   1713  CB  HIS A 223     146.450 131.710 129.643  1.00 77.16           C  
ATOM   1714  CG  HIS A 223     146.444 132.839 130.627  1.00 77.16           C  
ATOM   1715  ND1 HIS A 223     145.329 133.181 131.361  1.00 77.16           N  
ATOM   1716  CD2 HIS A 223     147.418 133.705 130.998  1.00 77.16           C  
ATOM   1717  CE1 HIS A 223     145.615 134.208 132.141  1.00 77.16           C  
ATOM   1718  NE2 HIS A 223     146.876 134.545 131.940  1.00 77.16           N  
ATOM   1719  N   ALA A 224     147.819 128.918 128.897  1.00 74.87           N  
ATOM   1720  CA  ALA A 224     147.903 127.662 128.158  1.00 74.87           C  
ATOM   1721  C   ALA A 224     146.548 127.242 127.599  1.00 74.87           C  
ATOM   1722  O   ALA A 224     146.393 127.068 126.385  1.00 74.87           O  
ATOM   1723  CB  ALA A 224     148.476 126.565 129.059  1.00 74.87           C  
ATOM   1724  N   LYS A 225     145.554 127.068 128.474  1.00 74.46           N  
ATOM   1725  CA  LYS A 225     144.256 126.568 128.027  1.00 74.46           C  
ATOM   1726  C   LYS A 225     143.549 127.575 127.126  1.00 74.46           C  
ATOM   1727  O   LYS A 225     142.694 127.200 126.314  1.00 74.46           O  
ATOM   1728  CB  LYS A 225     143.383 126.220 129.231  1.00 74.46           C  
ATOM   1729  CG  LYS A 225     144.129 126.177 130.553  1.00 74.46           C  
ATOM   1730  CD  LYS A 225     143.204 125.781 131.692  1.00 74.46           C  
ATOM   1731  N   ILE A 226     143.886 128.859 127.256  1.00 72.88           N  
ATOM   1732  CA  ILE A 226     143.263 129.860 126.396  1.00 72.88           C  
ATOM   1733  C   ILE A 226     143.705 129.670 124.954  1.00 72.88           C  
ATOM   1734  O   ILE A 226     142.949 129.963 124.022  1.00 72.88           O  
ATOM   1735  CB  ILE A 226     143.565 131.284 126.911  1.00 72.88           C  
ATOM   1736  CG1 ILE A 226     142.332 132.172 126.754  1.00 72.88           C  
ATOM   1737  CG2 ILE A 226     144.721 131.901 126.158  1.00 72.88           C  
ATOM   1738  CD1 ILE A 226     141.239 131.874 127.751  1.00 72.88           C  
ATOM   1739  N   LYS A 227     144.926 129.171 124.740  1.00 72.33           N  
ATOM   1740  CA  LYS A 227     145.364 128.861 123.384  1.00 72.33           C  
ATOM   1741  C   LYS A 227     144.529 127.734 122.790  1.00 72.33           C  
ATOM   1742  O   LYS A 227     144.153 127.783 121.612  1.00 72.33           O  
ATOM   1743  CB  LYS A 227     146.848 128.497 123.380  1.00 72.33           C  
ATOM   1744  CG  LYS A 227     147.427 128.241 121.998  1.00 72.33           C  
ATOM   1745  CD  LYS A 227     146.985 129.296 121.000  1.00 72.33           C  
ATOM   1746  CE  LYS A 227     147.694 129.121 119.668  1.00 72.33           C  
ATOM   1747  NZ  LYS A 227     146.909 128.272 118.730  1.00 72.33           N  
ATOM   1748  N   ARG A 228     144.228 126.714 123.595  1.00 71.50           N  
ATOM   1749  CA  ARG A 228     143.336 125.654 123.142  1.00 71.50           C  
ATOM   1750  C   ARG A 228     141.948 126.203 122.843  1.00 71.50           C  
ATOM   1751  O   ARG A 228     141.318 125.812 121.856  1.00 71.50           O  
ATOM   1752  CB  ARG A 228     143.271 124.542 124.190  1.00 71.50           C  
ATOM   1753  CG  ARG A 228     141.934 123.820 124.268  1.00 71.50           C  
ATOM   1754  CD  ARG A 228     142.019 122.597 125.164  1.00 71.50           C  
ATOM   1755  NE  ARG A 228     143.028 121.653 124.699  1.00 71.50           N  
ATOM   1756  CZ  ARG A 228     142.761 120.443 124.228  1.00 71.50           C  
ATOM   1757  NH1 ARG A 228     141.520 119.991 124.147  1.00 71.50           N  
ATOM   1758  NH2 ARG A 228     143.764 119.667 123.826  1.00 71.50           N  
ATOM   1759  N   ALA A 229     141.458 127.118 123.679  1.00 68.84           N  
ATOM   1760  CA  ALA A 229     140.153 127.723 123.422  1.00 68.84           C  
ATOM   1761  C   ALA A 229     140.148 128.488 122.103  1.00 68.84           C  
ATOM   1762  O   ALA A 229     139.190 128.398 121.323  1.00 68.84           O  
ATOM   1763  CB  ALA A 229     139.765 128.644 124.577  1.00 68.84           C  
ATOM   1764  N   ILE A 230     141.212 129.249 121.840  1.00 66.49           N  
ATOM   1765  CA  ILE A 230     141.309 130.008 120.596  1.00 66.49           C  
ATOM   1766  C   ILE A 230     141.345 129.065 119.401  1.00 66.49           C  
ATOM   1767  O   ILE A 230     140.627 129.256 118.411  1.00 66.49           O  
ATOM   1768  CB  ILE A 230     142.541 130.931 120.626  1.00 66.49           C  
ATOM   1769  CG1 ILE A 230     142.201 132.260 121.299  1.00 66.49           C  
ATOM   1770  CG2 ILE A 230     143.079 131.169 119.226  1.00 66.49           C  
ATOM   1771  CD1 ILE A 230     143.387 133.185 121.447  1.00 66.49           C  
ATOM   1772  N   THR A 231     142.173 128.021 119.476  1.00 70.79           N  
ATOM   1773  CA  THR A 231     142.258 127.108 118.344  1.00 70.79           C  
ATOM   1774  C   THR A 231     140.952 126.348 118.146  1.00 70.79           C  
ATOM   1775  O   THR A 231     140.585 126.051 117.006  1.00 70.79           O  
ATOM   1776  CB  THR A 231     143.444 126.150 118.504  1.00 70.79           C  
ATOM   1777  OG1 THR A 231     143.810 125.628 117.221  1.00 70.79           O  
ATOM   1778  CG2 THR A 231     143.115 124.990 119.430  1.00 70.79           C  
ATOM   1779  N   PHE A 232     140.209 126.079 119.225  1.00 69.70           N  
ATOM   1780  CA  PHE A 232     138.943 125.368 119.087  1.00 69.70           C  
ATOM   1781  C   PHE A 232     137.845 126.249 118.504  1.00 69.70           C  
ATOM   1782  O   PHE A 232     137.067 125.784 117.665  1.00 69.70           O  
ATOM   1783  CB  PHE A 232     138.517 124.767 120.425  1.00 69.70           C  
ATOM   1784  CG  PHE A 232     139.040 123.374 120.651  1.00 69.70           C  
ATOM   1785  CD1 PHE A 232     140.381 123.146 120.901  1.00 69.70           C  
ATOM   1786  CD2 PHE A 232     138.185 122.288 120.598  1.00 69.70           C  
ATOM   1787  CE1 PHE A 232     140.855 121.863 121.101  1.00 69.70           C  
ATOM   1788  CE2 PHE A 232     138.652 121.005 120.796  1.00 69.70           C  
ATOM   1789  CZ  PHE A 232     139.988 120.792 121.048  1.00 69.70           C  
ATOM   1790  N   ILE A 233     137.761 127.518 118.907  1.00 64.10           N  
ATOM   1791  CA  ILE A 233     136.786 128.389 118.254  1.00 64.10           C  
ATOM   1792  C   ILE A 233     137.161 128.590 116.787  1.00 64.10           C  
ATOM   1793  O   ILE A 233     136.289 128.643 115.905  1.00 64.10           O  
ATOM   1794  CB  ILE A 233     136.634 129.724 119.010  1.00 64.10           C  
