HEADER    MEMBRANE PROTEIN                        21-JUL-23   8K5B              
TITLE     CRYO-EM STRUCTURE OF NIACIN 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 8K5B    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.    3.43 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)  : 3.430                          
REMARK   3   NUMBER OF PARTICLES               : 291411                         
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 8K5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300039085.                                   
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                 : NIACIN BOUND HUMAN HYDROXY        
REMARK 245                                    -CARBOXYLIC ACID RECEPTOR 2       
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 3.10                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     CYS A  19    SG                                                  
REMARK 470     ASP A  23    CG   OD1  OD2                                       
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     SER A  58    OG                                                  
REMARK 470     ASP A  97    CG   OD1  OD2                                       
REMARK 470     ILE A  98    CG1  CG2  CD1                                       
REMARK 470     MET A 106    SD   CE                                             
REMARK 470     MET A 109    CE                                                  
REMARK 470     MET A 167    CG   SD   CE                                        
REMARK 470     CYS A 266    SG                                                  
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    LYS A  15        9.04     59.02                                   
REMARK 500    PHE A  25       18.00     57.21                                   
REMARK 500    TRP A  59      -99.29   -152.33                                   
REMARK 500    LYS A  60      171.77     72.04                                   
REMARK 500    TRP A  93       93.25    -68.15                                   
REMARK 500    LYS A  94       64.69   -100.90                                   
REMARK 500    SER A 298       72.36     53.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-36900   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF NIACIN BOUND HUMAN HYDROXY-CARBOXYLIC ACID      
REMARK 900 RECEPTOR 2 (LOCAL REFINEMENT)                                        
DBREF  8K5B A -112     0  PDB    8K5B     8K5B          -112      0             
DBREF  8K5B 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    NIO  A 401       9                                                       
HETNAM     NIO NICOTINIC ACID                                                   
FORMUL   2  NIO    C6 H5 N O2                                                   
HELIX    1 AA1 VAL A   29  PHE A   54  1                                  26    
HELIX    2 AA2 TRP A   59  ARG A   89  1                                  31    
HELIX    3 AA3 ASP A   97  HIS A  131  1                                  35    
HELIX    4 AA4 SER A  140  LEU A  158  1                                  19    
HELIX    5 AA5 VAL A  160  LYS A  165  1                                   6    
HELIX    6 AA6 GLN A  187  ARG A  218  1                                  32    
HELIX    7 AA7 LYS A  225  SER A  261  1                                  37    
HELIX    8 AA8 ASN A  265  VAL A  268  5                                   4    
HELIX    9 AA9 TYR A  269  TYR A  295  1                                  27    
SHEET    1 AA1 2 ILE A 169  ASN A 171  0                                        
SHEET    2 AA1 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     115.818 106.636 179.685  1.00124.10           N  
ATOM      2  CA  HIS A   9     116.783 105.811 180.401  1.00126.81           C  
ATOM      3  C   HIS A   9     117.875 105.309 179.461  1.00126.05           C  
ATOM      4  O   HIS A   9     118.275 106.009 178.530  1.00122.66           O  
ATOM      5  CB  HIS A   9     116.083 104.629 181.076  1.00123.82           C  
ATOM      6  CG  HIS A   9     116.628 104.297 182.430  1.00125.64           C  
ATOM      7  ND1 HIS A   9     116.314 105.024 183.558  1.00125.92           N  
ATOM      8  CD2 HIS A   9     117.468 103.316 182.836  1.00126.14           C  
ATOM      9  CE1 HIS A   9     116.936 104.505 184.601  1.00126.52           C  
ATOM     10  NE2 HIS A   9     117.643 103.467 184.190  1.00126.92           N  
ATOM     11  N   PHE A  10     118.353 104.092 179.709  1.00125.38           N  
ATOM     12  CA  PHE A  10     119.392 103.464 178.900  1.00125.66           C  
ATOM     13  C   PHE A  10     118.754 102.350 178.079  1.00125.38           C  
ATOM     14  O   PHE A  10     118.296 101.346 178.635  1.00123.60           O  
ATOM     15  CB  PHE A  10     120.520 102.927 179.779  1.00124.12           C  
ATOM     16  CG  PHE A  10     121.473 102.018 179.055  1.00124.89           C  
ATOM     17  CD1 PHE A  10     122.146 102.454 177.927  1.00125.86           C  
ATOM     18  CD2 PHE A  10     121.696 100.728 179.505  1.00122.41           C  
ATOM     19  CE1 PHE A  10     123.023 101.620 177.260  1.00124.32           C  
ATOM     20  CE2 PHE A  10     122.571  99.889 178.841  1.00121.35           C  
ATOM     21  CZ  PHE A  10     123.235 100.337 177.717  1.00122.91           C  
ATOM     22  N   LEU A  11     118.727 102.529 176.762  1.00122.10           N  
ATOM     23  CA  LEU A  11     118.159 101.548 175.852  1.00120.53           C  
ATOM     24  C   LEU A  11     119.261 100.608 175.366  1.00120.22           C  
ATOM     25  O   LEU A  11     120.380 100.609 175.885  1.00120.21           O  
ATOM     26  CB  LEU A  11     117.451 102.254 174.700  1.00122.31           C  
ATOM     27  CG  LEU A  11     116.548 103.410 175.130  1.00121.85           C  
ATOM     28  CD1 LEU A  11     116.393 104.408 173.998  1.00119.64           C  
ATOM     29  CD2 LEU A  11     115.192 102.898 175.596  1.00120.04           C  
ATOM     30  N   GLU A  12     118.957  99.789 174.361  1.00121.69           N  
ATOM     31  CA  GLU A  12     119.929  98.829 173.860  1.00122.67           C  
ATOM     32  C   GLU A  12     119.707  98.593 172.374  1.00121.64           C  
ATOM     33  O   GLU A  12     118.571  98.387 171.936  1.00120.71           O  
ATOM     34  CB  GLU A  12     119.839  97.505 174.628  1.00122.35           C  
ATOM     35  CG  GLU A  12     120.382  96.299 173.875  1.00122.16           C  
ATOM     36  CD  GLU A  12     121.892  96.330 173.721  1.00121.12           C  
ATOM     37  OE1 GLU A  12     122.557  97.062 174.483  1.00119.37           O  
ATOM     38  OE2 GLU A  12     122.414  95.615 172.841  1.00120.89           O  
ATOM     39  N   ILE A  13     120.796  98.627 171.612  1.00112.56           N  
ATOM     40  CA  ILE A  13     120.804  98.295 170.194  1.00112.59           C  
ATOM     41  C   ILE A  13     121.889  97.250 169.978  1.00113.05           C  
ATOM     42  O   ILE A  13     122.928  97.282 170.645  1.00110.24           O  
ATOM     43  CB  ILE A  13     121.037  99.549 169.320  1.00111.93           C  
ATOM     44  CG1 ILE A  13     119.705 100.227 168.999  1.00113.40           C  
ATOM     45  CG2 ILE A  13     121.784  99.211 168.037  1.00110.12           C  
ATOM     46  CD1 ILE A  13     118.835  99.429 168.059  1.00108.08           C  
ATOM     47  N   ASP A  14     121.632  96.300 169.077  1.00123.78           N  
ATOM     48  CA  ASP A  14     122.569  95.207 168.848  1.00123.39           C  
ATOM     49  C   ASP A  14     123.966  95.739 168.552  1.00122.85           C  
ATOM     50  O   ASP A  14     124.148  96.607 167.692  1.00124.08           O  
ATOM     51  CB  ASP A  14     122.068  94.317 167.704  1.00122.35           C  
ATOM     52  CG  ASP A  14     122.364  94.895 166.332  1.00122.12           C  
ATOM     53  OD1 ASP A  14     121.726  95.901 165.958  1.00121.46           O  
ATOM     54  OD2 ASP A  14     123.239  94.346 165.630  1.00120.76           O  
ATOM     55  N   LYS A  15     124.943  95.250 169.314  1.00109.13           N  
ATOM     56  CA  LYS A  15     126.354  95.611 169.205  1.00109.27           C  
ATOM     57  C   LYS A  15     126.612  97.102 169.405  1.00111.89           C  
ATOM     58  O   LYS A  15     127.736  97.564 169.178  1.00112.72           O  
ATOM     59  CB  LYS A  15     126.945  95.158 167.863  1.00110.25           C  
ATOM     60  CG  LYS A  15     126.557  93.742 167.458  1.00110.38           C  
ATOM     61  CD  LYS A  15     126.872  92.742 168.560  1.00108.95           C  
ATOM     62  CE  LYS A  15     126.450  91.336 168.168  1.00109.23           C  
ATOM     63  NZ  LYS A  15     126.799  90.341 169.219  1.00108.27           N  
ATOM     64  N   LYS A  16     125.606  97.871 169.829  1.00111.73           N  
ATOM     65  CA  LYS A  16     125.741  99.317 170.022  1.00108.99           C  
ATOM     66  C   LYS A  16     124.873  99.716 171.212  1.00110.20           C  
ATOM     67  O   LYS A  16     123.651  99.823 171.083  1.00110.06           O  
ATOM     68  CB  LYS A  16     125.331 100.090 168.771  1.00106.97           C  
ATOM     69  CG  LYS A  16     126.092  99.740 167.502  1.00108.54           C  
ATOM     70  CD  LYS A  16     125.483 100.435 166.294  1.00108.67           C  
ATOM     71  CE  LYS A  16     124.466  99.547 165.595  1.00107.53           C  
ATOM     72  NZ  LYS A  16     123.573 100.323 164.688  1.00106.52           N  
ATOM     73  N   ASN A  17     125.498  99.947 172.363  1.00111.07           N  
ATOM     74  CA  ASN A  17     124.765 100.399 173.544  1.00111.53           C  
ATOM     75  C   ASN A  17     124.451 101.883 173.384  1.00112.78           C  
ATOM     76  O   ASN A  17     125.305 102.743 173.610  1.00108.79           O  
ATOM     77  CB  ASN A  17     125.561 100.120 174.814  1.00109.64           C  
ATOM     78  CG  ASN A  17     127.032 100.450 174.667  1.00109.54           C  
ATOM     79  OD1 ASN A  17     127.458 100.998 173.653  1.00110.40           O  
ATOM     80  ND2 ASN A  17     127.818 100.115 175.684  1.00108.08           N  
ATOM     81  N   CYS A  18     123.216 102.185 172.996  1.00112.83           N  
ATOM     82  CA  CYS A  18     122.772 103.543 172.719  1.00108.57           C  
ATOM     83  C   CYS A  18     121.827 104.029 173.810  1.00108.06           C  
ATOM     84  O   CYS A  18     121.337 103.257 174.638  1.00106.54           O  
ATOM     85  CB  CYS A  18     122.079 103.621 171.354  1.00109.06           C  
ATOM     86  SG  CYS A  18     122.857 102.644 170.054  1.00117.17           S  
ATOM     87  N   CYS A  19     121.574 105.340 173.798  1.00 99.97           N  
ATOM     88  CA  CYS A  19     120.653 105.947 174.758  1.00 99.04           C  
ATOM     89  C   CYS A  19     120.129 107.244 174.143  1.00 97.71           C  
ATOM     90  O   CYS A  19     120.844 108.249 174.120  1.00 96.16           O  
ATOM     91  CB  CYS A  19     121.337 106.198 176.092  1.00 97.43           C  
ATOM     92  N   VAL A  20     118.894 107.208 173.648  1.00 91.18           N  
ATOM     93  CA  VAL A  20     118.226 108.379 173.091  1.00 91.33           C  
ATOM     94  C   VAL A  20     116.861 108.504 173.752  1.00 90.39           C  
ATOM     95  O   VAL A  20     116.110 107.526 173.822  1.00 87.06           O  
ATOM     96  CB  VAL A  20     118.086 108.290 171.560  1.00 90.80           C  
ATOM     97  CG1 VAL A  20     117.157 109.378 171.047  1.00 93.31           C  
ATOM     98  CG2 VAL A  20     119.449 108.402 170.902  1.00 88.37           C  
ATOM     99  N   PHE A  21     116.540 109.703 174.227  1.00 92.39           N  
ATOM    100  CA  PHE A  21     115.362 109.923 175.046  1.00 90.81           C  
ATOM    101  C   PHE A  21     114.208 110.452 174.200  1.00 91.49           C  
ATOM    102  O   PHE A  21     114.309 110.616 172.983  1.00 91.72           O  
ATOM    103  CB  PHE A  21     115.690 110.891 176.182  1.00 90.51           C  
ATOM    104  CG  PHE A  21     117.126 110.852 176.606  1.00 89.62           C  
ATOM    105  CD1 PHE A  21     117.646 109.736 177.234  1.00 92.11           C  
ATOM    106  CD2 PHE A  21     117.960 111.925 176.357  1.00 86.51           C  
ATOM    107  CE1 PHE A  21     118.968 109.699 177.616  1.00 94.85           C  
ATOM    108  CE2 PHE A  21     119.281 111.892 176.736  1.00 90.85           C  
ATOM    109  CZ  PHE A  21     119.785 110.778 177.364  1.00 94.45           C  
ATOM    110  N   ARG A  22     113.091 110.722 174.870  1.00 95.41           N  
ATOM    111  CA  ARG A  22     111.889 111.287 174.268  1.00 96.66           C  
ATOM    112  C   ARG A  22     111.442 112.512 175.053  1.00 97.49           C  
ATOM    113  O   ARG A  22     110.272 112.666 175.410  1.00 97.85           O  
ATOM    114  CB  ARG A  22     110.776 110.247 174.200  1.00 97.35           C  
ATOM    115  CG  ARG A  22     110.613 109.431 175.472  1.00100.53           C  
ATOM    116  CD  ARG A  22     109.401 108.519 175.396  1.00 98.11           C  
ATOM    117  NE  ARG A  22     109.131 108.090 174.030  1.00 99.08           N  
ATOM    118  CZ  ARG A  22     108.026 108.383 173.361  1.00 96.90           C  
ATOM    119  NH1 ARG A  22     107.054 109.092 173.910  1.00 95.31           N  
ATOM    120  NH2 ARG A  22     107.893 107.958 172.108  1.00 94.33           N  
ATOM    121  N   ASP A  23     112.390 113.404 175.333  1.00101.02           N  
ATOM    122  CA  ASP A  23     112.119 114.554 176.183  1.00101.33           C  
ATOM    123  C   ASP A  23     111.097 115.482 175.537  1.00100.55           C  
ATOM    124  O   ASP A  23     110.954 115.536 174.313  1.00 96.29           O  
ATOM    125  CB  ASP A  23     113.412 115.319 176.470  1.00 95.43           C  
ATOM    126  N   ASP A  24     110.381 116.219 176.381  1.00104.40           N  
ATOM    127  CA  ASP A  24     109.339 117.127 175.924  1.00101.93           C  
ATOM    128  C   ASP A  24     109.979 118.386 175.343  1.00100.76           C  
ATOM    129  O   ASP A  24     111.195 118.463 175.148  1.00102.28           O  
ATOM    130  CB  ASP A  24     108.376 117.441 177.064  1.00104.23           C  
ATOM    131  CG  ASP A  24     107.394 116.317 177.320  1.00105.45           C  
ATOM    132  OD1 ASP A  24     107.304 115.401 176.476  1.00104.78           O  
ATOM    133  OD2 ASP A  24     106.711 116.347 178.366  1.00105.11           O  
ATOM    134  N   PHE A  25     109.151 119.390 175.051  1.00 98.30           N  
ATOM    135  CA  PHE A  25     109.559 120.601 174.339  1.00 99.95           C  
ATOM    136  C   PHE A  25     110.168 120.284 172.979  1.00 96.55           C  
ATOM    137  O   PHE A  25     110.865 121.117 172.393  1.00 92.51           O  
ATOM    138  CB  PHE A  25     110.527 121.451 175.171  1.00 98.38           C  
ATOM    139  CG  PHE A  25     109.859 122.564 175.926  1.00 97.32           C  
ATOM    140  CD1 PHE A  25     108.882 122.291 176.868  1.00 95.66           C  
ATOM    141  CD2 PHE A  25     110.205 123.884 175.691  1.00 98.24           C  
ATOM    142  CE1 PHE A  25     108.265 123.313 177.564  1.00 97.36           C  
ATOM    143  CE2 PHE A  25     109.591 124.910 176.383  1.00 96.57           C  
ATOM    144  CZ  PHE A  25     108.620 124.624 177.320  1.00 96.43           C  
ATOM    145  N   ILE A  26     109.916 119.077 172.478  1.00 92.00           N  
ATOM    146  CA  ILE A  26     110.265 118.701 171.113  1.00 95.39           C  
ATOM    147  C   ILE A  26     109.042 118.618 170.219  1.00 91.23           C  
ATOM    148  O   ILE A  26     109.193 118.562 168.987  1.00 89.81           O  
ATOM    149  CB  ILE A  26     111.044 117.368 171.079  1.00 94.34           C  