ATOM   1795  CG1 ILE A 233     135.593 130.611 118.327  1.00 64.10           C  
ATOM   1796  CG2 ILE A 233     137.944 130.462 119.107  1.00 64.10           C  
ATOM   1797  CD1 ILE A 233     134.194 130.046 118.363  1.00 64.10           C  
ATOM   1798  N   MET A 234     138.465 128.655 116.494  1.00 65.52           N  
ATOM   1799  CA  MET A 234     138.902 128.786 115.109  1.00 65.52           C  
ATOM   1800  C   MET A 234     138.498 127.570 114.282  1.00 65.52           C  
ATOM   1801  O   MET A 234     137.990 127.711 113.163  1.00 65.52           O  
ATOM   1802  CB  MET A 234     140.414 129.001 115.056  1.00 65.52           C  
ATOM   1803  CG  MET A 234     140.827 130.364 114.528  1.00 65.52           C  
ATOM   1804  SD  MET A 234     142.613 130.611 114.556  1.00 65.52           S  
ATOM   1805  CE  MET A 234     143.137 129.461 113.289  1.00 65.52           C  
ATOM   1806  N   VAL A 235     138.712 126.360 114.813  1.00 63.87           N  
ATOM   1807  CA  VAL A 235     138.357 125.180 114.029  1.00 63.87           C  
ATOM   1808  C   VAL A 235     136.842 125.049 113.943  1.00 63.87           C  
ATOM   1809  O   VAL A 235     136.322 124.519 112.961  1.00 63.87           O  
ATOM   1810  CB  VAL A 235     139.005 123.893 114.584  1.00 63.87           C  
ATOM   1811  CG1 VAL A 235     138.824 123.778 116.063  1.00 63.87           C  
ATOM   1812  CG2 VAL A 235     138.472 122.649 113.880  1.00 63.87           C  
ATOM   1813  N   VAL A 236     136.106 125.540 114.943  1.00 61.02           N  
ATOM   1814  CA  VAL A 236     134.648 125.555 114.842  1.00 61.02           C  
ATOM   1815  C   VAL A 236     134.212 126.400 113.652  1.00 61.02           C  
ATOM   1816  O   VAL A 236     133.399 125.970 112.821  1.00 61.02           O  
ATOM   1817  CB  VAL A 236     134.022 126.063 116.153  1.00 61.02           C  
ATOM   1818  CG1 VAL A 236     132.682 126.730 115.885  1.00 61.02           C  
ATOM   1819  CG2 VAL A 236     133.851 124.924 117.131  1.00 61.02           C  
ATOM   1820  N   ALA A 237     134.764 127.611 113.540  1.00 60.79           N  
ATOM   1821  CA  ALA A 237     134.428 128.459 112.400  1.00 60.79           C  
ATOM   1822  C   ALA A 237     134.842 127.805 111.085  1.00 60.79           C  
ATOM   1823  O   ALA A 237     134.075 127.802 110.110  1.00 60.79           O  
ATOM   1824  CB  ALA A 237     135.089 129.828 112.550  1.00 60.79           C  
ATOM   1825  N   ILE A 238     136.045 127.227 111.049  1.00 59.72           N  
ATOM   1826  CA  ILE A 238     136.555 126.632 109.818  1.00 59.72           C  
ATOM   1827  C   ILE A 238     135.695 125.450 109.392  1.00 59.72           C  
ATOM   1828  O   ILE A 238     135.384 125.291 108.208  1.00 59.72           O  
ATOM   1829  CB  ILE A 238     138.030 126.226 109.991  1.00 59.72           C  
ATOM   1830  CG1 ILE A 238     138.917 127.467 110.097  1.00 59.72           C  
ATOM   1831  CG2 ILE A 238     138.486 125.353 108.833  1.00 59.72           C  
ATOM   1832  CD1 ILE A 238     140.236 127.212 110.790  1.00 59.72           C  
ATOM   1833  N   VAL A 239     135.307 124.597 110.342  1.00 58.04           N  
ATOM   1834  CA  VAL A 239     134.516 123.420 110.002  1.00 58.04           C  
ATOM   1835  C   VAL A 239     133.109 123.824 109.585  1.00 58.04           C  
ATOM   1836  O   VAL A 239     132.525 123.214 108.684  1.00 58.04           O  
ATOM   1837  CB  VAL A 239     134.510 122.404 111.161  1.00 58.04           C  
ATOM   1838  CG1 VAL A 239     133.688 122.896 112.337  1.00 58.04           C  
ATOM   1839  CG2 VAL A 239     133.982 121.070 110.677  1.00 58.04           C  
ATOM   1840  N   PHE A 240     132.542 124.858 110.215  1.00 54.86           N  
ATOM   1841  CA  PHE A 240     131.254 125.362 109.751  1.00 54.86           C  
ATOM   1842  C   PHE A 240     131.345 125.814 108.300  1.00 54.86           C  
ATOM   1843  O   PHE A 240     130.513 125.437 107.462  1.00 54.86           O  
ATOM   1844  CB  PHE A 240     130.782 126.508 110.647  1.00 54.86           C  
ATOM   1845  CG  PHE A 240     129.493 127.139 110.197  1.00 54.86           C  
ATOM   1846  CD1 PHE A 240     128.276 126.602 110.573  1.00 54.86           C  
ATOM   1847  CD2 PHE A 240     129.500 128.273 109.405  1.00 54.86           C  
ATOM   1848  CE1 PHE A 240     127.092 127.179 110.162  1.00 54.86           C  
ATOM   1849  CE2 PHE A 240     128.318 128.852 108.991  1.00 54.86           C  
ATOM   1850  CZ  PHE A 240     127.113 128.305 109.371  1.00 54.86           C  
ATOM   1851  N   VAL A 241     132.374 126.604 107.981  1.00 54.34           N  
ATOM   1852  CA  VAL A 241     132.532 127.097 106.615  1.00 54.34           C  
ATOM   1853  C   VAL A 241     132.735 125.937 105.648  1.00 54.34           C  
ATOM   1854  O   VAL A 241     132.114 125.886 104.582  1.00 54.34           O  
ATOM   1855  CB  VAL A 241     133.693 128.106 106.544  1.00 54.34           C  
ATOM   1856  CG1 VAL A 241     134.211 128.225 105.121  1.00 54.34           C  
ATOM   1857  CG2 VAL A 241     133.247 129.459 107.068  1.00 54.34           C  
ATOM   1858  N   ILE A 242     133.590 124.981 106.012  1.00 57.50           N  
ATOM   1859  CA  ILE A 242     133.903 123.870 105.117  1.00 57.50           C  
ATOM   1860  C   ILE A 242     132.669 123.014 104.871  1.00 57.50           C  
ATOM   1861  O   ILE A 242     132.421 122.564 103.746  1.00 57.50           O  
ATOM   1862  CB  ILE A 242     135.068 123.040 105.691  1.00 57.50           C  
ATOM   1863  CG1 ILE A 242     136.408 123.703 105.364  1.00 57.50           C  
ATOM   1864  CG2 ILE A 242     135.034 121.615 105.161  1.00 57.50           C  
ATOM   1865  CD1 ILE A 242     136.593 124.024 103.896  1.00 57.50           C  
ATOM   1866  N   CYS A 243     131.872 122.777 105.913  1.00 57.60           N  
ATOM   1867  CA  CYS A 243     130.709 121.915 105.775  1.00 57.60           C  
ATOM   1868  C   CYS A 243     129.565 122.594 105.035  1.00 57.60           C  
ATOM   1869  O   CYS A 243     128.797 121.914 104.346  1.00 57.60           O  
ATOM   1870  CB  CYS A 243     130.237 121.450 107.152  1.00 57.60           C  
ATOM   1871  SG  CYS A 243     130.785 119.787 107.597  1.00 57.60           S  
ATOM   1872  N   PHE A 244     129.424 123.914 105.154  1.00 55.39           N  
ATOM   1873  CA  PHE A 244     128.279 124.593 104.560  1.00 55.39           C  
ATOM   1874  C   PHE A 244     128.611 125.378 103.296  1.00 55.39           C  
ATOM   1875  O   PHE A 244     127.706 125.972 102.704  1.00 55.39           O  
ATOM   1876  CB  PHE A 244     127.636 125.524 105.591  1.00 55.39           C  
ATOM   1877  CG  PHE A 244     126.796 124.809 106.606  1.00 55.39           C  
ATOM   1878  CD1 PHE A 244     125.501 124.428 106.307  1.00 55.39           C  
ATOM   1879  CD2 PHE A 244     127.303 124.512 107.858  1.00 55.39           C  
ATOM   1880  CE1 PHE A 244     124.728 123.766 107.237  1.00 55.39           C  
ATOM   1881  CE2 PHE A 244     126.533 123.851 108.793  1.00 55.39           C  
ATOM   1882  CZ  PHE A 244     125.245 123.478 108.482  1.00 55.39           C  
ATOM   1883  N   LEU A 245     129.870 125.398 102.862  1.00 55.53           N  
ATOM   1884  CA  LEU A 245     130.234 126.180 101.686  1.00 55.53           C  
ATOM   1885  C   LEU A 245     129.929 125.479 100.362  1.00 55.53           C  
ATOM   1886  O   LEU A 245     129.379 126.122  99.461  1.00 55.53           O  
ATOM   1887  CB  LEU A 245     131.716 126.560 101.744  1.00 55.53           C  
ATOM   1888  CG  LEU A 245     132.163 127.724 100.858  1.00 55.53           C  
ATOM   1889  CD1 LEU A 245     131.048 128.744 100.695  1.00 55.53           C  
ATOM   1890  CD2 LEU A 245     133.413 128.379 101.423  1.00 55.53           C  
ATOM   1891  N   PRO A 246     130.296 124.203 100.170  1.00 54.41           N  
ATOM   1892  CA  PRO A 246     130.044 123.584  98.856  1.00 54.41           C  
ATOM   1893  C   PRO A 246     128.580 123.572  98.456  1.00 54.41           C  
ATOM   1894  O   PRO A 246     128.263 123.783  97.278  1.00 54.41           O  
ATOM   1895  CB  PRO A 246     130.598 122.165  99.030  1.00 54.41           C  
ATOM   1896  CG  PRO A 246     131.615 122.293 100.090  1.00 54.41           C  
ATOM   1897  CD  PRO A 246     131.040 123.284 101.049  1.00 54.41           C  
ATOM   1898  N   SER A 247     127.672 123.349  99.408  1.00 57.98           N  
ATOM   1899  CA  SER A 247     126.251 123.311  99.079  1.00 57.98           C  
ATOM   1900  C   SER A 247     125.776 124.658  98.548  1.00 57.98           C  
ATOM   1901  O   SER A 247     125.148 124.734  97.485  1.00 57.98           O  
ATOM   1902  CB  SER A 247     125.442 122.898 100.307  1.00 57.98           C  
ATOM   1903  OG  SER A 247     126.019 123.416 101.493  1.00 57.98           O  
ATOM   1904  N   VAL A 248     126.082 125.738  99.269  1.00 55.00           N  
ATOM   1905  CA  VAL A 248     125.647 127.057  98.828  1.00 55.00           C  
ATOM   1906  C   VAL A 248     126.363 127.468  97.546  1.00 55.00           C  
ATOM   1907  O   VAL A 248     125.782 128.159  96.703  1.00 55.00           O  
ATOM   1908  CB  VAL A 248     125.840 128.094  99.951  1.00 55.00           C  
ATOM   1909  CG1 VAL A 248     127.308 128.386 100.170  1.00 55.00           C  
ATOM   1910  CG2 VAL A 248     125.086 129.372  99.629  1.00 55.00           C  
ATOM   1911  N   VAL A 249     127.619 127.055  97.367  1.00 52.41           N  
ATOM   1912  CA  VAL A 249     128.344 127.410  96.150  1.00 52.41           C  
ATOM   1913  C   VAL A 249     127.705 126.744  94.940  1.00 52.41           C  
ATOM   1914  O   VAL A 249     127.490 127.381  93.902  1.00 52.41           O  
ATOM   1915  CB  VAL A 249     129.832 127.041  96.280  1.00 52.41           C  
ATOM   1916  CG1 VAL A 249     130.478 126.956  94.910  1.00 52.41           C  
ATOM   1917  CG2 VAL A 249     130.553 128.063  97.136  1.00 52.41           C  
ATOM   1918  N   VAL A 250     127.378 125.456  95.058  1.00 53.94           N  
ATOM   1919  CA  VAL A 250     126.713 124.773  93.956  1.00 53.94           C  
ATOM   1920  C   VAL A 250     125.319 125.345  93.734  1.00 53.94           C  
ATOM   1921  O   VAL A 250     124.852 125.430  92.593  1.00 53.94           O  
ATOM   1922  CB  VAL A 250     126.675 123.255  94.208  1.00 53.94           C  
ATOM   1923  CG1 VAL A 250     125.909 122.554  93.104  1.00 53.94           C  
ATOM   1924  CG2 VAL A 250     128.086 122.706  94.297  1.00 53.94           C  
ATOM   1925  N   ARG A 251     124.632 125.754  94.804  1.00 62.71           N  
ATOM   1926  CA  ARG A 251     123.317 126.367  94.638  1.00 62.71           C  
ATOM   1927  C   ARG A 251     123.413 127.686  93.879  1.00 62.71           C  
ATOM   1928  O   ARG A 251     122.593 127.965  92.998  1.00 62.71           O  
ATOM   1929  CB  ARG A 251     122.657 126.576  96.000  1.00 62.71           C  
ATOM   1930  CG  ARG A 251     121.161 126.808  95.920  1.00 62.71           C  
ATOM   1931  CD  ARG A 251     120.409 125.490  95.961  1.00 62.71           C  
ATOM   1932  NE  ARG A 251     119.045 125.621  95.465  1.00 62.71           N  
ATOM   1933  CZ  ARG A 251     118.490 124.806  94.580  1.00 62.71           C  
ATOM   1934  NH1 ARG A 251     119.155 123.783  94.070  1.00 62.71           N  
ATOM   1935  NH2 ARG A 251     117.234 125.021  94.199  1.00 62.71           N  
ATOM   1936  N   ILE A 252     124.410 128.509  94.201  1.00 55.65           N  
ATOM   1937  CA  ILE A 252     124.585 129.766  93.481  1.00 55.65           C  
ATOM   1938  C   ILE A 252     124.974 129.499  92.032  1.00 55.65           C  
ATOM   1939  O   ILE A 252     124.517 130.191  91.114  1.00 55.65           O  
ATOM   1940  CB  ILE A 252     125.620 130.652  94.197  1.00 55.65           C  
ATOM   1941  CG1 ILE A 252     125.099 131.069  95.572  1.00 55.65           C  
ATOM   1942  CG2 ILE A 252     125.940 131.881  93.367  1.00 55.65           C  
ATOM   1943  CD1 ILE A 252     126.190 131.407  96.559  1.00 55.65           C  
ATOM   1944  N   ARG A 253     125.818 128.491  91.801  1.00 61.65           N  
ATOM   1945  CA  ARG A 253     126.210 128.158  90.435  1.00 61.65           C  
ATOM   1946  C   ARG A 253     125.015 127.697  89.612  1.00 61.65           C  
ATOM   1947  O   ARG A 253     124.867 128.087  88.448  1.00 61.65           O  
ATOM   1948  CB  ARG A 253     127.299 127.088  90.447  1.00 61.65           C  
ATOM   1949  CG  ARG A 253     127.689 126.595  89.066  1.00 61.65           C  
ATOM   1950  CD  ARG A 253     128.476 127.649  88.307  1.00 61.65           C  
ATOM   1951  NE  ARG A 253     129.233 127.077  87.199  1.00 61.65           N  
ATOM   1952  CZ  ARG A 253     130.553 126.955  87.179  1.00 61.65           C  
ATOM   1953  NH1 ARG A 253     131.300 127.355  88.195  1.00 61.65           N  
ATOM   1954  NH2 ARG A 253     131.138 126.418  86.112  1.00 61.65           N  
ATOM   1955  N   ILE A 254     124.150 126.862  90.195  1.00 66.64           N  
ATOM   1956  CA  ILE A 254     122.978 126.406  89.457  1.00 66.64           C  
ATOM   1957  C   ILE A 254     121.981 127.546  89.282  1.00 66.64           C  
ATOM   1958  O   ILE A 254     121.282 127.610  88.268  1.00 66.64           O  