ATOM    150  CG1 ILE A  26     112.076 117.372 169.952  1.00 91.57           C  
ATOM    151  CG2 ILE A  26     110.093 116.187 170.937  1.00 94.48           C  
ATOM    152  CD1 ILE A  26     113.291 118.221 170.247  1.00 89.16           C  
ATOM    153  N   VAL A  27     107.838 118.621 170.794  1.00 85.63           N  
ATOM    154  CA  VAL A  27     106.599 118.593 170.032  1.00 86.67           C  
ATOM    155  C   VAL A  27     105.907 119.946 170.001  1.00 89.81           C  
ATOM    156  O   VAL A  27     104.810 120.059 169.438  1.00 93.01           O  
ATOM    157  CB  VAL A  27     105.641 117.522 170.590  1.00 86.45           C  
ATOM    158  CG1 VAL A  27     106.370 116.204 170.766  1.00 85.29           C  
ATOM    159  CG2 VAL A  27     105.045 117.982 171.910  1.00 87.91           C  
ATOM    160  N   LYS A  28     106.510 120.977 170.591  1.00 88.97           N  
ATOM    161  CA  LYS A  28     105.923 122.310 170.606  1.00 90.27           C  
ATOM    162  C   LYS A  28     106.681 123.323 169.765  1.00 90.64           C  
ATOM    163  O   LYS A  28     106.067 124.263 169.258  1.00 88.93           O  
ATOM    164  CB  LYS A  28     105.825 122.834 172.044  1.00 88.45           C  
ATOM    165  CG  LYS A  28     104.504 122.514 172.727  1.00 88.32           C  
ATOM    166  CD  LYS A  28     103.321 123.027 171.916  1.00 89.58           C  
ATOM    167  CE  LYS A  28     103.334 124.543 171.806  1.00 88.34           C  
ATOM    168  NZ  LYS A  28     101.998 125.085 171.436  1.00 85.22           N  
ATOM    169  N   VAL A  29     107.991 123.162 169.605  1.00 86.46           N  
ATOM    170  CA  VAL A  29     108.786 124.056 168.777  1.00 84.46           C  
ATOM    171  C   VAL A  29     109.101 123.438 167.420  1.00 81.90           C  
ATOM    172  O   VAL A  29     108.985 124.106 166.393  1.00 78.98           O  
ATOM    173  CB  VAL A  29     110.075 124.472 169.518  1.00 86.53           C  
ATOM    174  CG1 VAL A  29     110.863 123.254 169.974  1.00 82.60           C  
ATOM    175  CG2 VAL A  29     110.932 125.351 168.626  1.00 85.68           C  
ATOM    176  N   LEU A  30     109.500 122.169 167.399  1.00 84.24           N  
ATOM    177  CA  LEU A  30     109.866 121.530 166.138  1.00 86.20           C  
ATOM    178  C   LEU A  30     108.710 121.385 165.152  1.00 85.88           C  
ATOM    179  O   LEU A  30     108.931 121.641 163.955  1.00 82.65           O  
ATOM    180  CB  LEU A  30     110.518 120.171 166.416  1.00 80.25           C  
ATOM    181  CG  LEU A  30     112.041 120.235 166.373  1.00 79.60           C  
ATOM    182  CD1 LEU A  30     112.668 118.920 166.788  1.00 76.14           C  
ATOM    183  CD2 LEU A  30     112.476 120.632 164.988  1.00 80.54           C  
ATOM    184  N   PRO A  31     107.509 120.956 165.539  1.00 80.80           N  
ATOM    185  CA  PRO A  31     106.427 120.809 164.555  1.00 75.85           C  
ATOM    186  C   PRO A  31     106.075 122.121 163.867  1.00 79.58           C  
ATOM    187  O   PRO A  31     105.917 122.130 162.639  1.00 81.37           O  
ATOM    188  CB  PRO A  31     105.257 120.272 165.391  1.00 77.44           C  
ATOM    189  CG  PRO A  31     105.914 119.535 166.481  1.00 75.74           C  
ATOM    190  CD  PRO A  31     107.140 120.329 166.823  1.00 78.23           C  
ATOM    191  N   PRO A  32     105.909 123.243 164.591  1.00 76.70           N  
ATOM    192  CA  PRO A  32     105.641 124.501 163.867  1.00 78.15           C  
ATOM    193  C   PRO A  32     106.781 124.927 162.961  1.00 78.07           C  
ATOM    194  O   PRO A  32     106.544 125.451 161.860  1.00 77.80           O  
ATOM    195  CB  PRO A  32     105.402 125.511 164.998  1.00 77.11           C  
ATOM    196  CG  PRO A  32     104.978 124.686 166.149  1.00 75.38           C  
ATOM    197  CD  PRO A  32     105.824 123.462 166.048  1.00 74.58           C  
ATOM    198  N   VAL A  33     108.023 124.706 163.398  1.00 76.81           N  
ATOM    199  CA  VAL A  33     109.171 125.011 162.551  1.00 79.03           C  
ATOM    200  C   VAL A  33     109.078 124.227 161.252  1.00 81.06           C  
ATOM    201  O   VAL A  33     109.155 124.795 160.157  1.00 78.93           O  
ATOM    202  CB  VAL A  33     110.486 124.712 163.295  1.00 80.12           C  
ATOM    203  CG1 VAL A  33     111.639 124.601 162.312  1.00 78.12           C  
ATOM    204  CG2 VAL A  33     110.773 125.785 164.329  1.00 82.47           C  
ATOM    205  N   LEU A  34     108.862 122.913 161.358  1.00 87.17           N  
ATOM    206  CA  LEU A  34     108.785 122.068 160.173  1.00 85.46           C  
ATOM    207  C   LEU A  34     107.580 122.414 159.311  1.00 83.82           C  
ATOM    208  O   LEU A  34     107.642 122.277 158.088  1.00 81.99           O  
ATOM    209  CB  LEU A  34     108.741 120.595 160.573  1.00 78.95           C  
ATOM    210  CG  LEU A  34     110.070 119.962 160.984  1.00 78.00           C  
ATOM    211  CD1 LEU A  34     110.015 118.456 160.809  1.00 80.24           C  
ATOM    212  CD2 LEU A  34     111.220 120.554 160.192  1.00 78.81           C  
ATOM    213  N   GLY A  35     106.481 122.859 159.921  1.00 83.36           N  
ATOM    214  CA  GLY A  35     105.340 123.288 159.130  1.00 81.34           C  
ATOM    215  C   GLY A  35     105.658 124.503 158.284  1.00 83.04           C  
ATOM    216  O   GLY A  35     105.345 124.547 157.089  1.00 87.44           O  
ATOM    217  N   LEU A  36     106.296 125.505 158.892  1.00 81.78           N  
ATOM    218  CA  LEU A  36     106.714 126.674 158.125  1.00 86.22           C  
ATOM    219  C   LEU A  36     107.696 126.280 157.028  1.00 84.00           C  
ATOM    220  O   LEU A  36     107.602 126.764 155.888  1.00 80.55           O  
ATOM    221  CB  LEU A  36     107.330 127.718 159.055  1.00 88.98           C  
ATOM    222  CG  LEU A  36     106.446 128.911 159.424  1.00 88.98           C  
ATOM    223  CD1 LEU A  36     105.213 128.455 160.188  1.00 86.09           C  
ATOM    224  CD2 LEU A  36     107.233 129.931 160.234  1.00 84.07           C  
ATOM    225  N   GLU A  37     108.641 125.394 157.354  1.00 77.86           N  
ATOM    226  CA  GLU A  37     109.601 124.928 156.360  1.00 73.92           C  
ATOM    227  C   GLU A  37     108.894 124.261 155.192  1.00 72.72           C  
ATOM    228  O   GLU A  37     109.190 124.551 154.032  1.00 75.53           O  
ATOM    229  CB  GLU A  37     110.601 123.958 156.989  1.00 72.55           C  
ATOM    230  CG  GLU A  37     111.315 124.497 158.196  1.00 73.37           C  
ATOM    231  CD  GLU A  37     112.600 125.183 157.839  1.00 76.89           C  
ATOM    232  OE1 GLU A  37     113.329 124.656 156.976  1.00 77.43           O  
ATOM    233  OE2 GLU A  37     112.871 126.258 158.411  1.00 79.50           O  
ATOM    234  N   PHE A  38     107.951 123.365 155.481  1.00 73.85           N  
ATOM    235  CA  PHE A  38     107.279 122.632 154.416  1.00 75.54           C  
ATOM    236  C   PHE A  38     106.463 123.576 153.546  1.00 77.82           C  
ATOM    237  O   PHE A  38     106.534 123.510 152.315  1.00 77.96           O  
ATOM    238  CB  PHE A  38     106.405 121.528 155.014  1.00 77.00           C  
ATOM    239  CG  PHE A  38     105.137 121.266 154.253  1.00 79.75           C  
ATOM    240  CD1 PHE A  38     105.176 120.727 152.978  1.00 79.15           C  
ATOM    241  CD2 PHE A  38     103.906 121.531 154.823  1.00 79.40           C  
ATOM    242  CE1 PHE A  38     104.012 120.479 152.282  1.00 76.84           C  
ATOM    243  CE2 PHE A  38     102.738 121.279 154.131  1.00 78.15           C  
ATOM    244  CZ  PHE A  38     102.792 120.756 152.859  1.00 75.83           C  
ATOM    245  N   ILE A  39     105.711 124.489 154.168  1.00 79.68           N  
ATOM    246  CA  ILE A  39     104.923 125.455 153.401  1.00 79.46           C  
ATOM    247  C   ILE A  39     105.820 126.243 152.453  1.00 79.06           C  
ATOM    248  O   ILE A  39     105.632 126.227 151.227  1.00 76.71           O  
ATOM    249  CB  ILE A  39     104.149 126.396 154.340  1.00 79.09           C  
ATOM    250  CG1 ILE A  39     103.124 125.627 155.176  1.00 77.42           C  
ATOM    251  CG2 ILE A  39     103.472 127.496 153.542  1.00 77.53           C  
ATOM    252  CD1 ILE A  39     102.290 124.661 154.380  1.00 74.82           C  
ATOM    253  N   PHE A  40     106.808 126.950 153.010  1.00 80.86           N  
ATOM    254  CA  PHE A  40     107.610 127.838 152.175  1.00 81.98           C  
ATOM    255  C   PHE A  40     108.436 127.059 151.159  1.00 79.64           C  
ATOM    256  O   PHE A  40     108.565 127.485 150.007  1.00 78.79           O  
ATOM    257  CB  PHE A  40     108.513 128.720 153.033  1.00 81.25           C  
ATOM    258  CG  PHE A  40     109.029 129.931 152.308  1.00 81.07           C  
ATOM    259  CD1 PHE A  40     108.213 131.028 152.099  1.00 77.43           C  
ATOM    260  CD2 PHE A  40     110.324 129.964 151.819  1.00 82.91           C  
ATOM    261  CE1 PHE A  40     108.681 132.139 151.427  1.00 78.49           C  
ATOM    262  CE2 PHE A  40     110.798 131.072 151.146  1.00 80.75           C  
ATOM    263  CZ  PHE A  40     109.976 132.161 150.950  1.00 80.66           C  
ATOM    264  N   GLY A  41     109.008 125.923 151.562  1.00 76.15           N  
ATOM    265  CA  GLY A  41     109.808 125.144 150.638  1.00 77.05           C  
ATOM    266  C   GLY A  41     108.996 124.584 149.490  1.00 74.56           C  
ATOM    267  O   GLY A  41     109.419 124.653 148.336  1.00 76.78           O  
ATOM    268  N   LEU A  42     107.816 124.029 149.782  1.00 80.38           N  
ATOM    269  CA  LEU A  42     106.969 123.510 148.717  1.00 82.66           C  
ATOM    270  C   LEU A  42     106.548 124.625 147.772  1.00 83.79           C  
ATOM    271  O   LEU A  42     106.608 124.466 146.548  1.00 80.09           O  
ATOM    272  CB  LEU A  42     105.751 122.799 149.312  1.00 80.65           C  
ATOM    273  CG  LEU A  42     104.610 122.381 148.379  1.00 81.28           C  
ATOM    274  CD1 LEU A  42     103.999 121.084 148.867  1.00 82.16           C  
ATOM    275  CD2 LEU A  42     103.533 123.452 148.298  1.00 79.85           C  
ATOM    276  N   LEU A  43     106.144 125.777 148.319  1.00 84.64           N  
ATOM    277  CA  LEU A  43     105.727 126.881 147.460  1.00 82.71           C  
ATOM    278  C   LEU A  43     106.874 127.353 146.573  1.00 80.23           C  
ATOM    279  O   LEU A  43     106.726 127.458 145.348  1.00 82.80           O  
ATOM    280  CB  LEU A  43     105.191 128.034 148.308  1.00 81.51           C  
ATOM    281  CG  LEU A  43     103.669 128.151 148.417  1.00 79.97           C  
ATOM    282  CD1 LEU A  43     103.038 128.224 147.036  1.00 78.12           C  
ATOM    283  CD2 LEU A  43     103.089 126.996 149.216  1.00 76.74           C  
ATOM    284  N   GLY A  44     108.033 127.629 147.174  1.00 64.35           N  
ATOM    285  CA  GLY A  44     109.158 128.123 146.401  1.00 61.48           C  
ATOM    286  C   GLY A  44     109.645 127.125 145.371  1.00 71.34           C  
ATOM    287  O   GLY A  44     109.943 127.491 144.233  1.00 75.01           O  
ATOM    288  N   ASN A  45     109.712 125.846 145.744  1.00 72.13           N  
ATOM    289  CA  ASN A  45     110.213 124.836 144.822  1.00 68.52           C  
ATOM    290  C   ASN A  45     109.224 124.568 143.696  1.00 67.71           C  
ATOM    291  O   ASN A  45     109.632 124.324 142.557  1.00 65.26           O  
ATOM    292  CB  ASN A  45     110.539 123.558 145.589  1.00 69.61           C  
ATOM    293  CG  ASN A  45     111.696 123.742 146.548  1.00 65.60           C  
ATOM    294  OD1 ASN A  45     112.074 124.866 146.873  1.00 62.45           O  
ATOM    295  ND2 ASN A  45     112.259 122.639 147.015  1.00 66.32           N  
ATOM    296  N   GLY A  46     107.921 124.616 143.982  1.00 71.40           N  
ATOM    297  CA  GLY A  46     106.946 124.498 142.911  1.00 72.77           C  
ATOM    298  C   GLY A  46     107.018 125.659 141.939  1.00 73.95           C  
ATOM    299  O   GLY A  46     107.038 125.467 140.719  1.00 76.46           O  
ATOM    300  N   LEU A  47     107.075 126.886 142.468  1.00 72.74           N  
ATOM    301  CA  LEU A  47     107.186 128.048 141.595  1.00 72.98           C  
ATOM    302  C   LEU A  47     108.520 128.098 140.865  1.00 72.48           C  
ATOM    303  O   LEU A  47     108.616 128.756 139.826  1.00 70.32           O  
ATOM    304  CB  LEU A  47     106.976 129.338 142.387  1.00 75.81           C  
ATOM    305  CG  LEU A  47     105.663 129.449 143.160  1.00 76.63           C  
ATOM    306  CD1 LEU A  47     105.612 130.748 143.948  1.00 74.08           C  
ATOM    307  CD2 LEU A  47     104.475 129.341 142.216  1.00 74.34           C  
ATOM    308  N   ALA A  48     109.549 127.426 141.383  1.00 73.13           N  
ATOM    309  CA  ALA A  48     110.816 127.353 140.668  1.00 74.62           C  
ATOM    310  C   ALA A  48     110.766 126.305 139.565  1.00 78.56           C  
ATOM    311  O   ALA A  48     111.187 126.564 138.433  1.00 81.58           O  
ATOM    312  CB  ALA A  48     111.953 127.053 141.646  1.00 71.46           C  
ATOM    313  N   LEU A  49     110.242 125.118 139.875  1.00 75.38           N  
ATOM    314  CA  LEU A  49     110.137 124.054 138.885  1.00 77.63           C  
ATOM    315  C   LEU A  49     109.153 124.393 137.776  1.00 73.18           C  
ATOM    316  O   LEU A  49     109.247 123.817 136.687  1.00 69.34           O  
ATOM    317  CB  LEU A  49     109.726 122.745 139.561  1.00 74.57           C  
ATOM    318  CG  LEU A  49     110.800 122.037 140.387  1.00 68.80           C  
ATOM    319  CD1 LEU A  49     110.358 120.634 140.744  1.00 65.73           C  
ATOM    320  CD2 LEU A  49     112.111 122.008 139.635  1.00 66.94           C  
ATOM    321  N   TRP A  50     108.211 125.304 138.027  1.00 73.76           N  
ATOM    322  CA  TRP A  50     107.288 125.709 136.973  1.00 74.93           C  
ATOM    323  C   TRP A  50     108.030 126.322 135.792  1.00 76.05           C  
ATOM    324  O   TRP A  50     107.717 126.026 134.634  1.00 75.37           O  
ATOM    325  CB  TRP A  50     106.261 126.692 137.529  1.00 79.27           C  
ATOM    326  CG  TRP A  50     105.023 126.800 136.702  1.00 80.08           C  
ATOM    327  CD1 TRP A  50     104.930 127.255 135.420  1.00 75.83           C  
ATOM    328  CD2 TRP A  50     103.693 126.453 137.103  1.00 81.20           C  
ATOM    329  NE1 TRP A  50     103.625 127.208 134.996  1.00 81.89           N  
ATOM    330  CE2 TRP A  50     102.845 126.720 136.011  1.00 85.24           C  
ATOM    331  CE3 TRP A  50     103.137 125.941 138.279  1.00 77.57           C  
ATOM    332  CZ2 TRP A  50     101.472 126.492 136.060  1.00 82.40           C  
ATOM    333  CZ3 TRP A  50     101.775 125.716 138.326  1.00 79.43           C  
ATOM    334  CH2 TRP A  50     100.958 125.991 137.223  1.00 80.79           C  
ATOM    335  N   ILE A  51     109.016 127.179 136.064  1.00 70.81           N  
ATOM    336  CA  ILE A  51     109.762 127.817 134.982  1.00 73.76           C  
ATOM    337  C   ILE A  51     110.601 126.793 134.228  1.00 71.64           C  
ATOM    338  O   ILE A  51     110.596 126.756 132.992  1.00 75.68           O  
ATOM    339  CB  ILE A  51     110.628 128.968 135.523  1.00 67.03           C  
ATOM    340  CG1 ILE A  51     109.748 130.154 135.920  1.00 69.21           C  
ATOM    341  CG2 ILE A  51     111.659 129.392 134.492  1.00 65.55           C  
ATOM    342  CD1 ILE A  51     109.616 130.355 137.401  1.00 68.00           C  
ATOM    343  N   PHE A  52     111.328 125.943 134.956  1.00 57.63           N  
ATOM    344  CA  PHE A  52     112.197 124.972 134.299  1.00 61.27           C  
ATOM    345  C   PHE A  52     111.397 124.014 133.428  1.00 62.97           C  
ATOM    346  O   PHE A  52     111.815 123.676 132.314  1.00 58.47           O  
ATOM    347  CB  PHE A  52     113.004 124.196 135.339  1.00 62.30           C  
ATOM    348  CG  PHE A  52     113.892 125.056 136.187  1.00 60.97           C  
ATOM    349  CD1 PHE A  52     114.932 125.771 135.620  1.00 64.39           C  
ATOM    350  CD2 PHE A  52     113.696 125.141 137.552  1.00 60.12           C  
ATOM    351  CE1 PHE A  52     115.752 126.561 136.399  1.00 60.75           C  
ATOM    352  CE2 PHE A  52     114.511 125.929 138.334  1.00 63.12           C  
ATOM    353  CZ  PHE A  52     115.541 126.640 137.757  1.00 59.25           C  
ATOM    354  N   CYS A  53     110.241 123.568 133.918  1.00 72.79           N  
ATOM    355  CA  CYS A  53     109.464 122.576 133.185  1.00 78.66           C  
ATOM    356  C   CYS A  53     108.756 123.189 131.983  1.00 73.90           C  
ATOM    357  O   CYS A  53     108.648 122.551 130.930  1.00 72.91           O  
ATOM    358  CB  CYS A  53     108.453 121.911 134.121  1.00 76.76           C  
ATOM    359  SG  CYS A  53     109.175 120.765 135.319  1.00 63.48           S  
ATOM    360  N   PHE A  54     108.264 124.421 132.114  1.00 64.48           N  
ATOM    361  CA  PHE A  54     107.373 124.987 131.107  1.00 66.93           C  
ATOM    362  C   PHE A  54     107.963 126.191 130.384  1.00 62.89           C  
ATOM    363  O   PHE A  54     108.067 126.167 129.154  1.00 59.48           O  
ATOM    364  CB  PHE A  54     106.036 125.359 131.761  1.00 70.19           C  
ATOM    365  CG  PHE A  54     105.383 124.224 132.493  1.00 65.46           C  
ATOM    366  CD1 PHE A  54     104.981 123.088 131.815  1.00 63.04           C  
ATOM    367  CD2 PHE A  54     105.163 124.297 133.856  1.00 62.65           C  
ATOM    368  CE1 PHE A  54     104.376 122.045 132.484  1.00 64.26           C  
ATOM    369  CE2 PHE A  54     104.559 123.257 134.530  1.00 62.12           C  
ATOM    370  CZ  PHE A  54     104.165 122.129 133.844  1.00 61.18           C  
ATOM    371  N   HIS A  55     108.355 127.245 131.098  1.00 55.22           N  
ATOM    372  CA  HIS A  55     108.622 128.529 130.464  1.00 56.65           C  
ATOM    373  C   HIS A  55     110.098 128.915 130.485  1.00 51.92           C  
ATOM    374  O   HIS A  55     110.421 130.105 130.502  1.00 47.84           O  
ATOM    375  CB  HIS A  55     107.775 129.623 131.115  1.00 54.85           C  
ATOM    376  CG  HIS A  55     107.130 130.548 130.130  1.00 59.53           C  
ATOM    377  ND1 HIS A  55     107.817 131.107 129.074  1.00 64.89           N  
ATOM    378  CD2 HIS A  55     105.857 130.996 130.029  1.00 57.46           C  
ATOM    379  CE1 HIS A  55     106.997 131.867 128.371  1.00 58.11           C  
ATOM    380  NE2 HIS A  55     105.801 131.817 128.930  1.00 53.65           N  
ATOM    381  N   LEU A  56     110.998 127.938 130.481  1.00 61.81           N  
ATOM    382  CA  LEU A  56     112.427 128.188 130.325  1.00 65.03           C  
ATOM    383  C   LEU A  56     112.835 127.731 128.928  1.00 72.83           C  
ATOM    384  O   LEU A  56     112.880 126.529 128.650  1.00 75.24           O  
ATOM    385  CB  LEU A  56     113.232 127.464 131.402  1.00 64.31           C  
ATOM    386  CG  LEU A  56     114.741 127.711 131.416  1.00 65.99           C  
ATOM    387  CD1 LEU A  56     115.059 129.033 132.091  1.00 65.95           C  
ATOM    388  CD2 LEU A  56     115.462 126.571 132.108  1.00 66.62           C  
ATOM    389  N   LYS A  57     113.135 128.688 128.054  1.00 65.54           N  
ATOM    390  CA  LYS A  57     113.434 128.392 126.660  1.00 62.80           C  
ATOM    391  C   LYS A  57     114.906 128.092 126.409  1.00 61.45           C  
ATOM    392  O   LYS A  57     115.274 127.790 125.270  1.00 57.11           O  
ATOM    393  CB  LYS A  57     112.990 129.557 125.772  1.00 62.39           C  
ATOM    394  N   SER A  58     115.751 128.165 127.433  1.00 68.80           N  
ATOM    395  CA  SER A  58     117.163 127.832 127.321  1.00 71.13           C  
ATOM    396  C   SER A  58     117.509 126.797 128.385  1.00 72.95           C  
ATOM    397  O   SER A  58     116.639 126.318 129.118  1.00 72.13           O  
ATOM    398  CB  SER A  58     118.041 129.082 127.461  1.00 68.96           C  
ATOM    399  N   TRP A  59     118.792 126.444 128.470  1.00 67.54           N  
ATOM    400  CA  TRP A  59     119.229 125.486 129.479  1.00 65.86           C  
ATOM    401  C   TRP A  59     120.684 125.700 129.880  1.00 67.31           C  
ATOM    402  O   TRP A  59     120.979 126.564 130.709  1.00 64.43           O  
ATOM    403  CB  TRP A  59     119.020 124.057 128.980  1.00 59.06           C  
ATOM    404  CG  TRP A  59     117.666 123.518 129.320  1.00 65.16           C  
ATOM    405  CD1 TRP A  59     116.639 123.281 128.456  1.00 69.27           C  
ATOM    406  CD2 TRP A  59     117.184 123.168 130.622  1.00 64.27           C  
ATOM    407  NE1 TRP A  59     115.550 122.796 129.138  1.00 72.53           N  
ATOM    408  CE2 TRP A  59     115.861 122.717 130.470  1.00 69.67           C  
ATOM    409  CE3 TRP A  59     117.746 123.189 131.901  1.00 60.89           C  
ATOM    410  CZ2 TRP A  59     115.091 122.288 131.549  1.00 68.09           C  
ATOM    411  CZ3 TRP A  59     116.981 122.761 132.969  1.00 56.04           C  
ATOM    412  CH2 TRP A  59     115.669 122.318 132.787  1.00 57.48           C  
ATOM    413  N   LYS A  60     121.586 124.897 129.310  1.00 63.53           N  
ATOM    414  CA  LYS A  60     123.018 124.915 129.604  1.00 65.21           C  
ATOM    415  C   LYS A  60     123.326 124.338 130.984  1.00 64.94           C  
ATOM    416  O   LYS A  60     122.419 124.067 131.781  1.00 68.05           O  
ATOM    417  CB  LYS A  60     123.595 126.329 129.478  1.00 68.03           C  
ATOM    418  CG  LYS A  60     123.459 126.932 128.090  1.00 66.97           C  
ATOM    419  CD  LYS A  60     123.552 128.449 128.135  1.00 67.70           C  
ATOM    420  CE  LYS A  60     122.271 129.067 128.674  1.00 65.05           C  
ATOM    421  NZ  LYS A  60     122.010 130.411 128.090  1.00 63.03           N  
ATOM    422  N   SER A  61     124.619 124.159 131.264  1.00 50.58           N  
ATOM    423  CA  SER A  61     125.045 123.343 132.397  1.00 56.29           C  
ATOM    424  C   SER A  61     124.615 123.939 133.732  1.00 63.94           C  
ATOM    425  O   SER A  61     124.195 123.207 134.638  1.00 69.77           O  
ATOM    426  CB  SER A  61     126.561 123.164 132.356  1.00 61.95           C  
ATOM    427  OG  SER A  61     127.096 123.055 133.661  1.00 70.90           O  
ATOM    428  N   SER A  62     124.742 125.257 133.891  1.00 55.66           N  
ATOM    429  CA  SER A  62     124.422 125.865 135.177  1.00 55.67           C  
ATOM    430  C   SER A  62     122.942 125.719 135.506  1.00 63.86           C  
ATOM    431  O   SER A  62     122.579 125.421 136.651  1.00 67.07           O  
ATOM    432  CB  SER A  62     124.836 127.333 135.181  1.00 60.15           C  
ATOM    433  OG  SER A  62     126.131 127.483 135.735  1.00 62.12           O  
ATOM    434  N   ARG A  63     122.071 125.910 134.515  1.00 57.66           N  
ATOM    435  CA  ARG A  63     120.649 125.702 134.763  1.00 53.55           C  
ATOM    436  C   ARG A  63     120.324 124.227 134.948  1.00 57.73           C  
ATOM    437  O   ARG A  63     119.399 123.895 135.694  1.00 58.89           O  
ATOM    438  CB  ARG A  63     119.812 126.309 133.640  1.00 57.60           C  
ATOM    439  CG  ARG A  63     119.504 127.787 133.849  1.00 65.39           C  
ATOM    440  CD  ARG A  63     119.569 128.575 132.553  1.00 68.56           C  
ATOM    441  NE  ARG A  63     119.522 130.015 132.780  1.00 74.38           N  
ATOM    442  CZ  ARG A  63     119.361 130.918 131.822  1.00 69.82           C  
ATOM    443  NH1 ARG A  63     119.222 130.564 130.555  1.00 66.89           N  
ATOM    444  NH2 ARG A  63     119.339 132.208 132.144  1.00 59.75           N  
ATOM    445  N   ILE A  64     121.078 123.330 134.306  1.00 49.46           N  
ATOM    446  CA  ILE A  64     120.924 121.901 134.584  1.00 47.08           C  
ATOM    447  C   ILE A  64     121.175 121.620 136.061  1.00 51.23           C  
ATOM    448  O   ILE A  64     120.387 120.939 136.734  1.00 53.10           O  
ATOM    449  CB  ILE A  64     121.871 121.076 133.693  1.00 41.79           C  
ATOM    450  CG1 ILE A  64     121.389 121.067 132.243  1.00 47.81           C  
ATOM    451  CG2 ILE A  64     121.996 119.661 134.218  1.00 41.56           C  
ATOM    452  CD1 ILE A  64     119.978 120.571 132.080  1.00 46.43           C  
ATOM    453  N   PHE A  65     122.280 122.148 136.586  1.00 39.32           N  
ATOM    454  CA  PHE A  65     122.631 121.902 137.980  1.00 30.97           C  
ATOM    455  C   PHE A  65     121.629 122.547 138.929  1.00 38.00           C  
ATOM    456  O   PHE A  65     121.280 121.964 139.962  1.00 53.57           O  
ATOM    457  CB  PHE A  65     124.045 122.402 138.256  1.00 31.27           C  
ATOM    458  CG  PHE A  65     125.107 121.595 137.578  1.00 30.01           C  
ATOM    459  CD1 PHE A  65     125.044 120.217 137.574  1.00 36.08           C  
ATOM    460  CD2 PHE A  65     126.165 122.213 136.941  1.00 32.59           C  
ATOM    461  CE1 PHE A  65     126.016 119.470 136.949  1.00 38.13           C  
ATOM    462  CE2 PHE A  65     127.139 121.469 136.315  1.00 32.44           C  
ATOM    463  CZ  PHE A  65     127.063 120.095 136.320  1.00 36.30           C  
ATOM    464  N   LEU A  66     121.153 123.749 138.599  1.00 42.39           N  
ATOM    465  CA  LEU A  66     120.132 124.384 139.428  1.00 45.89           C  
ATOM    466  C   LEU A  66     118.836 123.580 139.421  1.00 48.21           C  
ATOM    467  O   LEU A  66     118.160 123.468 140.449  1.00 54.64           O  
ATOM    468  CB  LEU A  66     119.881 125.813 138.953  1.00 50.48           C  
ATOM    469  CG  LEU A  66     120.975 126.824 139.284  1.00 45.82           C  
ATOM    470  CD1 LEU A  66     120.626 128.188 138.723  1.00 42.48           C  
ATOM    471  CD2 LEU A  66     121.174 126.896 140.781  1.00 52.16           C  
ATOM    472  N   PHE A  67     118.470 123.020 138.267  1.00 37.78           N  
ATOM    473  CA  PHE A  67     117.288 122.168 138.199  1.00 42.88           C  
ATOM    474  C   PHE A  67     117.452 120.935 139.073  1.00 46.54           C  
ATOM    475  O   PHE A  67     116.510 120.519 139.755  1.00 53.38           O  
ATOM    476  CB  PHE A  67     117.021 121.763 136.751  1.00 49.78           C  
ATOM    477  CG  PHE A  67     115.844 120.849 136.584  1.00 46.79           C  
ATOM    478  CD1 PHE A  67     114.614 121.174 137.123  1.00 48.98           C  
ATOM    479  CD2 PHE A  67     115.969 119.664 135.883  1.00 46.49           C  
ATOM    480  CE1 PHE A  67     113.532 120.336 136.966  1.00 45.40           C  
ATOM    481  CE2 PHE A  67     114.891 118.823 135.724  1.00 51.96           C  
ATOM    482  CZ  PHE A  67     113.670 119.159 136.268  1.00 48.86           C  
ATOM    483  N   ASN A  68     118.641 120.329 139.059  1.00 45.19           N  
ATOM    484  CA  ASN A  68     118.878 119.177 139.924  1.00 44.43           C  
ATOM    485  C   ASN A  68     118.785 119.560 141.396  1.00 41.43           C  
ATOM    486  O   ASN A  68     118.228 118.813 142.211  1.00 38.82           O  
ATOM    487  CB  ASN A  68     120.236 118.557 139.620  1.00 37.78           C  
ATOM    488  CG  ASN A  68     120.162 117.520 138.534  1.00 43.89           C  
ATOM    489  OD1 ASN A  68     119.094 117.248 137.990  1.00 54.85           O  
ATOM    490  ND2 ASN A  68     121.291 116.916 138.225  1.00 36.81           N  
ATOM    491  N   LEU A  69     119.333 120.722 141.754  1.00 42.31           N  
ATOM    492  CA  LEU A  69     119.227 121.203 143.127  1.00 38.18           C  
ATOM    493  C   LEU A  69     117.770 121.391 143.529  1.00 52.15           C  
ATOM    494  O   LEU A  69     117.365 121.019 144.640  1.00 61.96           O  
ATOM    495  CB  LEU A  69     119.992 122.516 143.268  1.00 37.44           C  
ATOM    496  CG  LEU A  69     120.724 122.818 144.569  1.00 37.08           C  
ATOM    497  CD1 LEU A  69     121.699 123.952 144.340  1.00 45.03           C  
ATOM    498  CD2 LEU A  69     119.739 123.174 145.654  1.00 43.31           C  
ATOM    499  N   ALA A  70     116.968 121.973 142.635  1.00 41.55           N  
ATOM    500  CA  ALA A  70     115.552 122.171 142.920  1.00 34.63           C  
ATOM    501  C   ALA A  70     114.827 120.841 143.063  1.00 45.38           C  
ATOM    502  O   ALA A  70     113.952 120.698 143.920  1.00 49.71           O  
ATOM    503  CB  ALA A  70     114.908 123.018 141.825  1.00 44.01           C  
ATOM    504  N   VAL A  71     115.174 119.858 142.231  1.00 52.51           N  
ATOM    505  CA  VAL A  71     114.565 118.533 142.346  1.00 56.41           C  
ATOM    506  C   VAL A  71     114.880 117.923 143.706  1.00 56.49           C  
ATOM    507  O   VAL A  71     114.000 117.370 144.382  1.00 57.53           O  
ATOM    508  CB  VAL A  71     115.041 117.622 141.201  1.00 46.36           C  
ATOM    509  CG1 VAL A  71     114.725 116.174 141.510  1.00 44.91           C  
ATOM    510  CG2 VAL A  71     114.394 118.031 139.896  1.00 46.17           C  
ATOM    511  N   ALA A  72     116.145 118.015 144.123  1.00 50.87           N  
ATOM    512  CA  ALA A  72     116.543 117.455 145.411  1.00 46.53           C  
ATOM    513  C   ALA A  72     115.786 118.120 146.553  1.00 49.81           C  
ATOM    514  O   ALA A  72     115.208 117.442 147.413  1.00 64.32           O  
ATOM    515  CB  ALA A  72     118.051 117.604 145.602  1.00 46.71           C  
ATOM    516  N   ASP A  73     115.754 119.453 146.562  1.00 41.28           N  
ATOM    517  CA  ASP A  73     115.060 120.159 147.633  1.00 48.20           C  
ATOM    518  C   ASP A  73     113.562 119.875 147.607  1.00 49.54           C  
ATOM    519  O   ASP A  73     112.924 119.781 148.662  1.00 54.44           O  
ATOM    520  CB  ASP A  73     115.331 121.658 147.533  1.00 59.95           C  
ATOM    521  CG  ASP A  73     116.650 122.052 148.163  1.00 60.86           C  
ATOM    522  OD1 ASP A  73     117.303 121.174 148.762  1.00 52.64           O  
ATOM    523  OD2 ASP A  73     117.034 123.236 148.059  1.00 62.63           O  
ATOM    524  N   PHE A  74     112.983 119.739 146.412  1.00 42.18           N  
ATOM    525  CA  PHE A  74     111.558 119.455 146.292  1.00 50.48           C  
ATOM    526  C   PHE A  74     111.224 118.100 146.897  1.00 59.61           C  
ATOM    527  O   PHE A  74     110.282 117.972 147.689  1.00 66.29           O  
ATOM    528  CB  PHE A  74     111.149 119.500 144.820  1.00 50.96           C  
ATOM    529  CG  PHE A  74     109.678 119.313 144.586  1.00 56.86           C  
ATOM    530  CD1 PHE A  74     108.751 119.732 145.524  1.00 56.26           C  
ATOM    531  CD2 PHE A  74     109.223 118.698 143.435  1.00 57.35           C  
ATOM    532  CE1 PHE A  74     107.399 119.563 145.308  1.00 54.95           C  
ATOM    533  CE2 PHE A  74     107.872 118.520 143.215  1.00 61.65           C  
ATOM    534  CZ  PHE A  74     106.959 118.952 144.155  1.00 62.23           C  
ATOM    535  N   LEU A  75     111.990 117.071 146.533  1.00 56.69           N  
ATOM    536  CA  LEU A  75     111.774 115.765 147.142  1.00 53.51           C  
ATOM    537  C   LEU A  75     111.972 115.836 148.652  1.00 45.43           C  
ATOM    538  O   LEU A  75     111.240 115.196 149.417  1.00 44.20           O  
ATOM    539  CB  LEU A  75     112.705 114.732 146.509  1.00 47.32           C  