ATOM   1959  CB  ILE A 254     122.343 125.171  90.129  1.00 66.64           C  
ATOM   1960  CG1 ILE A 254     121.296 124.544  89.209  1.00 66.64           C  
ATOM   1961  CG2 ILE A 254     121.708 125.518  91.451  1.00 66.64           C  
ATOM   1962  CD1 ILE A 254     121.885 123.845  88.011  1.00 66.64           C  
ATOM   1963  N   PHE A 255     121.922 128.485  90.231  1.00 71.55           N  
ATOM   1964  CA  PHE A 255     121.108 129.681  90.028  1.00 71.55           C  
ATOM   1965  C   PHE A 255     121.608 130.498  88.844  1.00 71.55           C  
ATOM   1966  O   PHE A 255     120.811 130.991  88.037  1.00 71.55           O  
ATOM   1967  CB  PHE A 255     121.101 130.535  91.295  1.00 71.55           C  
ATOM   1968  CG  PHE A 255     119.993 130.198  92.248  1.00 71.55           C  
ATOM   1969  CD1 PHE A 255     119.204 129.080  92.046  1.00 71.55           C  
ATOM   1970  CD2 PHE A 255     119.739 131.004  93.343  1.00 71.55           C  
ATOM   1971  CE1 PHE A 255     118.184 128.772  92.920  1.00 71.55           C  
ATOM   1972  CE2 PHE A 255     118.720 130.700  94.220  1.00 71.55           C  
ATOM   1973  CZ  PHE A 255     117.942 129.583  94.007  1.00 71.55           C  
ATOM   1974  N   TRP A 256     122.927 130.664  88.733  1.00 68.70           N  
ATOM   1975  CA  TRP A 256     123.481 131.410  87.609  1.00 68.70           C  
ATOM   1976  C   TRP A 256     123.222 130.687  86.293  1.00 68.70           C  
ATOM   1977  O   TRP A 256     122.827 131.307  85.300  1.00 68.70           O  
ATOM   1978  CB  TRP A 256     124.976 131.643  87.809  1.00 68.70           C  
ATOM   1979  CG  TRP A 256     125.559 132.543  86.772  1.00 68.70           C  
ATOM   1980  CD1 TRP A 256     125.250 133.854  86.562  1.00 68.70           C  
ATOM   1981  CD2 TRP A 256     126.545 132.201  85.792  1.00 68.70           C  
ATOM   1982  NE1 TRP A 256     125.985 134.351  85.515  1.00 68.70           N  
ATOM   1983  CE2 TRP A 256     126.788 133.356  85.025  1.00 68.70           C  
ATOM   1984  CE3 TRP A 256     127.247 131.031  85.491  1.00 68.70           C  
ATOM   1985  CZ2 TRP A 256     127.703 133.375  83.976  1.00 68.70           C  
ATOM   1986  CZ3 TRP A 256     128.155 131.052  84.449  1.00 68.70           C  
ATOM   1987  CH2 TRP A 256     128.375 132.216  83.704  1.00 68.70           C  
ATOM   1988  N   LEU A 257     123.435 129.369  86.268  1.00 68.75           N  
ATOM   1989  CA  LEU A 257     123.121 128.588  85.076  1.00 68.75           C  
ATOM   1990  C   LEU A 257     121.628 128.559  84.788  1.00 68.75           C  
ATOM   1991  O   LEU A 257     121.228 128.204  83.676  1.00 68.75           O  
ATOM   1992  CB  LEU A 257     123.645 127.159  85.216  1.00 68.75           C  
ATOM   1993  CG  LEU A 257     125.041 126.863  84.660  1.00 68.75           C  
ATOM   1994  CD1 LEU A 257     125.081 127.110  83.160  1.00 68.75           C  
ATOM   1995  CD2 LEU A 257     126.112 127.673  85.372  1.00 68.75           C  
ATOM   1996  N   LEU A 258     120.801 128.905  85.773  1.00 74.82           N  
ATOM   1997  CA  LEU A 258     119.361 128.973  85.569  1.00 74.82           C  
ATOM   1998  C   LEU A 258     118.951 130.299  84.941  1.00 74.82           C  
ATOM   1999  O   LEU A 258     118.213 130.321  83.950  1.00 74.82           O  
ATOM   2000  CB  LEU A 258     118.648 128.763  86.905  1.00 74.82           C  
ATOM   2001  CG  LEU A 258     117.215 128.240  86.883  1.00 74.82           C  
ATOM   2002  CD1 LEU A 258     116.951 127.392  88.112  1.00 74.82           C  
ATOM   2003  CD2 LEU A 258     116.256 129.408  86.825  1.00 74.82           C  
ATOM   2004  N   HIS A 259     119.412 131.416  85.510  1.00 75.02           N  
ATOM   2005  CA  HIS A 259     119.027 132.721  84.980  1.00 75.02           C  
ATOM   2006  C   HIS A 259     119.557 132.916  83.565  1.00 75.02           C  
ATOM   2007  O   HIS A 259     118.799 133.249  82.647  1.00 75.02           O  
ATOM   2008  CB  HIS A 259     119.519 133.836  85.902  1.00 75.02           C  
ATOM   2009  CG  HIS A 259     118.550 134.969  86.040  1.00 75.02           C  
ATOM   2010  ND1 HIS A 259     117.789 135.427  84.986  1.00 75.02           N  
ATOM   2011  CD2 HIS A 259     118.213 135.731  87.107  1.00 75.02           C  
ATOM   2012  CE1 HIS A 259     117.028 136.425  85.397  1.00 75.02           C  
ATOM   2013  NE2 HIS A 259     117.266 136.629  86.680  1.00 75.02           N  
ATOM   2014  N   THR A 260     120.855 132.708  83.367  1.00 74.36           N  
ATOM   2015  CA  THR A 260     121.417 132.698  82.025  1.00 74.36           C  
ATOM   2016  C   THR A 260     121.071 131.375  81.360  1.00 74.36           C  
ATOM   2017  O   THR A 260     121.326 130.307  81.925  1.00 74.36           O  
ATOM   2018  CB  THR A 260     122.931 132.892  82.063  1.00 74.36           C  
ATOM   2019  OG1 THR A 260     123.572 131.616  82.181  1.00 74.36           O  
ATOM   2020  CG2 THR A 260     123.326 133.767  83.241  1.00 74.36           C  
ATOM   2021  N   SER A 261     120.492 131.448  80.164  1.00 82.45           N  
ATOM   2022  CA  SER A 261     119.906 130.282  79.490  1.00 82.45           C  
ATOM   2023  C   SER A 261     118.826 129.745  80.428  1.00 82.45           C  
ATOM   2024  O   SER A 261     117.967 130.525  80.868  1.00 82.45           O  
ATOM   2025  CB  SER A 261     120.998 129.293  79.096  1.00 82.45           C  
ATOM   2026  OG  SER A 261     120.450 128.027  78.774  1.00 82.45           O  
ATOM   2027  N   GLY A 262     118.825 128.467  80.763  1.00 82.42           N  
ATOM   2028  CA  GLY A 262     117.835 127.955  81.687  1.00 82.42           C  
ATOM   2029  C   GLY A 262     116.632 127.370  80.973  1.00 82.42           C  
ATOM   2030  O   GLY A 262     116.289 127.756  79.850  1.00 82.42           O  
ATOM   2031  N   THR A 263     115.972 126.420  81.641  1.00 89.17           N  
ATOM   2032  CA  THR A 263     114.833 125.668  81.099  1.00 89.17           C  
ATOM   2033  C   THR A 263     115.147 125.052  79.737  1.00 89.17           C  
ATOM   2034  O   THR A 263     114.238 124.715  78.972  1.00 89.17           O  
ATOM   2035  CB  THR A 263     113.560 126.524  81.016  1.00 89.17           C  
ATOM   2036  OG1 THR A 263     113.884 127.873  80.657  1.00 89.17           O  
ATOM   2037  CG2 THR A 263     112.833 126.522  82.352  1.00 89.17           C  
ATOM   2038  N   GLN A 264     116.429 124.898  79.429  1.00 89.84           N  
ATOM   2039  CA  GLN A 264     116.887 124.296  78.187  1.00 89.84           C  
ATOM   2040  C   GLN A 264     116.925 122.778  78.375  1.00 89.84           C  