ATOM    540  CG  LEU A  75     112.507 114.423 145.026  1.00 47.71           C  
ATOM    541  CD1 LEU A  75     113.821 114.000 144.401  1.00 43.02           C  
ATOM    542  CD2 LEU A  75     111.460 113.342 144.839  1.00 52.80           C  
ATOM    543  N   LEU A  76     112.927 116.652 149.103  1.00 39.75           N  
ATOM    544  CA  LEU A  76     113.179 116.757 150.536  1.00 39.38           C  
ATOM    545  C   LEU A  76     111.974 117.344 151.268  1.00 49.35           C  
ATOM    546  O   LEU A  76     111.556 116.822 152.309  1.00 54.00           O  
ATOM    547  CB  LEU A  76     114.433 117.602 150.773  1.00 50.05           C  
ATOM    548  CG  LEU A  76     115.320 117.370 152.002  1.00 41.96           C  
ATOM    549  CD1 LEU A  76     116.577 118.217 151.897  1.00 40.14           C  
ATOM    550  CD2 LEU A  76     114.615 117.643 153.304  1.00 42.64           C  
ATOM    551  N   ILE A  77     111.379 118.413 150.733  1.00 59.60           N  
ATOM    552  CA  ILE A  77     110.324 119.053 151.518  1.00 59.40           C  
ATOM    553  C   ILE A  77     108.985 118.357 151.301  1.00 57.40           C  
ATOM    554  O   ILE A  77     108.044 118.560 152.076  1.00 62.79           O  
ATOM    555  CB  ILE A  77     110.236 120.574 151.264  1.00 62.05           C  
ATOM    556  CG1 ILE A  77     110.413 120.970 149.799  1.00 62.11           C  
ATOM    557  CG2 ILE A  77     111.256 121.308 152.124  1.00 61.36           C  
ATOM    558  CD1 ILE A  77     109.294 120.532 148.898  1.00 64.78           C  
ATOM    559  N   ILE A  78     108.859 117.525 150.262  1.00 45.71           N  
ATOM    560  CA  ILE A  78     107.711 116.621 150.249  1.00 53.65           C  
ATOM    561  C   ILE A  78     107.936 115.457 151.198  1.00 64.58           C  
ATOM    562  O   ILE A  78     106.972 114.818 151.633  1.00 64.49           O  
ATOM    563  CB  ILE A  78     107.371 116.105 148.832  1.00 55.81           C  
ATOM    564  CG1 ILE A  78     108.309 114.968 148.415  1.00 52.66           C  
ATOM    565  CG2 ILE A  78     107.334 117.243 147.835  1.00 59.68           C  
ATOM    566  CD1 ILE A  78     108.283 114.666 146.936  1.00 56.99           C  
ATOM    567  N   CYS A  79     109.194 115.152 151.524  1.00 67.23           N  
ATOM    568  CA  CYS A  79     109.471 114.169 152.564  1.00 53.39           C  
ATOM    569  C   CYS A  79     109.229 114.733 153.961  1.00 56.31           C  
ATOM    570  O   CYS A  79     108.933 113.971 154.888  1.00 51.82           O  
ATOM    571  CB  CYS A  79     110.908 113.669 152.427  1.00 51.64           C  
ATOM    572  SG  CYS A  79     111.489 112.635 153.775  1.00 61.54           S  
ATOM    573  N   LEU A  80     109.349 116.052 154.122  1.00 64.55           N  
ATOM    574  CA  LEU A  80     109.170 116.687 155.432  1.00 62.86           C  
ATOM    575  C   LEU A  80     107.899 116.302 156.186  1.00 61.85           C  
ATOM    576  O   LEU A  80     108.010 115.948 157.369  1.00 62.59           O  
ATOM    577  CB  LEU A  80     109.215 118.217 155.303  1.00 63.07           C  
ATOM    578  CG  LEU A  80     110.486 118.977 155.684  1.00 63.04           C  
ATOM    579  CD1 LEU A  80     110.855 118.639 157.117  1.00 64.71           C  
ATOM    580  CD2 LEU A  80     111.633 118.683 154.771  1.00 62.49           C  
ATOM    581  N   PRO A  81     106.690 116.355 155.605  1.00 64.39           N  
ATOM    582  CA  PRO A  81     105.480 116.257 156.450  1.00 68.89           C  
ATOM    583  C   PRO A  81     105.389 114.989 157.288  1.00 70.86           C  
ATOM    584  O   PRO A  81     104.896 115.035 158.424  1.00 69.46           O  
ATOM    585  CB  PRO A  81     104.337 116.344 155.428  1.00 68.01           C  
ATOM    586  CG  PRO A  81     104.925 117.045 154.264  1.00 65.18           C  
ATOM    587  CD  PRO A  81     106.338 116.569 154.190  1.00 62.85           C  
ATOM    588  N   PHE A  82     105.842 113.851 156.762  1.00 71.50           N  
ATOM    589  CA  PHE A  82     105.830 112.631 157.561  1.00 69.11           C  
ATOM    590  C   PHE A  82     106.772 112.748 158.753  1.00 71.51           C  
ATOM    591  O   PHE A  82     106.435 112.323 159.865  1.00 77.80           O  
ATOM    592  CB  PHE A  82     106.196 111.436 156.685  1.00 69.24           C  
ATOM    593  CG  PHE A  82     105.408 111.366 155.411  1.00 70.96           C  
ATOM    594  CD1 PHE A  82     104.117 110.866 155.408  1.00 69.66           C  
ATOM    595  CD2 PHE A  82     105.952 111.811 154.220  1.00 74.18           C  
ATOM    596  CE1 PHE A  82     103.388 110.805 154.241  1.00 71.62           C  
ATOM    597  CE2 PHE A  82     105.227 111.752 153.050  1.00 74.23           C  
ATOM    598  CZ  PHE A  82     103.943 111.249 153.060  1.00 74.39           C  
ATOM    599  N   LEU A  83     107.951 113.334 158.542  1.00 64.26           N  
ATOM    600  CA  LEU A  83     108.864 113.588 159.650  1.00 61.62           C  
ATOM    601  C   LEU A  83     108.244 114.546 160.657  1.00 62.99           C  
ATOM    602  O   LEU A  83     108.442 114.405 161.870  1.00 62.38           O  
ATOM    603  CB  LEU A  83     110.179 114.147 159.111  1.00 61.05           C  
ATOM    604  CG  LEU A  83     111.315 114.361 160.106  1.00 63.19           C  
ATOM    605  CD1 LEU A  83     111.815 113.032 160.646  1.00 57.29           C  
ATOM    606  CD2 LEU A  83     112.441 115.147 159.457  1.00 68.16           C  
ATOM    607  N   MET A  84     107.495 115.534 160.166  1.00 79.11           N  
ATOM    608  CA  MET A  84     106.794 116.460 161.048  1.00 76.17           C  
ATOM    609  C   MET A  84     105.803 115.721 161.935  1.00 77.32           C  
ATOM    610  O   MET A  84     105.728 115.969 163.143  1.00 75.95           O  
ATOM    611  CB  MET A  84     106.077 117.523 160.218  1.00 77.00           C  
ATOM    612  CG  MET A  84     105.336 118.560 161.036  1.00 81.32           C  
ATOM    613  SD  MET A  84     104.882 119.991 160.042  1.00 93.90           S  
ATOM    614  CE  MET A  84     103.213 120.299 160.613  1.00 82.63           C  
ATOM    615  N   ASP A  85     105.033 114.804 161.348  1.00 83.56           N  
ATOM    616  CA  ASP A  85     104.103 114.007 162.143  1.00 86.09           C  
ATOM    617  C   ASP A  85     104.844 113.141 163.155  1.00 81.73           C  
ATOM    618  O   ASP A  85     104.398 112.987 164.301  1.00 80.79           O  
ATOM    619  CB  ASP A  85     103.238 113.135 161.237  1.00 82.19           C  
ATOM    620  CG  ASP A  85     102.656 111.941 161.969  1.00 82.42           C  
ATOM    621  OD1 ASP A  85     101.548 112.069 162.531  1.00 83.15           O  
ATOM    622  OD2 ASP A  85     103.309 110.877 161.991  1.00 78.00           O  
ATOM    623  N   ASN A  86     105.970 112.555 162.741  1.00 69.20           N  
ATOM    624  CA  ASN A  86     106.761 111.738 163.655  1.00 73.04           C  
ATOM    625  C   ASN A  86     107.223 112.552 164.854  1.00 77.61           C  
ATOM    626  O   ASN A  86     107.173 112.077 165.994  1.00 78.06           O  
ATOM    627  CB  ASN A  86     107.960 111.140 162.923  1.00 74.24           C  
ATOM    628  CG  ASN A  86     108.867 110.351 163.841  1.00 70.74           C  
ATOM    629  OD1 ASN A  86     108.403 109.670 164.754  1.00 68.79           O  
ATOM    630  ND2 ASN A  86     110.170 110.443 163.605  1.00 69.75           N  
ATOM    631  N   TYR A  87     107.681 113.781 164.616  1.00 76.87           N  
ATOM    632  CA  TYR A  87     108.024 114.661 165.728  1.00 70.99           C  
ATOM    633  C   TYR A  87     106.798 114.980 166.572  1.00 74.48           C  
ATOM    634  O   TYR A  87     106.877 115.011 167.805  1.00 77.47           O  
ATOM    635  CB  TYR A  87     108.666 115.949 165.217  1.00 71.02           C  
ATOM    636  CG  TYR A  87     110.103 115.795 164.787  1.00 67.99           C  
ATOM    637  CD1 TYR A  87     110.495 116.083 163.491  1.00 70.78           C  
ATOM    638  CD2 TYR A  87     111.069 115.356 165.680  1.00 70.96           C  
ATOM    639  CE1 TYR A  87     111.807 115.947 163.098  1.00 71.46           C  
ATOM    640  CE2 TYR A  87     112.383 115.212 165.293  1.00 74.08           C  
ATOM    641  CZ  TYR A  87     112.746 115.508 164.000  1.00 74.54           C  
ATOM    642  OH  TYR A  87     114.054 115.368 163.605  1.00 80.37           O  
ATOM    643  N   VAL A  88     105.656 115.217 165.923  1.00 82.54           N  
ATOM    644  CA  VAL A  88     104.447 115.606 166.646  1.00 83.45           C  
ATOM    645  C   VAL A  88     104.062 114.532 167.652  1.00 83.62           C  
ATOM    646  O   VAL A  88     103.772 114.822 168.819  1.00 85.45           O  
ATOM    647  CB  VAL A  88     103.296 115.883 165.662  1.00 81.12           C  
ATOM    648  CG1 VAL A  88     101.954 115.786 166.371  1.00 78.01           C  
ATOM    649  CG2 VAL A  88     103.458 117.244 165.024  1.00 81.63           C  
ATOM    650  N   ARG A  89     104.071 113.274 167.224  1.00 89.96           N  
ATOM    651  CA  ARG A  89     103.613 112.202 168.097  1.00 93.42           C  
ATOM    652  C   ARG A  89     104.712 111.705 169.048  1.00 91.89           C  
ATOM    653  O   ARG A  89     104.576 110.626 169.638  1.00 94.27           O  
ATOM    654  CB  ARG A  89     103.041 111.058 167.250  1.00 89.75           C  
ATOM    655  CG  ARG A  89     102.147 110.057 167.991  1.00 87.81           C  
ATOM    656  CD  ARG A  89     101.193 110.702 169.000  1.00 92.88           C  
ATOM    657  NE  ARG A  89     100.541 111.909 168.504  1.00 99.39           N  
ATOM    658  CZ  ARG A  89      99.695 112.646 169.212  1.00 96.00           C  
ATOM    659  NH1 ARG A  89      99.375 112.327 170.455  1.00 93.19           N  
ATOM    660  NH2 ARG A  89      99.160 113.731 168.660  1.00 91.20           N  
ATOM    661  N   ARG A  90     105.782 112.485 169.222  1.00 85.63           N  
ATOM    662  CA  ARG A  90     106.843 112.199 170.191  1.00 89.16           C  
ATOM    663  C   ARG A  90     107.501 110.843 169.918  1.00 90.39           C  
ATOM    664  O   ARG A  90     107.431 109.913 170.724  1.00 86.69           O  
ATOM    665  CB  ARG A  90     106.307 112.273 171.625  1.00 87.68           C  
ATOM    666  CG  ARG A  90     107.389 112.392 172.686  1.00 87.88           C  
ATOM    667  CD  ARG A  90     107.161 113.596 173.580  1.00 86.99           C  
ATOM    668  NE  ARG A  90     106.126 113.341 174.575  1.00 89.48           N  
ATOM    669  CZ  ARG A  90     106.291 112.588 175.654  1.00 88.37           C  
ATOM    670  NH1 ARG A  90     107.448 112.005 175.921  1.00 88.57           N  
ATOM    671  NH2 ARG A  90     105.269 112.419 176.489  1.00 86.91           N  
ATOM    672  N   TRP A  91     108.146 110.753 168.756  1.00 82.33           N  
ATOM    673  CA  TRP A  91     108.881 109.556 168.348  1.00 75.35           C  
ATOM    674  C   TRP A  91     107.993 108.315 168.408  1.00 81.39           C  
ATOM    675  O   TRP A  91     108.326 107.305 169.030  1.00 89.36           O  
ATOM    676  CB  TRP A  91     110.139 109.373 169.197  1.00 76.02           C  
ATOM    677  CG  TRP A  91     111.128 110.488 169.055  1.00 82.33           C  
ATOM    678  CD1 TRP A  91     111.534 111.352 170.028  1.00 83.11           C  
ATOM    679  CD2 TRP A  91     111.842 110.856 167.869  1.00 84.47           C  
ATOM    680  NE1 TRP A  91     112.455 112.236 169.523  1.00 81.25           N  
ATOM    681  CE2 TRP A  91     112.661 111.953 168.199  1.00 82.20           C  
ATOM    682  CE3 TRP A  91     111.868 110.366 166.561  1.00 82.47           C  
ATOM    683  CZ2 TRP A  91     113.495 112.566 167.269  1.00 78.33           C  
ATOM    684  CZ3 TRP A  91     112.696 110.976 165.641  1.00 78.35           C  
ATOM    685  CH2 TRP A  91     113.498 112.064 165.999  1.00 75.33           C  
ATOM    686  N   ASP A  92     106.841 108.406 167.751  1.00 82.39           N  
ATOM    687  CA  ASP A  92     105.845 107.340 167.694  1.00 81.20           C  
ATOM    688  C   ASP A  92     105.455 107.072 166.249  1.00 77.40           C  
ATOM    689  O   ASP A  92     104.280 107.067 165.879  1.00 84.59           O  
ATOM    690  CB  ASP A  92     104.621 107.677 168.535  1.00 85.69           C  
ATOM    691  CG  ASP A  92     104.632 106.984 169.882  1.00 89.34           C  
ATOM    692  OD1 ASP A  92     105.539 106.159 170.119  1.00 89.75           O  
ATOM    693  OD2 ASP A  92     103.733 107.263 170.703  1.00 90.64           O  
ATOM    694  N   TRP A  93     106.462 106.850 165.409  1.00 60.84           N  
ATOM    695  CA  TRP A  93     106.268 106.693 163.975  1.00 66.36           C  
ATOM    696  C   TRP A  93     105.522 105.394 163.701  1.00 69.25           C  
ATOM    697  O   TRP A  93     106.126 104.320 163.626  1.00 71.93           O  
ATOM    698  CB  TRP A  93     107.637 106.724 163.288  1.00 63.69           C  
ATOM    699  CG  TRP A  93     107.699 106.279 161.863  1.00 59.38           C  
ATOM    700  CD1 TRP A  93     107.742 105.000 161.403  1.00 61.73           C  
ATOM    701  CD2 TRP A  93     107.805 107.120 160.712  1.00 57.15           C  
ATOM    702  NE1 TRP A  93     107.835 104.988 160.035  1.00 61.27           N  
ATOM    703  CE2 TRP A  93     107.876 106.280 159.586  1.00 59.28           C  
ATOM    704  CE3 TRP A  93     107.829 108.501 160.524  1.00 57.17           C  
ATOM    705  CZ2 TRP A  93     107.973 106.777 158.292  1.00 62.76           C  
ATOM    706  CZ3 TRP A  93     107.917 108.991 159.242  1.00 59.45           C  
ATOM    707  CH2 TRP A  93     107.991 108.134 158.141  1.00 64.15           C  
ATOM    708  N   LYS A  94     104.198 105.480 163.605  1.00 79.09           N  
ATOM    709  CA  LYS A  94     103.345 104.304 163.430  1.00 81.87           C  
ATOM    710  C   LYS A  94     102.914 104.146 161.973  1.00 83.12           C  
ATOM    711  O   LYS A  94     101.733 104.229 161.637  1.00 87.07           O  
ATOM    712  CB  LYS A  94     102.135 104.395 164.354  1.00 84.77           C  
ATOM    713  CG  LYS A  94     101.553 105.795 164.469  1.00 83.12           C  
ATOM    714  CD  LYS A  94     100.768 105.968 165.759  1.00 86.46           C  
ATOM    715  CE  LYS A  94     101.590 105.559 166.970  1.00 87.44           C  
ATOM    716  NZ  LYS A  94     100.833 105.739 168.239  1.00 84.05           N  
ATOM    717  N   PHE A  95     103.884 103.900 161.095  1.00 76.05           N  
ATOM    718  CA  PHE A  95     103.593 103.655 159.687  1.00 74.67           C  
ATOM    719  C   PHE A  95     104.016 102.280 159.193  1.00 72.57           C  
ATOM    720  O   PHE A  95     103.309 101.702 158.366  1.00 75.38           O  
ATOM    721  CB  PHE A  95     104.250 104.719 158.787  1.00 74.02           C  
ATOM    722  CG  PHE A  95     103.924 106.141 159.161  1.00 72.84           C  
ATOM    723  CD1 PHE A  95     104.751 107.172 158.762  1.00 77.07           C  
ATOM    724  CD2 PHE A  95     102.760 106.456 159.835  1.00 74.38           C  
ATOM    725  CE1 PHE A  95     104.460 108.480 159.081  1.00 78.83           C  
ATOM    726  CE2 PHE A  95     102.461 107.762 160.156  1.00 78.56           C  
ATOM    727  CZ  PHE A  95     103.311 108.776 159.774  1.00 78.38           C  
ATOM    728  N   GLY A  96     105.125 101.743 159.663  1.00 60.56           N  
ATOM    729  CA  GLY A  96     105.550 100.424 159.244  1.00 64.06           C  
ATOM    730  C   GLY A  96     107.070 100.342 159.191  1.00 62.59           C  
ATOM    731  O   GLY A  96     107.760 100.984 159.987  1.00 67.90           O  
ATOM    732  N   ASP A  97     107.569  99.545 158.247  1.00 61.59           N  
ATOM    733  CA  ASP A  97     109.004  99.329 158.109  1.00 63.27           C  
ATOM    734  C   ASP A  97     109.531  99.957 156.827  1.00 63.04           C  
ATOM    735  O   ASP A  97     110.541 100.667 156.845  1.00 61.99           O  
ATOM    736  CB  ASP A  97     109.328  97.834 158.139  1.00 55.86           C  
ATOM    737  N   ILE A  98     108.860  99.692 155.712  1.00 59.85           N  
ATOM    738  CA  ILE A  98     109.187 100.312 154.431  1.00 55.78           C  
ATOM    739  C   ILE A  98     109.131 101.835 154.533  1.00 57.44           C  
ATOM    740  O   ILE A  98     110.026 102.506 153.999  1.00 59.57           O  
ATOM    741  CB  ILE A  98     108.260  99.802 153.316  1.00 53.38           C  
ATOM    742  N   PRO A  99     108.101 102.444 155.172  1.00 55.98           N  
ATOM    743  CA  PRO A  99     108.086 103.909 155.283  1.00 56.68           C  
ATOM    744  C   PRO A  99     109.285 104.492 156.018  1.00 59.26           C  
ATOM    745  O   PRO A  99     109.777 105.552 155.627  1.00 59.24           O  
ATOM    746  CB  PRO A  99     106.772 104.169 156.032  1.00 55.55           C  
ATOM    747  CG  PRO A  99     106.616 102.937 156.849  1.00 51.31           C  
ATOM    748  CD  PRO A  99     106.888 101.900 155.808  1.00 55.36           C  
ATOM    749  N   CYS A 100     109.774 103.823 157.063  1.00 61.10           N  
ATOM    750  CA  CYS A 100     110.979 104.280 157.747  1.00 56.64           C  
ATOM    751  C   CYS A 100     112.183 104.312 156.819  1.00 54.48           C  
ATOM    752  O   CYS A 100     112.898 105.319 156.750  1.00 60.57           O  
ATOM    753  CB  CYS A 100     111.291 103.396 158.959  1.00 59.77           C  
ATOM    754  SG  CYS A 100     110.655 104.002 160.525  1.00 69.18           S  
ATOM    755  N   ARG A 101     112.426 103.206 156.120  1.00 50.53           N  
ATOM    756  CA  ARG A 101     113.558 103.120 155.211  1.00 57.43           C  
ATOM    757  C   ARG A 101     113.438 104.208 154.161  1.00 56.09           C  
ATOM    758  O   ARG A 101     114.405 104.921 153.881  1.00 45.01           O  
ATOM    759  CB  ARG A 101     113.625 101.746 154.539  1.00 53.51           C  
ATOM    760  CG  ARG A 101     113.476 100.567 155.483  1.00 54.33           C  
ATOM    761  CD  ARG A 101     113.374  99.262 154.709  1.00 56.53           C  
ATOM    762  NE  ARG A 101     113.702  98.103 155.531  1.00 64.09           N  
ATOM    763  CZ  ARG A 101     112.849  97.131 155.825  1.00 61.78           C  
ATOM    764  NH1 ARG A 101     111.601  97.150 155.386  1.00 58.20           N  
ATOM    765  NH2 ARG A 101     113.257  96.115 156.580  1.00 59.66           N  
ATOM    766  N   LEU A 102     112.239 104.354 153.596  1.00 60.34           N  
ATOM    767  CA  LEU A 102     112.034 105.339 152.543  1.00 58.07           C  
ATOM    768  C   LEU A 102     112.252 106.758 153.046  1.00 50.29           C  
ATOM    769  O   LEU A 102     112.904 107.556 152.370  1.00 51.46           O  
ATOM    770  CB  LEU A 102     110.636 105.194 151.943  1.00 48.96           C  
ATOM    771  CG  LEU A 102     110.551 104.352 150.670  1.00 46.36           C  
ATOM    772  CD1 LEU A 102     111.308 105.038 149.545  1.00 47.23           C  
ATOM    773  CD2 LEU A 102     111.074 102.939 150.891  1.00 44.72           C  
ATOM    774  N   MET A 103     111.739 107.095 154.230  1.00 43.99           N  
ATOM    775  CA  MET A 103     111.868 108.469 154.695  1.00 49.34           C  
ATOM    776  C   MET A 103     113.307 108.794 155.071  1.00 58.25           C  
ATOM    777  O   MET A 103     113.809 109.873 154.735  1.00 65.89           O  
ATOM    778  CB  MET A 103     110.935 108.740 155.874  1.00 50.19           C  
ATOM    779  CG  MET A 103     110.807 110.224 156.156  1.00 50.38           C  
ATOM    780  SD  MET A 103     110.330 110.689 157.822  1.00 64.59           S  
ATOM    781  CE  MET A 103     111.389 109.635 158.796  1.00 50.15           C  
ATOM    782  N   LEU A 104     113.989 107.884 155.774  1.00 43.67           N  
ATOM    783  CA  LEU A 104     115.386 108.140 156.114  1.00 27.82           C  
ATOM    784  C   LEU A 104     116.242 108.236 154.862  1.00 38.31           C  
ATOM    785  O   LEU A 104     117.099 109.123 154.753  1.00 34.85           O  
ATOM    786  CB  LEU A 104     115.930 107.055 157.041  1.00 37.05           C  
ATOM    787  CG  LEU A 104     115.646 107.092 158.544  1.00 40.04           C  
ATOM    788  CD1 LEU A 104     114.277 107.636 158.865  1.00 33.06           C  
ATOM    789  CD2 LEU A 104     115.830 105.714 159.154  1.00 48.11           C  
ATOM    790  N   PHE A 105     116.021 107.334 153.901  1.00 48.03           N  
ATOM    791  CA  PHE A 105     116.758 107.390 152.648  1.00 45.39           C  
ATOM    792  C   PHE A 105     116.490 108.695 151.918  1.00 48.53           C  
ATOM    793  O   PHE A 105     117.418 109.325 151.407  1.00 47.76           O  
ATOM    794  CB  PHE A 105     116.381 106.200 151.768  1.00 43.27           C  
ATOM    795  CG  PHE A 105     117.136 106.138 150.475  1.00 38.29           C  
ATOM    796  CD1 PHE A 105     118.445 106.573 150.399  1.00 37.86           C  
ATOM    797  CD2 PHE A 105     116.531 105.658 149.332  1.00 43.34           C  
ATOM    798  CE1 PHE A 105     119.137 106.522 149.209  1.00 38.14           C  
ATOM    799  CE2 PHE A 105     117.220 105.605 148.140  1.00 48.11           C  
ATOM    800  CZ  PHE A 105     118.524 106.037 148.079  1.00 38.82           C  
ATOM    801  N   MET A 106     115.230 109.121 151.867  1.00 44.70           N  
ATOM    802  CA  MET A 106     114.875 110.350 151.179  1.00 33.32           C  
ATOM    803  C   MET A 106     115.580 111.527 151.831  1.00 37.34           C  
ATOM    804  O   MET A 106     116.254 112.298 151.147  1.00 44.11           O  
ATOM    805  CB  MET A 106     113.361 110.548 151.185  1.00 31.01           C  
ATOM    806  CG  MET A 106     112.662 109.941 149.980  1.00 41.56           C  
ATOM    807  N   LEU A 107     115.470 111.648 153.154  1.00 35.36           N  
ATOM    808  CA  LEU A 107     116.094 112.770 153.847  1.00 27.27           C  
ATOM    809  C   LEU A 107     117.600 112.798 153.614  1.00 33.05           C  
ATOM    810  O   LEU A 107     118.153 113.819 153.192  1.00 40.50           O  
ATOM    811  CB  LEU A 107     115.783 112.700 155.340  1.00 22.88           C  
ATOM    812  CG  LEU A 107     114.403 113.200 155.753  1.00 24.02           C  
ATOM    813  CD1 LEU A 107     114.126 112.830 157.192  1.00 34.40           C  
ATOM    814  CD2 LEU A 107     114.304 114.697 155.563  1.00 32.00           C  
ATOM    815  N   ALA A 108     118.280 111.675 153.865  1.00 33.60           N  
ATOM    816  CA  ALA A 108     119.735 111.663 153.763  1.00 31.38           C  
ATOM    817  C   ALA A 108     120.223 111.835 152.331  1.00 38.59           C  
ATOM    818  O   ALA A 108     121.153 112.614 152.091  1.00 50.27           O  
ATOM    819  CB  ALA A 108     120.294 110.372 154.354  1.00 41.41           C  
ATOM    820  N   MET A 109     119.622 111.127 151.371  1.00 40.20           N  
ATOM    821  CA  MET A 109     120.012 111.275 149.976  1.00 42.96           C  
ATOM    822  C   MET A 109     119.757 112.683 149.468  1.00 55.84           C  
ATOM    823  O   MET A 109     120.579 113.226 148.728  1.00 57.84           O  
ATOM    824  CB  MET A 109     119.259 110.264 149.113  1.00 42.75           C  
ATOM    825  CG  MET A 109     119.524 110.397 147.627  1.00 47.50           C  
ATOM    826  SD  MET A 109     118.334 109.477 146.636  1.00 78.71           S  
ATOM    827  N   ASN A 110     118.638 113.296 149.854  1.00 54.46           N  
ATOM    828  CA  ASN A 110     118.332 114.639 149.384  1.00 39.53           C  
ATOM    829  C   ASN A 110     119.249 115.673 150.021  1.00 32.23           C  
ATOM    830  O   ASN A 110     119.640 116.645 149.372  1.00 39.89           O  
ATOM    831  CB  ASN A 110     116.868 114.955 149.664  1.00 37.87           C  
ATOM    832  CG  ASN A 110     115.933 114.022 148.936  1.00 48.85           C  
ATOM    833  OD1 ASN A 110     116.336 112.954 148.479  1.00 45.92           O  
ATOM    834  ND2 ASN A 110     114.672 114.393 148.866  1.00 45.64           N  
ATOM    835  N   ARG A 111     119.603 115.487 151.295  1.00 35.96           N  
ATOM    836  CA  ARG A 111     120.571 116.386 151.916  1.00 34.80           C  
ATOM    837  C   ARG A 111     121.938 116.258 151.259  1.00 40.64           C  
ATOM    838  O   ARG A 111     122.608 117.265 150.993  1.00 47.04           O  
ATOM    839  CB  ARG A 111     120.668 116.103 153.412  1.00 32.65           C  
ATOM    840  CG  ARG A 111     121.432 117.154 154.182  1.00 32.53           C  
ATOM    841  CD  ARG A 111     121.037 117.135 155.641  1.00 36.57           C  
ATOM    842  NE  ARG A 111     121.073 115.785 156.183  1.00 31.66           N  
ATOM    843  CZ  ARG A 111     120.039 115.181 156.750  1.00 31.07           C  
ATOM    844  NH1 ARG A 111     118.872 115.785 156.878  1.00 28.74           N  
ATOM    845  NH2 ARG A 111     120.182 113.937 157.197  1.00 37.38           N  
ATOM    846  N   GLN A 112     122.365 115.023 150.983  1.00 33.68           N  
ATOM    847  CA  GLN A 112     123.619 114.818 150.269  1.00 35.50           C  
ATOM    848  C   GLN A 112     123.574 115.450 148.887  1.00 51.49           C  
ATOM    849  O   GLN A 112     124.556 116.049 148.441  1.00 48.49           O  
ATOM    850  CB  GLN A 112     123.924 113.328 150.152  1.00 48.37           C  
ATOM    851  CG  GLN A 112     124.529 112.707 151.382  1.00 44.36           C  
ATOM    852  CD  GLN A 112     126.003 112.430 151.206  1.00 48.83           C  
ATOM    853  OE1 GLN A 112     126.666 113.051 150.377  1.00 52.17           O  
ATOM    854  NE2 GLN A 112     126.522 111.485 151.975  1.00 45.72           N  
ATOM    855  N   GLY A 113     122.450 115.307 148.187  1.00 52.22           N  
ATOM    856  CA  GLY A 113     122.326 115.911 146.873  1.00 45.54           C  
ATOM    857  C   GLY A 113     122.359 117.424 146.929  1.00 40.49           C  
ATOM    858  O   GLY A 113     123.023 118.066 146.114  1.00 39.12           O  
ATOM    859  N   SER A 114     121.654 118.014 147.894  1.00 32.65           N  
ATOM    860  CA  SER A 114     121.683 119.462 148.051  1.00 25.56           C  
ATOM    861  C   SER A 114     123.098 119.950 148.306  1.00 33.41           C  
ATOM    862  O   SER A 114     123.557 120.900 147.666  1.00 48.85           O  
ATOM    863  CB  SER A 114     120.760 119.886 149.190  1.00 33.40           C  
ATOM    864  OG  SER A 114     119.404 119.679 148.847  1.00 52.42           O  
ATOM    865  N   ILE A 115     123.819 119.293 149.217  1.00 33.31           N  
ATOM    866  CA  ILE A 115     125.191 119.699 149.502  1.00 34.91           C  
ATOM    867  C   ILE A 115     126.122 119.493 148.313  1.00 41.95           C  
ATOM    868  O   ILE A 115     126.924 120.383 148.003  1.00 51.62           O  
ATOM    869  CB  ILE A 115     125.725 118.942 150.725  1.00 36.71           C  
ATOM    870  CG1 ILE A 115     125.041 119.440 151.994  1.00 37.91           C  
ATOM    871  CG2 ILE A 115     127.212 119.117 150.837  1.00 32.62           C  
ATOM    872  CD1 ILE A 115     125.860 119.233 153.240  1.00 47.07           C  
ATOM    873  N   ILE A 116     126.035 118.350 147.632  1.00 38.21           N  
ATOM    874  CA  ILE A 116     126.909 118.075 146.499  1.00 33.33           C  
ATOM    875  C   ILE A 116     126.641 119.047 145.361  1.00 34.39           C  
ATOM    876  O   ILE A 116     127.572 119.530 144.712  1.00 36.18           O  
ATOM    877  CB  ILE A 116     126.744 116.612 146.049  1.00 33.94           C  
ATOM    878  CG1 ILE A 116     127.583 115.688 146.929  1.00 38.80           C  
ATOM    879  CG2 ILE A 116     127.147 116.448 144.600  1.00 42.22           C  
ATOM    880  CD1 ILE A 116     129.053 116.039 146.950  1.00 39.05           C  
ATOM    881  N   PHE A 117     125.372 119.364 145.102  1.00 34.58           N  
ATOM    882  CA  PHE A 117     125.062 120.290 144.024  1.00 36.53           C  
ATOM    883  C   PHE A 117     125.389 121.727 144.406  1.00 30.82           C  
ATOM    884  O   PHE A 117     125.763 122.520 143.539  1.00 31.99           O  
ATOM    885  CB  PHE A 117     123.600 120.136 143.614  1.00 39.76           C  
ATOM    886  CG  PHE A 117     123.351 118.928 142.761  1.00 34.80           C  
ATOM    887  CD1 PHE A 117     123.992 118.786 141.546  1.00 29.50           C  
ATOM    888  CD2 PHE A 117     122.502 117.925 143.182  1.00 35.37           C  
ATOM    889  CE1 PHE A 117     123.779 117.677 140.763  1.00 37.96           C  
ATOM    890  CE2 PHE A 117     122.286 116.814 142.403  1.00 21.71           C  
ATOM    891  CZ  PHE A 117     122.925 116.691 141.192  1.00 34.76           C  
ATOM    892  N   LEU A 118     125.288 122.077 145.690  1.00 43.31           N  
ATOM    893  CA  LEU A 118     125.808 123.362 146.139  1.00 41.83           C  
ATOM    894  C   LEU A 118     127.305 123.455 145.885  1.00 46.89           C  
ATOM    895  O   LEU A 118     127.800 124.466 145.373  1.00 51.97           O  
ATOM    896  CB  LEU A 118     125.511 123.554 147.624  1.00 40.07           C  
ATOM    897  CG  LEU A 118     124.427 124.548 148.031  1.00 41.08           C  
ATOM    898  CD1 LEU A 118     123.059 124.034 147.651  1.00 45.11           C  
ATOM    899  CD2 LEU A 118     124.498 124.805 149.521  1.00 51.72           C  
ATOM    900  N   THR A 119     128.040 122.395 146.221  1.00 30.24           N  
ATOM    901  CA  THR A 119     129.477 122.386 145.979  1.00 18.77           C  
ATOM    902  C   THR A 119     129.786 122.464 144.491  1.00 42.81           C  
ATOM    903  O   THR A 119     130.726 123.151 144.080  1.00 41.51           O  
ATOM    904  CB  THR A 119     130.101 121.136 146.588  1.00 26.29           C  
ATOM    905  OG1 THR A 119     129.404 120.797 147.791  1.00 48.52           O  
ATOM    906  CG2 THR A 119     131.558 121.378 146.910  1.00 29.14           C  
ATOM    907  N   VAL A 120     129.004 121.768 143.664  1.00 50.62           N  
ATOM    908  CA  VAL A 120     129.298 121.740 142.236  1.00 40.02           C  
ATOM    909  C   VAL A 120     128.942 123.066 141.574  1.00 39.07           C  
ATOM    910  O   VAL A 120     129.633 123.498 140.649  1.00 44.86           O  
ATOM    911  CB  VAL A 120     128.603 120.543 141.557  1.00 31.68           C  
ATOM    912  CG1 VAL A 120     127.181 120.874 141.167  1.00 44.17           C  
ATOM    913  CG2 VAL A 120     129.401 120.100 140.347  1.00 37.01           C  
ATOM    914  N   VAL A 121     127.891 123.753 142.034  1.00 39.04           N  
ATOM    915  CA  VAL A 121     127.626 125.081 141.487  1.00 36.26           C  
ATOM    916  C   VAL A 121     128.667 126.076 141.982  1.00 41.96           C  
ATOM    917  O   VAL A 121     129.044 126.999 141.250  1.00 49.87           O  
ATOM    918  CB  VAL A 121     126.190 125.553 141.795  1.00 30.97           C  
ATOM    919  CG1 VAL A 121     125.178 124.581 141.226  1.00 35.99           C  
ATOM    920  CG2 VAL A 121     125.975 125.744 143.277  1.00 46.70           C  
ATOM    921  N   ALA A 122     129.167 125.907 143.210  1.00 27.83           N  
ATOM    922  CA  ALA A 122     130.259 126.758 143.670  1.00 27.16           C  
ATOM    923  C   ALA A 122     131.512 126.547 142.832  1.00 40.55           C  
ATOM    924  O   ALA A 122     132.192 127.510 142.464  1.00 57.60           O  
ATOM    925  CB  ALA A 122     130.549 126.494 145.145  1.00 38.06           C  
ATOM    926  N   VAL A 123     131.830 125.292 142.511  1.00 31.46           N  
ATOM    927  CA  VAL A 123     132.994 125.005 141.677  1.00 40.26           C  
ATOM    928  C   VAL A 123     132.779 125.524 140.260  1.00 39.40           C  