ATOM   2041  O   GLN A 264     116.306 122.246  79.301  1.00 89.84           O  
ATOM   2042  CB  GLN A 264     118.239 124.901  77.789  1.00 89.84           C  
ATOM   2043  CG  GLN A 264     118.587 124.811  76.302  1.00 89.84           C  
ATOM   2044  CD  GLN A 264     117.798 125.782  75.436  1.00 89.84           C  
ATOM   2045  OE1 GLN A 264     116.602 125.994  75.639  1.00 89.84           O  
ATOM   2046  NE2 GLN A 264     118.473 126.378  74.461  1.00 89.84           N  
ATOM   2047  N   ASN A 265     117.626 122.067  77.489  1.00 91.52           N  
ATOM   2048  CA  ASN A 265     117.795 120.617  77.559  1.00 91.52           C  
ATOM   2049  C   ASN A 265     118.114 120.135  78.971  1.00 91.52           C  
ATOM   2050  O   ASN A 265     117.816 118.988  79.320  1.00 91.52           O  
ATOM   2051  CB  ASN A 265     118.901 120.173  76.600  1.00 91.52           C  
ATOM   2052  CG  ASN A 265     120.168 120.993  76.753  1.00 91.52           C  
ATOM   2053  OD1 ASN A 265     120.254 121.868  77.615  1.00 91.52           O  
ATOM   2054  ND2 ASN A 265     121.159 120.713  75.916  1.00 91.52           N  
ATOM   2055  N   CYS A 266     118.740 120.995  79.774  1.00 85.23           N  
ATOM   2056  CA  CYS A 266     118.997 120.792  81.197  1.00 85.23           C  
ATOM   2057  C   CYS A 266     120.031 119.710  81.470  1.00 85.23           C  
ATOM   2058  O   CYS A 266     120.261 119.368  82.636  1.00 85.23           O  
ATOM   2059  CB  CYS A 266     117.712 120.471  81.969  1.00 85.23           C  
ATOM   2060  N   GLU A 267     120.659 119.151  80.434  1.00 84.01           N  
ATOM   2061  CA  GLU A 267     121.794 118.267  80.668  1.00 84.01           C  
ATOM   2062  C   GLU A 267     122.949 119.018  81.313  1.00 84.01           C  
ATOM   2063  O   GLU A 267     123.683 118.448  82.129  1.00 84.01           O  
ATOM   2064  CB  GLU A 267     122.241 117.618  79.359  1.00 84.01           C  
ATOM   2065  CG  GLU A 267     123.199 116.454  79.543  1.00 84.01           C  
ATOM   2066  CD  GLU A 267     122.523 115.229  80.123  1.00 84.01           C  
ATOM   2067  OE1 GLU A 267     121.303 115.065  79.912  1.00 84.01           O  
ATOM   2068  OE2 GLU A 267     123.211 114.430  80.793  1.00 84.01           O  
ATOM   2069  N   VAL A 268     123.112 120.299  80.972  1.00 77.56           N  
ATOM   2070  CA  VAL A 268     124.152 121.117  81.587  1.00 77.56           C  
ATOM   2071  C   VAL A 268     123.939 121.219  83.090  1.00 77.56           C  
ATOM   2072  O   VAL A 268     124.896 121.417  83.848  1.00 77.56           O  
ATOM   2073  CB  VAL A 268     124.196 122.507  80.922  1.00 77.56           C  
ATOM   2074  CG1 VAL A 268     124.481 122.369  79.436  1.00 77.56           C  
ATOM   2075  CG2 VAL A 268     122.886 123.247  81.142  1.00 77.56           C  
ATOM   2076  N   TYR A 269     122.691 121.096  83.547  1.00 69.89           N  
ATOM   2077  CA  TYR A 269     122.432 121.054  84.982  1.00 69.89           C  
ATOM   2078  C   TYR A 269     123.050 119.813  85.613  1.00 69.89           C  
ATOM   2079  O   TYR A 269     123.647 119.887  86.694  1.00 69.89           O  
ATOM   2080  CB  TYR A 269     120.927 121.082  85.249  1.00 69.89           C  
ATOM   2081  CG  TYR A 269     120.241 122.394  84.944  1.00 69.89           C  
ATOM   2082  CD1 TYR A 269     120.969 123.529  84.619  1.00 69.89           C  
ATOM   2083  CD2 TYR A 269     118.857 122.494  84.982  1.00 69.89           C  
ATOM   2084  CE1 TYR A 269     120.337 124.724  84.343  1.00 69.89           C  
ATOM   2085  CE2 TYR A 269     118.218 123.682  84.707  1.00 69.89           C  
ATOM   2086  CZ  TYR A 269     118.961 124.794  84.389  1.00 69.89           C  
ATOM   2087  OH  TYR A 269     118.323 125.979  84.115  1.00 69.89           O  
ATOM   2088  N   ARG A 270     122.935 118.665  84.937  1.00 69.79           N  
ATOM   2089  CA  ARG A 270     123.319 117.397  85.551  1.00 69.79           C  
ATOM   2090  C   ARG A 270     124.778 117.395  85.978  1.00 69.79           C  
ATOM   2091  O   ARG A 270     125.100 116.925  87.076  1.00 69.79           O  
ATOM   2092  CB  ARG A 270     123.048 116.243  84.586  1.00 69.79           C  
ATOM   2093  N   SER A 271     125.665 117.942  85.142  1.00 67.91           N  
ATOM   2094  CA  SER A 271     127.087 117.963  85.468  1.00 67.91           C  
ATOM   2095  C   SER A 271     127.334 118.593  86.832  1.00 67.91           C  
ATOM   2096  O   SER A 271     128.252 118.184  87.553  1.00 67.91           O  
ATOM   2097  CB  SER A 271     127.862 118.712  84.384  1.00 67.91           C  
ATOM   2098  OG  SER A 271     129.133 119.123  84.859  1.00 67.91           O  
ATOM   2099  N   VAL A 272     126.527 119.585  87.207  1.00 60.50           N  
ATOM   2100  CA  VAL A 272     126.646 120.177  88.533  1.00 60.50           C  
ATOM   2101  C   VAL A 272     125.602 119.636  89.502  1.00 60.50           C  
ATOM   2102  O   VAL A 272     125.804 119.729  90.723  1.00 60.50           O  
ATOM   2103  CB  VAL A 272     126.565 121.717  88.470  1.00 60.50           C  
ATOM   2104  CG1 VAL A 272     127.549 122.258  87.445  1.00 60.50           C  
ATOM   2105  CG2 VAL A 272     125.153 122.173  88.168  1.00 60.50           C  
ATOM   2106  N   ASP A 273     124.504 119.061  89.003  1.00 62.81           N  
ATOM   2107  CA  ASP A 273     123.456 118.583  89.899  1.00 62.81           C  
ATOM   2108  C   ASP A 273     123.975 117.467  90.797  1.00 62.81           C  
ATOM   2109  O   ASP A 273     123.736 117.477  92.010  1.00 62.81           O  
ATOM   2110  CB  ASP A 273     122.246 118.124  89.082  1.00 62.81           C  
ATOM   2111  CG  ASP A 273     121.067 117.703  89.946  1.00 62.81           C  
ATOM   2112  OD1 ASP A 273     121.230 116.854  90.847  1.00 62.81           O  
ATOM   2113  OD2 ASP A 273     119.960 118.234  89.718  1.00 62.81           O  
ATOM   2114  N   LEU A 274     124.707 116.508  90.222  1.00 61.79           N  
ATOM   2115  CA  LEU A 274     125.319 115.460  91.032  1.00 61.79           C  
ATOM   2116  C   LEU A 274     126.308 116.047  92.029  1.00 61.79           C  
ATOM   2117  O   LEU A 274     126.551 115.464  93.092  1.00 61.79           O  
ATOM   2118  CB  LEU A 274     126.012 114.433  90.137  1.00 61.79           C  
ATOM   2119  CG  LEU A 274     125.201 113.241  89.622  1.00 61.79           C  
ATOM   2120  CD1 LEU A 274     125.034 112.217  90.730  1.00 61.79           C  
ATOM   2121  CD2 LEU A 274     123.847 113.655  89.063  1.00 61.79           C  
ATOM   2122  N   ALA A 275     126.893 117.200  91.702  1.00 58.18           N  
ATOM   2123  CA  ALA A 275     127.795 117.851  92.641  1.00 58.18           C  
ATOM   2124  C   ALA A 275     127.045 118.395  93.847  1.00 58.18           C  
ATOM   2125  O   ALA A 275     127.623 118.512  94.932  1.00 58.18           O  
ATOM   2126  CB  ALA A 275     128.566 118.971  91.946  1.00 58.18           C  
ATOM   2127  N   PHE A 276     125.764 118.729  93.682  1.00 54.73           N  
ATOM   2128  CA  PHE A 276     125.011 119.318  94.784  1.00 54.73           C  
ATOM   2129  C   PHE A 276     124.743 118.292  95.877  1.00 54.73           C  
ATOM   2130  O   PHE A 276     125.241 118.421  97.003  1.00 54.73           O  
ATOM   2131  CB  PHE A 276     123.699 119.904  94.259  1.00 54.73           C  
ATOM   2132  CG  PHE A 276     122.962 120.750  95.260  1.00 54.73           C  
ATOM   2133  CD1 PHE A 276     123.595 121.225  96.397  1.00 54.73           C  
ATOM   2134  CD2 PHE A 276     121.632 121.076  95.059  1.00 54.73           C  
ATOM   2135  CE1 PHE A 276     122.917 122.002  97.312  1.00 54.73           C  
ATOM   2136  CE2 PHE A 276     120.950 121.854  95.971  1.00 54.73           C  
ATOM   2137  CZ  PHE A 276     121.593 122.316  97.099  1.00 54.73           C  
ATOM   2138  N   PHE A 277     123.989 117.240  95.546  1.00 53.81           N  
ATOM   2139  CA  PHE A 277     123.478 116.332  96.567  1.00 53.81           C  
ATOM   2140  C   PHE A 277     124.598 115.660  97.346  1.00 53.81           C  
ATOM   2141  O   PHE A 277     124.491 115.512  98.570  1.00 53.81           O  
ATOM   2142  CB  PHE A 277     122.566 115.292  95.924  1.00 53.81           C  
ATOM   2143  CG  PHE A 277     121.241 115.844  95.494  1.00 53.81           C  
ATOM   2144  CD1 PHE A 277     120.607 116.813  96.250  1.00 53.81           C  
ATOM   2145  CD2 PHE A 277     120.635 115.407  94.332  1.00 53.81           C  
ATOM   2146  CE1 PHE A 277     119.391 117.328  95.861  1.00 53.81           C  
ATOM   2147  CE2 PHE A 277     119.417 115.921  93.937  1.00 53.81           C  
ATOM   2148  CZ  PHE A 277     118.795 116.883  94.703  1.00 53.81           C  
ATOM   2149  N   ILE A 278     125.675 115.260  96.666  1.00 55.08           N  
ATOM   2150  CA  ILE A 278     126.840 114.730  97.367  1.00 55.08           C  
ATOM   2151  C   ILE A 278     127.277 115.692  98.463  1.00 55.08           C  
ATOM   2152  O   ILE A 278     127.332 115.328  99.645  1.00 55.08           O  
ATOM   2153  CB  ILE A 278     127.983 114.456  96.373  1.00 55.08           C  
ATOM   2154  CG1 ILE A 278     127.660 113.241  95.505  1.00 55.08           C  
ATOM   2155  CG2 ILE A 278     129.293 114.249  97.115  1.00 55.08           C  
ATOM   2156  CD1 ILE A 278     128.622 113.047  94.356  1.00 55.08           C  
ATOM   2157  N   THR A 279     127.537 116.949  98.096  1.00 56.41           N  
ATOM   2158  CA  THR A 279     127.939 117.946  99.077  1.00 56.41           C  
ATOM   2159  C   THR A 279     126.885 118.159 100.151  1.00 56.41           C  
ATOM   2160  O   THR A 279     127.236 118.547 101.272  1.00 56.41           O  
ATOM   2161  CB  THR A 279     128.249 119.275  98.390  1.00 56.41           C  
ATOM   2162  OG1 THR A 279     127.092 119.724  97.673  1.00 56.41           O  
ATOM   2163  CG2 THR A 279     129.416 119.116  97.431  1.00 56.41           C  
ATOM   2164  N   LEU A 280     125.612 117.900  99.843  1.00 53.08           N  
ATOM   2165  CA  LEU A 280     124.582 117.993 100.870  1.00 53.08           C  
ATOM   2166  C   LEU A 280     124.879 117.039 102.017  1.00 53.08           C  
ATOM   2167  O   LEU A 280     124.804 117.425 103.190  1.00 53.08           O  
ATOM   2168  CB  LEU A 280     123.208 117.706 100.266  1.00 53.08           C  
ATOM   2169  CG  LEU A 280     122.253 118.898 100.192  1.00 53.08           C  
ATOM   2170  CD1 LEU A 280     120.868 118.449  99.767  1.00 53.08           C  
ATOM   2171  CD2 LEU A 280     122.197 119.620 101.524  1.00 53.08           C  
ATOM   2172  N   SER A 281     125.261 115.799 101.698  1.00 55.61           N  
ATOM   2173  CA  SER A 281     125.642 114.866 102.750  1.00 55.61           C  
ATOM   2174  C   SER A 281     126.808 115.394 103.569  1.00 55.61           C  
ATOM   2175  O   SER A 281     126.899 115.098 104.767  1.00 55.61           O  
ATOM   2176  CB  SER A 281     125.997 113.506 102.152  1.00 55.61           C  
ATOM   2177  OG  SER A 281     126.606 113.658 100.884  1.00 55.61           O  
ATOM   2178  N   PHE A 282     127.681 116.196 102.952  1.00 58.80           N  
ATOM   2179  CA  PHE A 282     128.799 116.779 103.680  1.00 58.80           C  
ATOM   2180  C   PHE A 282     128.321 117.587 104.877  1.00 58.80           C  
ATOM   2181  O   PHE A 282     128.989 117.603 105.918  1.00 58.80           O  
ATOM   2182  CB  PHE A 282     129.628 117.656 102.744  1.00 58.80           C  
ATOM   2183  CG  PHE A 282     130.960 117.069 102.387  1.00 58.80           C  
ATOM   2184  CD1 PHE A 282     131.160 116.481 101.150  1.00 58.80           C  
ATOM   2185  CD2 PHE A 282     132.013 117.109 103.282  1.00 58.80           C  
ATOM   2186  CE1 PHE A 282     132.384 115.939 100.815  1.00 58.80           C  
ATOM   2187  CE2 PHE A 282     133.241 116.571 102.951  1.00 58.80           C  
ATOM   2188  CZ  PHE A 282     133.427 115.985 101.717  1.00 58.80           C  
ATOM   2189  N   THR A 283     127.162 118.243 104.761  1.00 56.04           N  
ATOM   2190  CA  THR A 283     126.649 119.012 105.888  1.00 56.04           C  
ATOM   2191  C   THR A 283     126.400 118.140 107.109  1.00 56.04           C  
ATOM   2192  O   THR A 283     126.606 118.605 108.236  1.00 56.04           O  
ATOM   2193  CB  THR A 283     125.363 119.744 105.504  1.00 56.04           C  
ATOM   2194  OG1 THR A 283     124.260 118.832 105.549  1.00 56.04           O  
ATOM   2195  CG2 THR A 283     125.479 120.342 104.112  1.00 56.04           C  
ATOM   2196  N   TYR A 284     125.988 116.886 106.918  1.00 52.79           N  
ATOM   2197  CA  TYR A 284     125.799 116.000 108.058  1.00 52.79           C  
ATOM   2198  C   TYR A 284     127.104 115.703 108.780  1.00 52.79           C  
ATOM   2199  O   TYR A 284     127.075 115.408 109.980  1.00 52.79           O  
ATOM   2200  CB  TYR A 284     125.135 114.698 107.614  1.00 52.79           C  
ATOM   2201  CG  TYR A 284     123.864 114.931 106.844  1.00 52.79           C  
ATOM   2202  CD1 TYR A 284     122.895 115.799 107.320  1.00 52.79           C  
ATOM   2203  CD2 TYR A 284     123.638 114.296 105.636  1.00 52.79           C  
ATOM   2204  CE1 TYR A 284     121.735 116.022 106.618  1.00 52.79           C  