ATOM    929  O   VAL A 123     133.710 126.022 139.616  1.00 33.02           O  
ATOM    930  CB  VAL A 123     133.298 123.496 141.690  1.00 33.06           C  
ATOM    931  CG1 VAL A 123     134.377 123.164 140.685  1.00 25.94           C  
ATOM    932  CG2 VAL A 123     133.720 123.057 143.077  1.00 35.48           C  
ATOM    933  N   ASP A 124     131.551 125.416 139.751  1.00 43.22           N  
ATOM    934  CA  ASP A 124     131.240 125.970 138.441  1.00 40.09           C  
ATOM    935  C   ASP A 124     131.455 127.474 138.421  1.00 49.53           C  
ATOM    936  O   ASP A 124     132.036 128.011 137.473  1.00 58.11           O  
ATOM    937  CB  ASP A 124     129.801 125.637 138.060  1.00 42.01           C  
ATOM    938  CG  ASP A 124     129.558 125.745 136.575  1.00 52.00           C  
ATOM    939  OD1 ASP A 124     130.545 125.745 135.812  1.00 53.67           O  
ATOM    940  OD2 ASP A 124     128.382 125.839 136.169  1.00 59.38           O  
ATOM    941  N   ARG A 125     130.996 128.171 139.461  1.00 43.14           N  
ATOM    942  CA  ARG A 125     131.216 129.611 139.537  1.00 34.05           C  
ATOM    943  C   ARG A 125     132.697 129.935 139.662  1.00 43.48           C  
ATOM    944  O   ARG A 125     133.176 130.913 139.078  1.00 59.88           O  
ATOM    945  CB  ARG A 125     130.438 130.202 140.709  1.00 27.44           C  
ATOM    946  CG  ARG A 125     128.965 130.400 140.429  1.00 40.74           C  
ATOM    947  CD  ARG A 125     128.152 130.302 141.701  1.00 47.06           C  
ATOM    948  NE  ARG A 125     126.754 130.643 141.475  1.00 48.54           N  
ATOM    949  CZ  ARG A 125     125.884 130.901 142.440  1.00 42.32           C  
ATOM    950  NH1 ARG A 125     126.237 130.874 143.713  1.00 37.11           N  
ATOM    951  NH2 ARG A 125     124.627 131.193 142.118  1.00 47.54           N  
ATOM    952  N   TYR A 126     133.438 129.131 140.428  1.00 33.72           N  
ATOM    953  CA  TYR A 126     134.873 129.357 140.560  1.00 34.95           C  
ATOM    954  C   TYR A 126     135.575 129.230 139.216  1.00 45.13           C  
ATOM    955  O   TYR A 126     136.438 130.046 138.878  1.00 50.70           O  
ATOM    956  CB  TYR A 126     135.471 128.378 141.568  1.00 41.94           C  
ATOM    957  CG  TYR A 126     136.977 128.276 141.501  1.00 36.35           C  
ATOM    958  CD1 TYR A 126     137.778 129.280 142.011  1.00 37.68           C  
ATOM    959  CD2 TYR A 126     137.594 127.176 140.930  1.00 40.38           C  
ATOM    960  CE1 TYR A 126     139.149 129.192 141.954  1.00 43.64           C  
ATOM    961  CE2 TYR A 126     138.966 127.081 140.868  1.00 37.28           C  
ATOM    962  CZ  TYR A 126     139.737 128.093 141.383  1.00 41.67           C  
ATOM    963  OH  TYR A 126     141.107 128.009 141.328  1.00 48.59           O  
ATOM    964  N   PHE A 127     135.220 128.209 138.436  1.00 44.45           N  
ATOM    965  CA  PHE A 127     135.794 128.076 137.101  1.00 42.77           C  
ATOM    966  C   PHE A 127     135.353 129.216 136.194  1.00 43.90           C  
ATOM    967  O   PHE A 127     136.150 129.726 135.402  1.00 47.61           O  
ATOM    968  CB  PHE A 127     135.419 126.728 136.488  1.00 40.64           C  
ATOM    969  CG  PHE A 127     136.303 125.602 136.926  1.00 49.36           C  
ATOM    970  CD1 PHE A 127     137.624 125.552 136.523  1.00 49.94           C  
ATOM    971  CD2 PHE A 127     135.816 124.589 137.731  1.00 47.31           C  
ATOM    972  CE1 PHE A 127     138.444 124.522 136.921  1.00 50.20           C  
ATOM    973  CE2 PHE A 127     136.633 123.554 138.130  1.00 43.04           C  
ATOM    974  CZ  PHE A 127     137.947 123.520 137.725  1.00 47.52           C  
ATOM    975  N   ARG A 128     134.091 129.632 136.297  1.00 39.38           N  
ATOM    976  CA  ARG A 128     133.576 130.681 135.431  1.00 35.45           C  
ATOM    977  C   ARG A 128     134.162 132.048 135.752  1.00 42.62           C  
ATOM    978  O   ARG A 128     134.165 132.924 134.883  1.00 49.14           O  
ATOM    979  CB  ARG A 128     132.054 130.733 135.532  1.00 38.65           C  
ATOM    980  CG  ARG A 128     131.355 129.628 134.769  1.00 44.91           C  
ATOM    981  CD  ARG A 128     129.851 129.820 134.766  1.00 41.97           C  
ATOM    982  NE  ARG A 128     129.177 128.732 134.069  1.00 46.87           N  
ATOM    983  CZ  ARG A 128     129.026 128.668 132.754  1.00 55.44           C  
ATOM    984  NH1 ARG A 128     129.480 129.623 131.959  1.00 58.18           N  
ATOM    985  NH2 ARG A 128     128.403 127.621 132.223  1.00 53.38           N  
ATOM    986  N   VAL A 129     134.650 132.251 136.970  1.00 48.51           N  
ATOM    987  CA  VAL A 129     135.164 133.548 137.397  1.00 41.32           C  
ATOM    988  C   VAL A 129     136.686 133.600 137.353  1.00 47.64           C  
ATOM    989  O   VAL A 129     137.263 134.510 136.760  1.00 60.57           O  
ATOM    990  CB  VAL A 129     134.635 133.892 138.806  1.00 44.15           C  
ATOM    991  CG1 VAL A 129     135.364 135.098 139.360  1.00 49.57           C  
ATOM    992  CG2 VAL A 129     133.141 134.143 138.760  1.00 43.79           C  
ATOM    993  N   VAL A 130     137.358 132.632 137.977  1.00 46.00           N  
ATOM    994  CA  VAL A 130     138.811 132.712 138.089  1.00 51.98           C  
ATOM    995  C   VAL A 130     139.503 132.192 136.832  1.00 56.93           C  
ATOM    996  O   VAL A 130     140.557 132.709 136.444  1.00 59.71           O  
ATOM    997  CB  VAL A 130     139.282 131.963 139.345  1.00 57.09           C  
ATOM    998  CG1 VAL A 130     140.796 131.970 139.439  1.00 54.28           C  
ATOM    999  CG2 VAL A 130     138.672 132.591 140.580  1.00 59.01           C  
ATOM   1000  N   HIS A 131     138.932 131.194 136.163  1.00 56.61           N  
ATOM   1001  CA  HIS A 131     139.520 130.607 134.959  1.00 60.42           C  
ATOM   1002  C   HIS A 131     138.494 130.652 133.835  1.00 58.81           C  
ATOM   1003  O   HIS A 131     137.970 129.616 133.410  1.00 60.13           O  
ATOM   1004  CB  HIS A 131     139.983 129.173 135.220  1.00 57.90           C  
ATOM   1005  CG  HIS A 131     141.354 129.079 135.811  1.00 64.27           C  
ATOM   1006  ND1 HIS A 131     141.598 129.261 137.155  1.00 64.83           N  
ATOM   1007  CD2 HIS A 131     142.553 128.813 135.243  1.00 63.24           C  
ATOM   1008  CE1 HIS A 131     142.890 129.117 137.389  1.00 61.55           C  
ATOM   1009  NE2 HIS A 131     143.492 128.844 136.245  1.00 65.52           N  
ATOM   1010  N   PRO A 132     138.196 131.847 133.321  1.00 48.27           N  
ATOM   1011  CA  PRO A 132     137.107 131.970 132.339  1.00 45.32           C  
ATOM   1012  C   PRO A 132     137.339 131.179 131.068  1.00 53.36           C  
ATOM   1013  O   PRO A 132     136.370 130.723 130.448  1.00 62.80           O  
ATOM   1014  CB  PRO A 132     137.054 133.479 132.058  1.00 52.48           C  
ATOM   1015  CG  PRO A 132     137.890 134.124 133.121  1.00 58.08           C  
ATOM   1016  CD  PRO A 132     138.903 133.118 133.526  1.00 54.12           C  
ATOM   1017  N   HIS A 133     138.589 130.996 130.658  1.00 54.49           N  
ATOM   1018  CA  HIS A 133     138.903 130.342 129.397  1.00 63.11           C  
ATOM   1019  C   HIS A 133     139.128 128.843 129.541  1.00 66.26           C  
ATOM   1020  O   HIS A 133     139.521 128.194 128.567  1.00 66.25           O  
ATOM   1021  CB  HIS A 133     140.130 130.997 128.764  1.00 60.95           C  
ATOM   1022  CG  HIS A 133     140.068 132.491 128.743  1.00 62.15           C  
ATOM   1023  ND1 HIS A 133     139.556 133.200 127.677  1.00 63.36           N  
ATOM   1024  CD2 HIS A 133     140.453 133.412 129.657  1.00 60.80           C  
ATOM   1025  CE1 HIS A 133     139.629 134.493 127.936  1.00 62.12           C  
ATOM   1026  NE2 HIS A 133     140.169 134.649 129.131  1.00 60.38           N  
ATOM   1027  N   HIS A 134     138.898 128.283 130.725  1.00 63.96           N  
ATOM   1028  CA  HIS A 134     139.053 126.848 130.910  1.00 58.18           C  
ATOM   1029  C   HIS A 134     138.011 126.093 130.098  1.00 54.17           C  
ATOM   1030  O   HIS A 134     136.874 126.546 129.942  1.00 53.61           O  
ATOM   1031  CB  HIS A 134     138.929 126.484 132.388  1.00 58.16           C  
ATOM   1032  CG  HIS A 134     139.623 125.210 132.756  1.00 60.16           C  
ATOM   1033  ND1 HIS A 134     139.218 124.421 133.811  1.00 60.37           N  
ATOM   1034  CD2 HIS A 134     140.696 124.590 132.213  1.00 61.87           C  
ATOM   1035  CE1 HIS A 134     140.010 123.368 133.901  1.00 57.64           C  
ATOM   1036  NE2 HIS A 134     140.916 123.447 132.943  1.00 58.85           N  
ATOM   1037  N   ALA A 135     138.408 124.931 129.578  1.00 59.64           N  
ATOM   1038  CA  ALA A 135     137.509 124.136 128.750  1.00 60.13           C  
ATOM   1039  C   ALA A 135     136.292 123.646 129.519  1.00 60.16           C  
ATOM   1040  O   ALA A 135     135.267 123.337 128.902  1.00 61.49           O  
ATOM   1041  CB  ALA A 135     138.260 122.946 128.152  1.00 56.77           C  
ATOM   1042  N   LEU A 136     136.377 123.565 130.847  1.00 52.48           N  
ATOM   1043  CA  LEU A 136     135.242 123.086 131.625  1.00 52.10           C  
ATOM   1044  C   LEU A 136     134.085 124.076 131.602  1.00 60.57           C  
ATOM   1045  O   LEU A 136     132.934 123.684 131.825  1.00 66.61           O  
ATOM   1046  CB  LEU A 136     135.676 122.798 133.061  1.00 48.97           C  
ATOM   1047  CG  LEU A 136     134.824 121.790 133.831  1.00 51.57           C  
ATOM   1048  CD1 LEU A 136     135.706 120.911 134.697  1.00 56.46           C  
ATOM   1049  CD2 LEU A 136     133.780 122.493 134.680  1.00 48.62           C  
ATOM   1050  N   ASN A 137     134.363 125.356 131.344  1.00 63.84           N  
ATOM   1051  CA  ASN A 137     133.285 126.331 131.211  1.00 54.59           C  
ATOM   1052  C   ASN A 137     132.403 126.011 130.011  1.00 55.92           C  
ATOM   1053  O   ASN A 137     131.171 126.050 130.107  1.00 54.71           O  
ATOM   1054  CB  ASN A 137     133.861 127.739 131.090  1.00 45.38           C  
ATOM   1055  CG  ASN A 137     134.795 128.081 132.227  1.00 57.05           C  
ATOM   1056  OD1 ASN A 137     134.380 128.169 133.381  1.00 56.81           O  
ATOM   1057  ND2 ASN A 137     136.068 128.270 131.908  1.00 58.54           N  
ATOM   1058  N   LYS A 138     133.017 125.686 128.875  1.00 50.48           N  
ATOM   1059  CA  LYS A 138     132.288 125.309 127.665  1.00 50.97           C  
ATOM   1060  C   LYS A 138     132.068 123.804 127.710  1.00 49.56           C  
ATOM   1061  O   LYS A 138     132.869 123.019 127.201  1.00 48.60           O  
ATOM   1062  CB  LYS A 138     133.055 125.733 126.420  1.00 55.21           C  
ATOM   1063  CG  LYS A 138     133.175 127.236 126.250  1.00 52.97           C  
ATOM   1064  CD  LYS A 138     133.936 127.587 124.984  1.00 51.97           C  
ATOM   1065  CE  LYS A 138     133.957 129.088 124.753  1.00 54.83           C  
ATOM   1066  NZ  LYS A 138     132.604 129.620 124.438  1.00 51.21           N  
ATOM   1067  N   ILE A 139     130.965 123.395 128.331  1.00 57.93           N  
ATOM   1068  CA  ILE A 139     130.654 121.988 128.547  1.00 63.57           C  
ATOM   1069  C   ILE A 139     129.274 121.706 127.968  1.00 65.31           C  
ATOM   1070  O   ILE A 139     128.328 122.465 128.204  1.00 69.64           O  
ATOM   1071  CB  ILE A 139     130.725 121.619 130.042  1.00 56.41           C  
ATOM   1072  CG1 ILE A 139     130.298 120.172 130.275  1.00 56.46           C  
ATOM   1073  CG2 ILE A 139     129.895 122.578 130.880  1.00 57.31           C  
ATOM   1074  CD1 ILE A 139     130.718 119.638 131.625  1.00 55.17           C  
ATOM   1075  N   SER A 140     129.165 120.625 127.199  1.00 60.21           N  
ATOM   1076  CA  SER A 140     127.933 120.322 126.486  1.00 60.35           C  
ATOM   1077  C   SER A 140     126.834 119.892 127.452  1.00 60.08           C  
ATOM   1078  O   SER A 140     127.090 119.431 128.567  1.00 59.89           O  
ATOM   1079  CB  SER A 140     128.170 119.228 125.446  1.00 59.46           C  
ATOM   1080  OG  SER A 140     128.310 117.962 126.063  1.00 57.35           O  
ATOM   1081  N   ASN A 141     125.587 120.052 127.002  1.00 57.16           N  
ATOM   1082  CA  ASN A 141     124.445 119.720 127.846  1.00 61.76           C  
ATOM   1083  C   ASN A 141     124.363 118.220 128.109  1.00 59.67           C  
ATOM   1084  O   ASN A 141     123.989 117.797 129.209  1.00 55.25           O  
ATOM   1085  CB  ASN A 141     123.156 120.227 127.204  1.00 61.14           C  
ATOM   1086  CG  ASN A 141     122.051 120.447 128.214  1.00 64.08           C  
ATOM   1087  OD1 ASN A 141     121.949 119.729 129.207  1.00 64.56           O  
ATOM   1088  ND2 ASN A 141     121.216 121.448 127.965  1.00 65.46           N  
ATOM   1089  N   ARG A 142     124.693 117.400 127.110  1.00 53.67           N  
ATOM   1090  CA  ARG A 142     124.746 115.959 127.333  1.00 47.32           C  
ATOM   1091  C   ARG A 142     125.820 115.604 128.353  1.00 54.93           C  
ATOM   1092  O   ARG A 142     125.607 114.748 129.220  1.00 59.85           O  
ATOM   1093  CB  ARG A 142     124.996 115.235 126.010  1.00 51.24           C  
ATOM   1094  CG  ARG A 142     125.345 113.764 126.153  1.00 54.55           C  
ATOM   1095  CD  ARG A 142     124.111 112.888 126.067  1.00 56.64           C  
ATOM   1096  NE  ARG A 142     124.442 111.513 125.712  1.00 62.25           N  
ATOM   1097  CZ  ARG A 142     124.360 111.014 124.486  1.00 60.36           C  
ATOM   1098  NH1 ARG A 142     123.956 111.753 123.466  1.00 56.97           N  
ATOM   1099  NH2 ARG A 142     124.687 109.742 124.280  1.00 53.44           N  
ATOM   1100  N   THR A 143     126.983 116.255 128.267  1.00 53.12           N  
ATOM   1101  CA  THR A 143     128.035 116.023 129.251  1.00 49.36           C  
ATOM   1102  C   THR A 143     127.584 116.450 130.639  1.00 45.58           C  
ATOM   1103  O   THR A 143     127.895 115.785 131.633  1.00 38.72           O  
ATOM   1104  CB  THR A 143     129.308 116.768 128.854  1.00 50.04           C  
ATOM   1105  OG1 THR A 143     129.539 116.609 127.449  1.00 47.64           O  
ATOM   1106  CG2 THR A 143     130.498 116.219 129.618  1.00 47.67           C  
ATOM   1107  N   ALA A 144     126.857 117.565 130.728  1.00 50.34           N  
ATOM   1108  CA  ALA A 144     126.323 117.995 132.014  1.00 46.43           C  
ATOM   1109  C   ALA A 144     125.331 116.981 132.562  1.00 45.49           C  
ATOM   1110  O   ALA A 144     125.309 116.715 133.767  1.00 50.24           O  
ATOM   1111  CB  ALA A 144     125.669 119.368 131.883  1.00 48.40           C  
ATOM   1112  N   ALA A 145     124.500 116.404 131.693  1.00 45.93           N  
ATOM   1113  CA  ALA A 145     123.558 115.384 132.141  1.00 48.30           C  
ATOM   1114  C   ALA A 145     124.284 114.143 132.648  1.00 47.89           C  
ATOM   1115  O   ALA A 145     123.897 113.563 133.668  1.00 46.39           O  
ATOM   1116  CB  ALA A 145     122.596 115.023 131.011  1.00 46.77           C  
ATOM   1117  N   ILE A 146     125.341 113.722 131.949  1.00 40.25           N  
ATOM   1118  CA  ILE A 146     126.116 112.567 132.403  1.00 33.01           C  
ATOM   1119  C   ILE A 146     126.791 112.862 133.737  1.00 46.76           C  
ATOM   1120  O   ILE A 146     126.803 112.020 134.642  1.00 54.23           O  
ATOM   1121  CB  ILE A 146     127.141 112.143 131.335  1.00 38.23           C  
ATOM   1122  CG1 ILE A 146     126.442 111.858 130.005  1.00 47.39           C  
ATOM   1123  CG2 ILE A 146     127.936 110.934 131.807  1.00 35.16           C  
ATOM   1124  CD1 ILE A 146     125.415 110.747 130.076  1.00 44.29           C  
ATOM   1125  N   ILE A 147     127.364 114.059 133.880  1.00 49.35           N  
ATOM   1126  CA  ILE A 147     128.025 114.430 135.129  1.00 38.07           C  
ATOM   1127  C   ILE A 147     127.020 114.469 136.272  1.00 36.29           C  
ATOM   1128  O   ILE A 147     127.309 114.028 137.388  1.00 28.15           O  
ATOM   1129  CB  ILE A 147     128.756 115.775 134.966  1.00 36.76           C  
ATOM   1130  CG1 ILE A 147     130.105 115.565 134.280  1.00 34.95           C  
ATOM   1131  CG2 ILE A 147     128.946 116.453 136.310  1.00 36.50           C  
ATOM   1132  CD1 ILE A 147     130.904 116.835 134.108  1.00 38.62           C  
ATOM   1133  N   SER A 148     125.823 114.993 136.013  1.00 38.92           N  
ATOM   1134  CA  SER A 148     124.814 115.085 137.060  1.00 32.63           C  
ATOM   1135  C   SER A 148     124.277 113.712 137.443  1.00 39.13           C  
ATOM   1136  O   SER A 148     124.016 113.451 138.622  1.00 45.53           O  
ATOM   1137  CB  SER A 148     123.688 116.004 136.606  1.00 19.00           C  
ATOM   1138  OG  SER A 148     123.255 115.671 135.303  1.00 44.47           O  
ATOM   1139  N   CYS A 149     124.103 112.818 136.467  1.00 50.52           N  
ATOM   1140  CA  CYS A 149     123.712 111.450 136.793  1.00 44.63           C  
ATOM   1141  C   CYS A 149     124.806 110.744 137.584  1.00 48.75           C  
ATOM   1142  O   CYS A 149     124.518 109.968 138.500  1.00 50.76           O  
ATOM   1143  CB  CYS A 149     123.378 110.678 135.519  1.00 37.46           C  
ATOM   1144  SG  CYS A 149     121.878 111.242 134.690  1.00 66.67           S  
ATOM   1145  N   LEU A 150     126.071 111.010 137.252  1.00 48.56           N  
ATOM   1146  CA  LEU A 150     127.175 110.453 138.027  1.00 40.35           C  
ATOM   1147  C   LEU A 150     127.177 110.991 139.453  1.00 49.87           C  
ATOM   1148  O   LEU A 150     127.456 110.252 140.405  1.00 50.55           O  
ATOM   1149  CB  LEU A 150     128.500 110.762 137.334  1.00 38.79           C  
ATOM   1150  CG  LEU A 150     129.725 109.981 137.802  1.00 43.27           C  
ATOM   1151  CD1 LEU A 150     130.497 109.454 136.608  1.00 50.30           C  
ATOM   1152  CD2 LEU A 150     130.611 110.860 138.659  1.00 38.48           C  
ATOM   1153  N   LEU A 151     126.888 112.283 139.619  1.00 51.59           N  
ATOM   1154  CA  LEU A 151     126.818 112.862 140.956  1.00 43.90           C  
ATOM   1155  C   LEU A 151     125.667 112.265 141.754  1.00 43.69           C  
ATOM   1156  O   LEU A 151     125.801 112.009 142.955  1.00 45.36           O  
ATOM   1157  CB  LEU A 151     126.682 114.380 140.870  1.00 22.41           C  
ATOM   1158  CG  LEU A 151     128.003 115.120 140.685  1.00 27.31           C  
ATOM   1159  CD1 LEU A 151     127.771 116.615 140.607  1.00 34.35           C  
ATOM   1160  CD2 LEU A 151     128.955 114.778 141.816  1.00 39.63           C  
ATOM   1161  N   TRP A 152     124.526 112.037 141.105  1.00 30.65           N  
ATOM   1162  CA  TRP A 152     123.434 111.344 141.778  1.00 27.33           C  
ATOM   1163  C   TRP A 152     123.820 109.915 142.129  1.00 37.74           C  
ATOM   1164  O   TRP A 152     123.399 109.396 143.168  1.00 39.73           O  
ATOM   1165  CB  TRP A 152     122.180 111.363 140.908  1.00 24.09           C  
ATOM   1166  CG  TRP A 152     121.377 112.607 141.065  1.00 28.21           C  
ATOM   1167  CD1 TRP A 152     121.329 113.664 140.210  1.00 36.17           C  
ATOM   1168  CD2 TRP A 152     120.503 112.930 142.151  1.00 31.26           C  
ATOM   1169  NE1 TRP A 152     120.478 114.626 140.693  1.00 33.84           N  
ATOM   1170  CE2 TRP A 152     119.958 114.198 141.885  1.00 31.19           C  
ATOM   1171  CE3 TRP A 152     120.127 112.267 143.322  1.00 35.35           C  
ATOM   1172  CZ2 TRP A 152     119.059 114.817 142.745  1.00 34.70           C  
ATOM   1173  CZ3 TRP A 152     119.234 112.884 144.174  1.00 29.80           C  
ATOM   1174  CH2 TRP A 152     118.710 114.145 143.882  1.00 30.50           C  
ATOM   1175  N   GLY A 153     124.617 109.266 141.280  1.00 36.69           N  
ATOM   1176  CA  GLY A 153     125.102 107.935 141.607  1.00 39.03           C  
ATOM   1177  C   GLY A 153     126.009 107.932 142.821  1.00 47.87           C  
ATOM   1178  O   GLY A 153     125.923 107.046 143.672  1.00 58.75           O  
ATOM   1179  N   ILE A 154     126.894 108.923 142.914  1.00 40.93           N  
ATOM   1180  CA  ILE A 154     127.733 109.060 144.101  1.00 36.18           C  
ATOM   1181  C   ILE A 154     126.871 109.321 145.328  1.00 45.22           C  
ATOM   1182  O   ILE A 154     127.091 108.740 146.398  1.00 48.99           O  
ATOM   1183  CB  ILE A 154     128.775 110.173 143.894  1.00 39.95           C  
ATOM   1184  CG1 ILE A 154     129.951 109.653 143.073  1.00 46.14           C  
ATOM   1185  CG2 ILE A 154     129.263 110.708 145.227  1.00 46.03           C  
ATOM   1186  CD1 ILE A 154     130.636 110.722 142.257  1.00 50.91           C  
ATOM   1187  N   THR A 155     125.870 110.192 145.188  1.00 44.08           N  
ATOM   1188  CA  THR A 155     124.992 110.524 146.305  1.00 41.12           C  
ATOM   1189  C   THR A 155     124.260 109.292 146.820  1.00 43.68           C  
ATOM   1190  O   THR A 155     124.196 109.054 148.031  1.00 46.99           O  
ATOM   1191  CB  THR A 155     123.991 111.596 145.871  1.00 35.76           C  
ATOM   1192  OG1 THR A 155     124.672 112.839 145.666  1.00 30.72           O  
ATOM   1193  CG2 THR A 155     122.912 111.778 146.920  1.00 30.60           C  
ATOM   1194  N   ILE A 156     123.701 108.493 145.910  1.00 42.71           N  
ATOM   1195  CA  ILE A 156     122.934 107.326 146.332  1.00 43.31           C  
ATOM   1196  C   ILE A 156     123.856 106.230 146.853  1.00 40.96           C  
ATOM   1197  O   ILE A 156     123.529 105.543 147.825  1.00 50.19           O  
ATOM   1198  CB  ILE A 156     122.034 106.824 145.187  1.00 41.21           C  
ATOM   1199  CG1 ILE A 156     122.863 106.428 143.968  1.00 45.45           C  
ATOM   1200  CG2 ILE A 156     121.012 107.883 144.816  1.00 43.16           C  
ATOM   1201  CD1 ILE A 156     122.046 106.209 142.717  1.00 50.64           C  
ATOM   1202  N   GLY A 157     125.030 106.066 146.241  1.00 43.65           N  
ATOM   1203  CA  GLY A 157     125.907 104.961 146.586  1.00 46.30           C  
ATOM   1204  C   GLY A 157     126.365 104.949 148.028  1.00 52.96           C  
ATOM   1205  O   GLY A 157     126.719 103.887 148.548  1.00 61.03           O  
ATOM   1206  N   LEU A 158     126.371 106.102 148.688  1.00 37.88           N  
ATOM   1207  CA  LEU A 158     126.757 106.187 150.088  1.00 40.21           C  
ATOM   1208  C   LEU A 158     125.573 106.078 151.040  1.00 47.28           C  
ATOM   1209  O   LEU A 158     125.775 106.092 152.258  1.00 47.23           O  
ATOM   1210  CB  LEU A 158     127.496 107.501 150.349  1.00 39.93           C  
ATOM   1211  CG  LEU A 158     128.475 107.951 149.268  1.00 38.75           C  
ATOM   1212  CD1 LEU A 158     128.703 109.446 149.347  1.00 39.55           C  
ATOM   1213  CD2 LEU A 158     129.788 107.205 149.400  1.00 44.01           C  
ATOM   1214  N   THR A 159     124.350 105.958 150.523  1.00 46.48           N  
ATOM   1215  CA  THR A 159     123.159 106.091 151.343  1.00 42.08           C  
ATOM   1216  C   THR A 159     122.223 104.889 151.273  1.00 49.86           C  
ATOM   1217  O   THR A 159     121.298 104.800 152.089  1.00 49.84           O  
ATOM   1218  CB  THR A 159     122.395 107.363 150.940  1.00 36.44           C  
ATOM   1219  OG1 THR A 159     123.322 108.447 150.823  1.00 40.13           O  
ATOM   1220  CG2 THR A 159     121.383 107.748 152.000  1.00 44.93           C  
ATOM   1221  N   VAL A 160     122.445 103.946 150.353  1.00 47.49           N  
ATOM   1222  CA  VAL A 160     121.565 102.786 150.259  1.00 41.01           C  
ATOM   1223  C   VAL A 160     121.625 101.932 151.516  1.00 44.92           C  
ATOM   1224  O   VAL A 160     120.712 101.140 151.768  1.00 41.91           O  
ATOM   1225  CB  VAL A 160     121.900 101.934 149.018  1.00 48.94           C  
ATOM   1226  CG1 VAL A 160     120.711 101.071 148.635  1.00 50.83           C  
ATOM   1227  CG2 VAL A 160     122.288 102.811 147.856  1.00 47.70           C  
ATOM   1228  N   HIS A 161     122.676 102.078 152.325  1.00 51.84           N  
ATOM   1229  CA  HIS A 161     122.777 101.285 153.544  1.00 55.98           C  
ATOM   1230  C   HIS A 161     121.668 101.613 154.533  1.00 48.94           C  
ATOM   1231  O   HIS A 161     121.440 100.841 155.468  1.00 46.21           O  
ATOM   1232  CB  HIS A 161     124.149 101.482 154.193  1.00 52.79           C  
ATOM   1233  CG  HIS A 161     124.253 102.708 155.045  1.00 44.64           C  
ATOM   1234  ND1 HIS A 161     124.582 103.944 154.532  1.00 49.08           N  
ATOM   1235  CD2 HIS A 161     124.089 102.885 156.377  1.00 46.15           C  
ATOM   1236  CE1 HIS A 161     124.606 104.831 155.510  1.00 55.14           C  
ATOM   1237  NE2 HIS A 161     124.311 104.214 156.640  1.00 52.33           N  
ATOM   1238  N   LEU A 162     120.975 102.735 154.347  1.00 45.92           N  
ATOM   1239  CA  LEU A 162     119.801 103.050 155.147  1.00 48.85           C  
ATOM   1240  C   LEU A 162     118.569 102.269 154.714  1.00 52.22           C  
ATOM   1241  O   LEU A 162     117.561 102.289 155.427  1.00 59.89           O  
ATOM   1242  CB  LEU A 162     119.508 104.550 155.082  1.00 44.00           C  
ATOM   1243  CG  LEU A 162     120.605 105.455 155.642  1.00 43.86           C  
ATOM   1244  CD1 LEU A 162     120.253 106.907 155.432  1.00 43.09           C  
ATOM   1245  CD2 LEU A 162     120.820 105.168 157.115  1.00 52.27           C  
ATOM   1246  N   LEU A 163     118.625 101.591 153.568  1.00 49.32           N  
ATOM   1247  CA  LEU A 163     117.522 100.758 153.110  1.00 51.22           C  
ATOM   1248  C   LEU A 163     117.640  99.321 153.595  1.00 55.60           C  
ATOM   1249  O   LEU A 163     116.621  98.638 153.738  1.00 48.00           O  
ATOM   1250  CB  LEU A 163     117.452 100.771 151.581  1.00 39.13           C  
ATOM   1251  CG  LEU A 163     117.037 102.091 150.936  1.00 40.23           C  
ATOM   1252  CD1 LEU A 163     117.048 101.982 149.422  1.00 37.74           C  
ATOM   1253  CD2 LEU A 163     115.671 102.513 151.435  1.00 43.17           C  
ATOM   1254  N   LYS A 164     118.862  98.849 153.846  1.00 64.45           N  
ATOM   1255  CA  LYS A 164     119.059  97.473 154.286  1.00 60.46           C  
ATOM   1256  C   LYS A 164     118.670  97.286 155.747  1.00 55.79           C  
ATOM   1257  O   LYS A 164     118.117  96.244 156.114  1.00 58.85           O  
ATOM   1258  CB  LYS A 164     120.515  97.057 154.068  1.00 59.10           C  
ATOM   1259  CG  LYS A 164     121.063  97.391 152.686  1.00 56.84           C  
ATOM   1260  CD  LYS A 164     120.288  96.682 151.587  1.00 53.20           C  
ATOM   1261  CE  LYS A 164     120.765  97.114 150.209  1.00 57.18           C  
ATOM   1262  NZ  LYS A 164     119.764  96.810 149.148  1.00 53.76           N  
ATOM   1263  N   LYS A 165     118.946  98.275 156.590  1.00 57.50           N  
ATOM   1264  CA  LYS A 165     118.672  98.145 158.012  1.00 67.14           C  
ATOM   1265  C   LYS A 165     117.171  98.174 158.285  1.00 71.03           C  
ATOM   1266  O   LYS A 165     116.376  98.698 157.501  1.00 64.24           O  
ATOM   1267  CB  LYS A 165     119.358  99.264 158.797  1.00 67.87           C  
ATOM   1268  CG  LYS A 165     120.751  99.613 158.307  1.00 69.10           C  
ATOM   1269  CD  LYS A 165     121.359 100.743 159.124  1.00 62.94           C  
ATOM   1270  CE  LYS A 165     121.079 100.573 160.607  1.00 64.28           C  
ATOM   1271  NZ  LYS A 165     121.847  99.438 161.187  1.00 65.84           N  
ATOM   1272  N   LYS A 166     116.788  97.594 159.420  1.00 79.79           N  
ATOM   1273  CA  LYS A 166     115.409  97.672 159.900  1.00 75.81           C  
ATOM   1274  C   LYS A 166     115.268  98.975 160.675  1.00 80.39           C  
ATOM   1275  O   LYS A 166     115.453  99.032 161.892  1.00 82.27           O  
ATOM   1276  CB  LYS A 166     115.053  96.458 160.749  1.00 72.90           C  
ATOM   1277  CG  LYS A 166     116.148  96.003 161.698  1.00 76.96           C  
ATOM   1278  CD  LYS A 166     115.569  95.220 162.865  1.00 80.16           C  
ATOM   1279  CE  LYS A 166     114.557  94.188 162.395  1.00 77.74           C  
ATOM   1280  NZ  LYS A 166     115.192  93.128 161.565  1.00 77.42           N  
ATOM   1281  N   MET A 167     114.944 100.040 159.944  1.00 75.10           N  
ATOM   1282  CA  MET A 167     114.873 101.370 160.543  1.00 70.32           C  
ATOM   1283  C   MET A 167     113.863 101.504 161.680  1.00 73.10           C  
ATOM   1284  O   MET A 167     114.207 102.140 162.691  1.00 67.75           O  
ATOM   1285  CB  MET A 167     114.590 102.401 159.446  1.00 69.07           C  
ATOM   1286  N   PRO A 168     112.627 100.969 161.599  1.00 69.25           N  
ATOM   1287  CA  PRO A 168     111.663 101.213 162.683  1.00 69.86           C  
ATOM   1288  C   PRO A 168     112.004 100.466 163.962  1.00 69.52           C  
ATOM   1289  O   PRO A 168     111.466  99.386 164.224  1.00 61.66           O  
ATOM   1290  CB  PRO A 168     110.340 100.719 162.089  1.00 61.42           C  
ATOM   1291  CG  PRO A 168     110.749  99.676 161.134  1.00 64.17           C  
ATOM   1292  CD  PRO A 168     112.012 100.186 160.512  1.00 62.39           C  
ATOM   1293  N   ILE A 169     112.898 101.035 164.768  1.00 72.17           N  
ATOM   1294  CA  ILE A 169     113.350 100.354 165.977  1.00 68.18           C  
ATOM   1295  C   ILE A 169     112.257 100.430 167.034  1.00 73.57           C  
ATOM   1296  O   ILE A 169     111.881 101.518 167.481  1.00 75.28           O  
ATOM   1297  CB  ILE A 169     114.656 100.966 166.491  1.00 72.23           C  
ATOM   1298  CG1 ILE A 169     115.600 101.246 165.324  1.00 74.21           C  
ATOM   1299  CG2 ILE A 169     115.301 100.041 167.505  1.00 73.57           C  
ATOM   1300  CD1 ILE A 169     116.445 102.485 165.502  1.00 70.15           C  
ATOM   1301  N   GLN A 170     111.751  99.274 167.447  1.00 89.52           N  
ATOM   1302  CA  GLN A 170     110.722  99.208 168.475  1.00 91.89           C  
ATOM   1303  C   GLN A 170     111.377  99.129 169.848  1.00 92.01           C  
ATOM   1304  O   GLN A 170     112.208  98.251 170.095  1.00 89.66           O  
ATOM   1305  CB  GLN A 170     109.812  98.001 168.249  1.00 89.59           C  
ATOM   1306  CG  GLN A 170     108.956  97.618 169.448  1.00 93.13           C  
ATOM   1307  CD  GLN A 170     108.101  98.762 169.954  1.00 93.19           C  
ATOM   1308  OE1 GLN A 170     108.459  99.441 170.916  1.00 95.21           O  
ATOM   1309  NE2 GLN A 170     106.961  98.978 169.310  1.00 86.69           N  
ATOM   1310  N   ASN A 171     111.002 100.048 170.737  1.00104.02           N  
ATOM   1311  CA  ASN A 171     111.555 100.056 172.090  1.00105.39           C  
ATOM   1312  C   ASN A 171     110.525 100.559 173.098  1.00106.88           C  
ATOM   1313  O   ASN A 171     109.962 101.646 172.956  1.00105.88           O  
ATOM   1314  CB  ASN A 171     112.897 100.817 172.129  1.00104.78           C  
ATOM   1315  CG  ASN A 171     112.775 102.345 172.235  1.00104.36           C  
ATOM   1316  OD1 ASN A 171     113.720 103.069 172.525  1.00101.72           O  
ATOM   1317  ND2 ASN A 171     111.567 102.830 171.997  1.00103.27           N  
ATOM   1318  N   GLY A 172     110.189  99.698 174.054  1.00107.21           N  