ATOM   2205  CE2 TYR A 284     122.481 114.512 104.927  1.00 52.79           C  
ATOM   2206  CZ  TYR A 284     121.533 115.376 105.422  1.00 52.79           C  
ATOM   2207  OH  TYR A 284     120.379 115.592 104.714  1.00 52.79           O  
ATOM   2208  N   MET A 285     128.243 115.789 108.085  1.00 63.36           N  
ATOM   2209  CA  MET A 285     129.522 115.674 108.774  1.00 63.36           C  
ATOM   2210  C   MET A 285     129.654 116.737 109.851  1.00 63.36           C  
ATOM   2211  O   MET A 285     130.245 116.480 110.906  1.00 63.36           O  
ATOM   2212  CB  MET A 285     130.678 115.770 107.779  1.00 63.36           C  
ATOM   2213  CG  MET A 285     132.050 115.770 108.435  1.00 63.36           C  
ATOM   2214  SD  MET A 285     133.169 114.531 107.755  1.00 63.36           S  
ATOM   2215  CE  MET A 285     133.543 115.247 106.160  1.00 63.36           C  
ATOM   2216  N   ASN A 286     129.090 117.925 109.614  1.00 57.99           N  
ATOM   2217  CA  ASN A 286     129.022 118.927 110.669  1.00 57.99           C  
ATOM   2218  C   ASN A 286     128.385 118.344 111.921  1.00 57.99           C  
ATOM   2219  O   ASN A 286     128.967 118.412 113.011  1.00 57.99           O  
ATOM   2220  CB  ASN A 286     128.240 120.146 110.181  1.00 57.99           C  
ATOM   2221  CG  ASN A 286     127.859 121.086 111.307  1.00 57.99           C  
ATOM   2222  OD1 ASN A 286     128.643 121.329 112.223  1.00 57.99           O  
ATOM   2223  ND2 ASN A 286     126.647 121.624 111.242  1.00 57.99           N  
ATOM   2224  N   SER A 287     127.219 117.709 111.773  1.00 58.21           N  
ATOM   2225  CA  SER A 287     126.551 117.105 112.921  1.00 58.21           C  
ATOM   2226  C   SER A 287     127.437 116.060 113.587  1.00 58.21           C  
ATOM   2227  O   SER A 287     127.341 115.834 114.799  1.00 58.21           O  
ATOM   2228  CB  SER A 287     125.225 116.482 112.489  1.00 58.21           C  
ATOM   2229  OG  SER A 287     125.415 115.161 112.016  1.00 58.21           O  
ATOM   2230  N   MET A 288     128.307 115.412 112.812  1.00 63.39           N  
ATOM   2231  CA  MET A 288     129.211 114.430 113.395  1.00 63.39           C  
ATOM   2232  C   MET A 288     130.355 115.106 114.142  1.00 63.39           C  
ATOM   2233  O   MET A 288     130.791 114.618 115.191  1.00 63.39           O  
ATOM   2234  CB  MET A 288     129.751 113.504 112.304  1.00 63.39           C  
ATOM   2235  CG  MET A 288     131.132 112.941 112.588  1.00 63.39           C  
ATOM   2236  SD  MET A 288     131.836 112.043 111.195  1.00 63.39           S  
ATOM   2237  CE  MET A 288     130.503 110.912 110.821  1.00 63.39           C  
ATOM   2238  N   LEU A 289     130.849 116.236 113.628  1.00 62.96           N  
ATOM   2239  CA  LEU A 289     132.060 116.827 114.189  1.00 62.96           C  
ATOM   2240  C   LEU A 289     131.805 117.693 115.414  1.00 62.96           C  
ATOM   2241  O   LEU A 289     132.737 117.914 116.194  1.00 62.96           O  
ATOM   2242  CB  LEU A 289     132.803 117.651 113.132  1.00 62.96           C  
ATOM   2243  CG  LEU A 289     133.267 116.991 111.829  1.00 62.96           C  
ATOM   2244  CD1 LEU A 289     134.567 117.617 111.368  1.00 62.96           C  
ATOM   2245  CD2 LEU A 289     133.463 115.500 111.997  1.00 62.96           C  
ATOM   2246  N   ASP A 290     130.584 118.193 115.606  1.00 65.42           N  
ATOM   2247  CA  ASP A 290     130.308 118.996 116.795  1.00 65.42           C  
ATOM   2248  C   ASP A 290     130.576 118.253 118.099  1.00 65.42           C  
ATOM   2249  O   ASP A 290     131.179 118.860 119.002  1.00 65.42           O  
ATOM   2250  CB  ASP A 290     128.869 119.530 116.762  1.00 65.42           C  
ATOM   2251  CG  ASP A 290     128.503 120.140 115.428  1.00 65.42           C  
ATOM   2252  OD1 ASP A 290     127.461 119.750 114.862  1.00 65.42           O  
ATOM   2253  OD2 ASP A 290     129.257 121.010 114.947  1.00 65.42           O  
ATOM   2254  N   PRO A 291     130.175 116.989 118.281  1.00 67.03           N  
ATOM   2255  CA  PRO A 291     130.543 116.296 119.526  1.00 67.03           C  
ATOM   2256  C   PRO A 291     132.039 116.238 119.765  1.00 67.03           C  
ATOM   2257  O   PRO A 291     132.474 116.281 120.922  1.00 67.03           O  
ATOM   2258  CB  PRO A 291     129.952 114.894 119.335  1.00 67.03           C  
ATOM   2259  CG  PRO A 291     128.830 115.090 118.407  1.00 67.03           C  
ATOM   2260  CD  PRO A 291     129.238 116.186 117.474  1.00 67.03           C  
ATOM   2261  N   VAL A 292     132.839 116.143 118.703  1.00 66.04           N  
ATOM   2262  CA  VAL A 292     134.288 116.079 118.864  1.00 66.04           C  
ATOM   2263  C   VAL A 292     134.822 117.378 119.454  1.00 66.04           C  
ATOM   2264  O   VAL A 292     135.683 117.365 120.343  1.00 66.04           O  
ATOM   2265  CB  VAL A 292     134.957 115.751 117.517  1.00 66.04           C  
ATOM   2266  CG1 VAL A 292     136.469 115.751 117.658  1.00 66.04           C  
ATOM   2267  CG2 VAL A 292     134.465 114.410 116.998  1.00 66.04           C  
ATOM   2268  N   VAL A 293     134.316 118.516 118.983  1.00 66.33           N  
ATOM   2269  CA  VAL A 293     134.911 119.807 119.313  1.00 66.33           C  
ATOM   2270  C   VAL A 293     134.134 120.516 120.418  1.00 66.33           C  
ATOM   2271  O   VAL A 293     134.731 121.128 121.310  1.00 66.33           O  
ATOM   2272  CB  VAL A 293     135.018 120.692 118.056  1.00 66.33           C  
ATOM   2273  CG1 VAL A 293     133.690 120.753 117.320  1.00 66.33           C  
ATOM   2274  CG2 VAL A 293     135.494 122.081 118.423  1.00 66.33           C  
ATOM   2275  N   TYR A 294     132.804 120.433 120.381  1.00 61.75           N  
ATOM   2276  CA  TYR A 294     131.997 121.237 121.295  1.00 61.75           C  
ATOM   2277  C   TYR A 294     131.955 120.637 122.696  1.00 61.75           C  
ATOM   2278  O   TYR A 294     132.424 121.251 123.659  1.00 61.75           O  
ATOM   2279  CB  TYR A 294     130.582 121.402 120.737  1.00 61.75           C  
ATOM   2280  CG  TYR A 294     130.396 122.695 119.988  1.00 61.75           C  
ATOM   2281  CD1 TYR A 294     130.746 123.902 120.570  1.00 61.75           C  
ATOM   2282  CD2 TYR A 294     129.886 122.711 118.699  1.00 61.75           C  
ATOM   2283  CE1 TYR A 294     130.586 125.088 119.897  1.00 61.75           C  
ATOM   2284  CE2 TYR A 294     129.724 123.898 118.014  1.00 61.75           C  
ATOM   2285  CZ  TYR A 294     130.078 125.083 118.621  1.00 61.75           C  
ATOM   2286  OH  TYR A 294     129.925 126.275 117.960  1.00 61.75           O  
ATOM   2287  N   TYR A 295     131.392 119.439 122.831  1.00 67.61           N  
ATOM   2288  CA  TYR A 295     131.275 118.818 124.143  1.00 67.61           C  
ATOM   2289  C   TYR A 295     132.563 118.147 124.595  1.00 67.61           C  
ATOM   2290  O   TYR A 295     132.852 118.125 125.797  1.00 67.61           O  
ATOM   2291  CB  TYR A 295     130.136 117.794 124.152  1.00 67.61           C  
ATOM   2292  CG  TYR A 295     129.017 118.106 123.186  1.00 67.61           C  
ATOM   2293  CD1 TYR A 295     128.330 119.310 123.250  1.00 67.61           C  
ATOM   2294  CD2 TYR A 295     128.643 117.191 122.216  1.00 67.61           C  
ATOM   2295  CE1 TYR A 295     127.308 119.594 122.366  1.00 67.61           C  
ATOM   2296  CE2 TYR A 295     127.625 117.465 121.330  1.00 67.61           C  
ATOM   2297  CZ  TYR A 295     126.960 118.665 121.409  1.00 67.61           C  
ATOM   2298  OH  TYR A 295     125.945 118.937 120.525  1.00 67.61           O  
ATOM   2299  N   PHE A 296     133.344 117.602 123.665  1.00 70.89           N  
ATOM   2300  CA  PHE A 296     134.585 116.907 124.008  1.00 70.89           C  
ATOM   2301  C   PHE A 296     135.765 117.880 123.986  1.00 70.89           C  
ATOM   2302  O   PHE A 296     136.705 117.760 123.202  1.00 70.89           O  
ATOM   2303  CB  PHE A 296     134.812 115.733 123.063  1.00 70.89           C  
ATOM   2304  CG  PHE A 296     133.798 114.633 123.205  1.00 70.89           C  
ATOM   2305  CD1 PHE A 296     132.904 114.623 124.263  1.00 70.89           C  
ATOM   2306  CD2 PHE A 296     133.736 113.610 122.275  1.00 70.89           C  
ATOM   2307  CE1 PHE A 296     131.970 113.614 124.390  1.00 70.89           C  
ATOM   2308  CE2 PHE A 296     132.805 112.597 122.398  1.00 70.89           C  
ATOM   2309  CZ  PHE A 296     131.921 112.600 123.456  1.00 70.89           C  
ATOM   2310  N   SER A 297     135.693 118.867 124.879  1.00 74.54           N  
ATOM   2311  CA  SER A 297     136.751 119.852 125.025  1.00 74.54           C  
ATOM   2312  C   SER A 297     137.115 120.131 126.476  1.00 74.54           C  
ATOM   2313  O   SER A 297     137.969 120.987 126.727  1.00 74.54           O  
ATOM   2314  CB  SER A 297     136.359 121.170 124.342  1.00 74.54           C  
ATOM   2315  OG  SER A 297     137.307 122.186 124.616  1.00 74.54           O  
ATOM   2316  N   SER A 298     136.499 119.446 127.428  1.00 80.22           N  
ATOM   2317  CA  SER A 298     136.838 119.640 128.831  1.00 80.22           C  
ATOM   2318  C   SER A 298     138.186 118.997 129.126  1.00 80.22           C  
ATOM   2319  O   SER A 298     138.347 117.789 128.907  1.00 80.22           O  
ATOM   2320  CB  SER A 298     135.757 119.044 129.728  1.00 80.22           C  
ATOM   2321  OG  SER A 298     136.047 117.695 130.051  1.00 80.22           O  
ATOM   2322  N   PRO A 299     139.180 119.752 129.616  1.00 82.99           N  
ATOM   2323  CA  PRO A 299     140.506 119.219 129.949  1.00 82.99           C  
ATOM   2324  C   PRO A 299     140.458 118.169 131.056  1.00 82.99           C  
ATOM   2325  O   PRO A 299     140.663 118.516 132.219  1.00 82.99           O  
ATOM   2326  CB  PRO A 299     141.279 120.461 130.411  1.00 82.99           C  
ATOM   2327  CG  PRO A 299     140.230 121.459 130.777  1.00 82.99           C  
ATOM   2328  CD  PRO A 299     139.094 121.203 129.844  1.00 82.99           C  
TER    2329      PRO A 299                                                      
HETATM 2330  C10 OKL A 401     116.795 118.004 102.471  1.00 52.42           C  
HETATM 2331  C12 OKL A 401     117.749 117.028 102.080  1.00 52.42           C  
HETATM 2332  C13 OKL A 401     117.478 116.233 101.000  1.00 52.42           C  
HETATM 2333  C15 OKL A 401     119.420 115.671 101.784  1.00 52.42           C  
HETATM 2334  C01 OKL A 401     114.528 112.382 102.773  1.00 52.42           C  
HETATM 2335  C02 OKL A 401     114.733 112.513 101.266  1.00 52.42           C  
HETATM 2336  C03 OKL A 401     114.921 113.968 100.844  1.00 52.42           C  
HETATM 2337  C04 OKL A 401     115.829 114.121  99.624  1.00 52.42           C  
HETATM 2338  C05 OKL A 401     115.999 115.581  99.205  1.00 52.42           C  
HETATM 2339  C07 OKL A 401     115.437 117.332 100.739  1.00 52.42           C  
HETATM 2340  N06 OKL A 401     116.304 116.414 100.352  1.00 52.42           N  
HETATM 2341  N09 OKL A 401     115.669 118.120 101.783  1.00 52.42           N  
HETATM 2342  N14 OKL A 401     118.538 115.400 100.843  1.00 52.42           N  
HETATM 2343  N16 OKL A 401     118.969 116.655 102.548  1.00 52.42           N  
HETATM 2344  O08 OKL A 401     114.239 117.477 100.033  1.00 52.42           O  
HETATM 2345  O11 OKL A 401     117.037 118.833 103.568  1.00 52.42           O  
HETATM 2346 CL17 OKL A 401     120.980 114.828 101.978  1.00 52.42          CL  
CONECT   82 1372                                                                
CONECT  732 1329                                                                
CONECT 1329  732                                                                
CONECT 1372   82                                                                
CONECT 2330 2331 2341 2345                                                      
CONECT 2331 2330 2332 2343                                                      
CONECT 2332 2331 2340 2342                                                      
CONECT 2333 2342 2343 2346                                                      
CONECT 2334 2335                                                                
CONECT 2335 2334 2336                                                           
CONECT 2336 2335 2337                                                           
CONECT 2337 2336 2338                                                           
CONECT 2338 2337 2340                                                           
CONECT 2339 2340 2341 2344                                                      
CONECT 2340 2332 2338 2339                                                      
CONECT 2341 2330 2339                                                           
CONECT 2342 2332 2333                                                           
CONECT 2343 2331 2333                                                           
CONECT 2344 2339                                                                
CONECT 2345 2330                                                                
CONECT 2346 2333                                                                
MASTER      337    0    1    8    4    0    0    6 2345    1   21   37          
END