ATOM   1319  CA  GLY A 172     109.334 100.066 175.163  1.00105.72           C  
ATOM   1320  C   GLY A 172     107.881 100.202 174.762  1.00106.10           C  
ATOM   1321  O   GLY A 172     107.064  99.313 175.019  1.00107.29           O  
ATOM   1322  N   GLY A 173     107.553 101.324 174.124  1.00100.35           N  
ATOM   1323  CA  GLY A 173     106.243 101.537 173.541  1.00101.08           C  
ATOM   1324  C   GLY A 173     106.303 102.403 172.299  1.00100.85           C  
ATOM   1325  O   GLY A 173     105.269 102.802 171.757  1.00 98.88           O  
ATOM   1326  N   ALA A 174     107.518 102.698 171.843  1.00 91.85           N  
ATOM   1327  CA  ALA A 174     107.756 103.669 170.788  1.00 88.52           C  
ATOM   1328  C   ALA A 174     108.420 103.007 169.589  1.00 85.33           C  
ATOM   1329  O   ALA A 174     109.069 101.964 169.712  1.00 86.87           O  
ATOM   1330  CB  ALA A 174     108.634 104.821 171.287  1.00 88.09           C  
ATOM   1331  N   ASN A 175     108.247 103.630 168.426  1.00 73.31           N  
ATOM   1332  CA  ASN A 175     108.796 103.147 167.162  1.00 75.96           C  
ATOM   1333  C   ASN A 175     109.703 104.235 166.594  1.00 71.24           C  
ATOM   1334  O   ASN A 175     109.255 105.101 165.840  1.00 73.81           O  
ATOM   1335  CB  ASN A 175     107.679 102.782 166.191  1.00 75.89           C  
ATOM   1336  CG  ASN A 175     106.993 101.481 166.557  1.00 79.12           C  
ATOM   1337  OD1 ASN A 175     107.647 100.465 166.790  1.00 79.19           O  
ATOM   1338  ND2 ASN A 175     105.666 101.508 166.617  1.00 80.40           N  
ATOM   1339  N   LEU A 176     110.980 104.186 166.959  1.00 60.81           N  
ATOM   1340  CA  LEU A 176     111.939 105.162 166.466  1.00 61.25           C  
ATOM   1341  C   LEU A 176     112.151 105.020 164.964  1.00 60.20           C  
ATOM   1342  O   LEU A 176     112.300 103.912 164.438  1.00 72.70           O  
ATOM   1343  CB  LEU A 176     113.276 105.009 167.189  1.00 67.67           C  
ATOM   1344  CG  LEU A 176     113.431 105.781 168.497  1.00 65.61           C  
ATOM   1345  CD1 LEU A 176     113.091 104.902 169.685  1.00 67.34           C  
ATOM   1346  CD2 LEU A 176     114.839 106.328 168.613  1.00 61.09           C  
ATOM   1347  N   CYS A 177     112.185 106.163 164.288  1.00 44.09           N  
ATOM   1348  CA  CYS A 177     112.474 106.312 162.866  1.00 45.99           C  
ATOM   1349  C   CYS A 177     113.522 107.388 162.645  1.00 56.43           C  
ATOM   1350  O   CYS A 177     113.374 108.268 161.796  1.00 64.13           O  
ATOM   1351  CB  CYS A 177     111.216 106.649 162.077  1.00 65.69           C  
ATOM   1352  SG  CYS A 177     111.123 105.969 160.399  1.00 95.42           S  
ATOM   1353  N   SER A 178     114.600 107.341 163.420  1.00 59.43           N  
ATOM   1354  CA  SER A 178     115.666 108.329 163.337  1.00 55.52           C  
ATOM   1355  C   SER A 178     116.962 107.652 162.920  1.00 49.10           C  
ATOM   1356  O   SER A 178     117.420 106.717 163.584  1.00 49.20           O  
ATOM   1357  CB  SER A 178     115.850 109.050 164.674  1.00 49.49           C  
ATOM   1358  OG  SER A 178     115.963 108.121 165.737  1.00 54.13           O  
ATOM   1359  N   SER A 179     117.549 108.130 161.821  1.00 38.05           N  
ATOM   1360  CA  SER A 179     118.847 107.617 161.399  1.00 38.34           C  
ATOM   1361  C   SER A 179     119.961 108.153 162.287  1.00 51.86           C  
ATOM   1362  O   SER A 179     120.944 107.451 162.553  1.00 52.45           O  
ATOM   1363  CB  SER A 179     119.108 107.981 159.940  1.00 43.69           C  
ATOM   1364  OG  SER A 179     119.155 109.385 159.769  1.00 43.12           O  
ATOM   1365  N   PHE A 180     119.824 109.391 162.754  1.00 64.46           N  
ATOM   1366  CA  PHE A 180     120.830 110.025 163.602  1.00 54.41           C  
ATOM   1367  C   PHE A 180     120.573 109.618 165.044  1.00 53.48           C  
ATOM   1368  O   PHE A 180     119.626 110.088 165.678  1.00 56.86           O  
ATOM   1369  CB  PHE A 180     120.795 111.539 163.439  1.00 34.50           C  
ATOM   1370  CG  PHE A 180     121.668 112.045 162.336  1.00 35.35           C  
ATOM   1371  CD1 PHE A 180     122.950 111.560 162.177  1.00 41.78           C  
ATOM   1372  CD2 PHE A 180     121.208 113.005 161.458  1.00 43.89           C  
ATOM   1373  CE1 PHE A 180     123.756 112.023 161.163  1.00 45.37           C  
ATOM   1374  CE2 PHE A 180     122.010 113.470 160.443  1.00 49.61           C  
ATOM   1375  CZ  PHE A 180     123.285 112.979 160.295  1.00 47.57           C  
ATOM   1376  N   SER A 181     121.417 108.737 165.565  1.00 64.11           N  
ATOM   1377  CA  SER A 181     121.324 108.286 166.942  1.00 70.06           C  
ATOM   1378  C   SER A 181     122.717 108.276 167.551  1.00 77.37           C  
ATOM   1379  O   SER A 181     123.721 108.175 166.840  1.00 77.56           O  
ATOM   1380  CB  SER A 181     120.693 106.891 167.032  1.00 69.57           C  
ATOM   1381  OG  SER A 181     120.007 106.718 168.259  1.00 71.52           O  
ATOM   1382  N   ILE A 182     122.775 108.391 168.874  1.00 81.51           N  
ATOM   1383  CA  ILE A 182     124.037 108.396 169.602  1.00 73.98           C  
ATOM   1384  C   ILE A 182     124.285 107.004 170.166  1.00 75.69           C  
ATOM   1385  O   ILE A 182     123.426 106.431 170.847  1.00 74.20           O  
ATOM   1386  CB  ILE A 182     124.046 109.471 170.705  1.00 73.85           C  
ATOM   1387  CG1 ILE A 182     125.431 109.556 171.342  1.00 75.12           C  
ATOM   1388  CG2 ILE A 182     122.951 109.237 171.741  1.00 78.09           C  
ATOM   1389  CD1 ILE A 182     126.497 110.019 170.384  1.00 81.91           C  
ATOM   1390  N   CYS A 183     125.450 106.444 169.851  1.00 98.57           N  
ATOM   1391  CA  CYS A 183     125.821 105.114 170.307  1.00100.58           C  
ATOM   1392  C   CYS A 183     127.322 105.081 170.542  1.00100.13           C  
ATOM   1393  O   CYS A 183     128.079 105.819 169.905  1.00100.03           O  
ATOM   1394  CB  CYS A 183     125.427 104.034 169.294  1.00101.69           C  
ATOM   1395  SG  CYS A 183     123.686 104.024 168.821  1.00107.78           S  
ATOM   1396  N   HIS A 184     127.752 104.207 171.451  1.00 99.24           N  
ATOM   1397  CA  HIS A 184     129.172 104.074 171.773  1.00101.22           C  
ATOM   1398  C   HIS A 184     129.853 103.231 170.690  1.00101.43           C  
ATOM   1399  O   HIS A 184     130.337 102.123 170.919  1.00105.55           O  
ATOM   1400  CB  HIS A 184     129.342 103.473 173.163  1.00104.97           C  
ATOM   1401  CG  HIS A 184     130.764 103.382 173.630  1.00104.67           C  
ATOM   1402  ND1 HIS A 184     131.095 103.283 174.965  1.00103.30           N  
ATOM   1403  CD2 HIS A 184     131.938 103.404 172.954  1.00102.23           C  
ATOM   1404  CE1 HIS A 184     132.409 103.229 175.088  1.00102.67           C  
ATOM   1405  NE2 HIS A 184     132.944 103.301 173.883  1.00102.86           N  
ATOM   1406  N   THR A 185     129.850 103.778 169.478  1.00 88.57           N  
ATOM   1407  CA  THR A 185     130.462 103.128 168.328  1.00 91.52           C  
ATOM   1408  C   THR A 185     130.622 104.164 167.226  1.00 90.15           C  
ATOM   1409  O   THR A 185     130.069 105.264 167.294  1.00 88.40           O  
ATOM   1410  CB  THR A 185     129.631 101.935 167.841  1.00 91.66           C  
ATOM   1411  OG1 THR A 185     130.486 100.991 167.184  1.00 90.10           O  
ATOM   1412  CG2 THR A 185     128.547 102.390 166.876  1.00 91.38           C  
ATOM   1413  N   PHE A 186     131.396 103.801 166.208  1.00 84.22           N  
ATOM   1414  CA  PHE A 186     131.571 104.630 165.025  1.00 84.19           C  
ATOM   1415  C   PHE A 186     130.983 103.905 163.825  1.00 82.17           C  
ATOM   1416  O   PHE A 186     131.362 102.765 163.535  1.00 82.96           O  
ATOM   1417  CB  PHE A 186     133.044 104.956 164.787  1.00 84.83           C  
ATOM   1418  CG  PHE A 186     133.259 106.239 164.041  1.00 84.85           C  
ATOM   1419  CD1 PHE A 186     132.907 107.450 164.610  1.00 82.00           C  
ATOM   1420  CD2 PHE A 186     133.801 106.235 162.769  1.00 83.66           C  
ATOM   1421  CE1 PHE A 186     133.099 108.633 163.929  1.00 80.47           C  
ATOM   1422  CE2 PHE A 186     133.995 107.416 162.083  1.00 86.59           C  
ATOM   1423  CZ  PHE A 186     133.643 108.617 162.665  1.00 83.35           C  
ATOM   1424  N   GLN A 187     130.063 104.565 163.133  1.00 78.79           N  
ATOM   1425  CA  GLN A 187     129.438 104.038 161.933  1.00 80.04           C  
ATOM   1426  C   GLN A 187     129.662 105.006 160.781  1.00 80.27           C  
ATOM   1427  O   GLN A 187     130.042 106.163 160.973  1.00 80.48           O  
ATOM   1428  CB  GLN A 187     127.938 103.799 162.147  1.00 80.64           C  
ATOM   1429  CG  GLN A 187     127.549 102.333 162.252  1.00 83.79           C  
ATOM   1430  CD  GLN A 187     126.172 102.055 161.683  1.00 82.72           C  
ATOM   1431  OE1 GLN A 187     125.204 102.744 162.006  1.00 78.79           O  
ATOM   1432  NE2 GLN A 187     126.076 101.041 160.830  1.00 79.67           N  
ATOM   1433  N   TRP A 188     129.425 104.515 159.565  1.00 67.54           N  
ATOM   1434  CA  TRP A 188     129.598 105.352 158.387  1.00 63.11           C  
ATOM   1435  C   TRP A 188     128.635 106.531 158.368  1.00 61.67           C  
ATOM   1436  O   TRP A 188     128.905 107.517 157.681  1.00 66.48           O  
ATOM   1437  CB  TRP A 188     129.434 104.513 157.118  1.00 63.85           C  
ATOM   1438  CG  TRP A 188     129.360 105.320 155.855  1.00 62.97           C  
ATOM   1439  CD1 TRP A 188     128.318 105.371 154.979  1.00 66.84           C  
ATOM   1440  CD2 TRP A 188     130.368 106.192 155.330  1.00 60.57           C  
ATOM   1441  NE1 TRP A 188     128.613 106.219 153.941  1.00 65.15           N  
ATOM   1442  CE2 TRP A 188     129.866 106.737 154.133  1.00 61.25           C  
ATOM   1443  CE3 TRP A 188     131.646 106.565 155.755  1.00 64.20           C  
ATOM   1444  CZ2 TRP A 188     130.596 107.633 153.357  1.00 61.08           C  
ATOM   1445  CZ3 TRP A 188     132.369 107.454 154.983  1.00 69.91           C  
ATOM   1446  CH2 TRP A 188     131.842 107.978 153.798  1.00 65.48           C  
ATOM   1447  N   HIS A 189     127.527 106.459 159.108  1.00 65.67           N  
ATOM   1448  CA  HIS A 189     126.568 107.560 159.118  1.00 69.80           C  
ATOM   1449  C   HIS A 189     127.180 108.824 159.715  1.00 71.65           C  
ATOM   1450  O   HIS A 189     127.154 109.896 159.095  1.00 69.51           O  
ATOM   1451  CB  HIS A 189     125.320 107.147 159.897  1.00 64.71           C  
ATOM   1452  CG  HIS A 189     124.084 107.893 159.505  1.00 66.39           C  
ATOM   1453  ND1 HIS A 189     123.760 108.158 158.193  1.00 71.83           N  
ATOM   1454  CD2 HIS A 189     123.085 108.419 160.251  1.00 68.22           C  
ATOM   1455  CE1 HIS A 189     122.620 108.823 158.147  1.00 70.31           C  
ATOM   1456  NE2 HIS A 189     122.189 108.993 159.383  1.00 72.50           N  
ATOM   1457  N   GLU A 190     127.750 108.710 160.917  1.00 74.36           N  
ATOM   1458  CA  GLU A 190     128.323 109.875 161.586  1.00 69.73           C  
ATOM   1459  C   GLU A 190     129.516 110.424 160.815  1.00 67.91           C  
ATOM   1460  O   GLU A 190     129.653 111.642 160.645  1.00 72.33           O  
ATOM   1461  CB  GLU A 190     128.726 109.501 163.011  1.00 68.72           C  
ATOM   1462  CG  GLU A 190     127.573 108.984 163.858  1.00 74.80           C  
ATOM   1463  CD  GLU A 190     127.673 109.405 165.311  1.00 79.69           C  
ATOM   1464  OE1 GLU A 190     127.148 110.482 165.658  1.00 77.76           O  
ATOM   1465  OE2 GLU A 190     128.269 108.652 166.109  1.00 80.26           O  
ATOM   1466  N   ALA A 191     130.389 109.537 160.336  1.00 67.51           N  
ATOM   1467  CA  ALA A 191     131.539 109.978 159.558  1.00 69.80           C  
ATOM   1468  C   ALA A 191     131.095 110.668 158.277  1.00 68.22           C  
ATOM   1469  O   ALA A 191     131.651 111.702 157.888  1.00 66.65           O  
ATOM   1470  CB  ALA A 191     132.446 108.790 159.241  1.00 69.65           C  
ATOM   1471  N   MET A 192     130.097 110.101 157.599  1.00 64.29           N  
ATOM   1472  CA  MET A 192     129.625 110.716 156.371  1.00 61.09           C  
ATOM   1473  C   MET A 192     129.035 112.085 156.651  1.00 64.32           C  
ATOM   1474  O   MET A 192     129.230 113.004 155.859  1.00 70.65           O  
ATOM   1475  CB  MET A 192     128.603 109.819 155.672  1.00 62.02           C  
ATOM   1476  CG  MET A 192     127.593 110.583 154.834  1.00 63.65           C  
ATOM   1477  SD  MET A 192     126.141 109.636 154.352  1.00 67.60           S  
ATOM   1478  CE  MET A 192     125.212 109.675 155.872  1.00 61.38           C  
ATOM   1479  N   PHE A 193     128.346 112.249 157.783  1.00 57.92           N  
ATOM   1480  CA  PHE A 193     127.885 113.577 158.183  1.00 58.54           C  
ATOM   1481  C   PHE A 193     129.059 114.532 158.390  1.00 58.76           C  
ATOM   1482  O   PHE A 193     129.015 115.696 157.961  1.00 62.51           O  
ATOM   1483  CB  PHE A 193     127.047 113.464 159.457  1.00 57.07           C  
ATOM   1484  CG  PHE A 193     126.191 114.664 159.739  1.00 60.18           C  
ATOM   1485  CD1 PHE A 193     125.358 115.186 158.765  1.00 60.50           C  
ATOM   1486  CD2 PHE A 193     126.203 115.258 160.989  1.00 61.53           C  
ATOM   1487  CE1 PHE A 193     124.564 116.285 159.029  1.00 56.82           C  
ATOM   1488  CE2 PHE A 193     125.411 116.355 161.257  1.00 60.67           C  
ATOM   1489  CZ  PHE A 193     124.591 116.869 160.275  1.00 51.31           C  
ATOM   1490  N   LEU A 194     130.123 114.052 159.039  1.00 60.11           N  
ATOM   1491  CA  LEU A 194     131.272 114.910 159.322  1.00 57.79           C  
ATOM   1492  C   LEU A 194     131.933 115.400 158.037  1.00 63.90           C  
ATOM   1493  O   LEU A 194     132.163 116.604 157.869  1.00 65.95           O  
ATOM   1494  CB  LEU A 194     132.281 114.171 160.202  1.00 56.34           C  
ATOM   1495  CG  LEU A 194     131.882 113.974 161.665  1.00 60.78           C  
ATOM   1496  CD1 LEU A 194     133.095 113.606 162.505  1.00 59.08           C  
ATOM   1497  CD2 LEU A 194     131.202 115.218 162.213  1.00 58.34           C  
ATOM   1498  N   LEU A 195     132.255 114.484 157.117  1.00 64.82           N  
ATOM   1499  CA  LEU A 195     132.794 114.932 155.831  1.00 63.56           C  
ATOM   1500  C   LEU A 195     131.776 115.744 155.041  1.00 59.27           C  
ATOM   1501  O   LEU A 195     132.148 116.725 154.389  1.00 59.91           O  
ATOM   1502  CB  LEU A 195     133.332 113.775 154.979  1.00 63.75           C  
ATOM   1503  CG  LEU A 195     134.461 112.809 155.375  1.00 63.86           C  
ATOM   1504  CD1 LEU A 195     134.195 111.892 156.535  1.00 60.44           C  
ATOM   1505  CD2 LEU A 195     134.859 111.994 154.148  1.00 62.24           C  
ATOM   1506  N   GLU A 196     130.495 115.365 155.107  1.00 60.41           N  
ATOM   1507  CA  GLU A 196     129.424 116.106 154.453  1.00 60.57           C  
ATOM   1508  C   GLU A 196     129.476 117.578 154.807  1.00 62.42           C  
ATOM   1509  O   GLU A 196     129.239 118.442 153.957  1.00 59.03           O  
ATOM   1510  CB  GLU A 196     128.076 115.524 154.875  1.00 54.94           C  
ATOM   1511  CG  GLU A 196     126.923 115.818 153.950  1.00 57.88           C  
ATOM   1512  CD  GLU A 196     125.608 115.325 154.517  1.00 69.59           C  
ATOM   1513  OE1 GLU A 196     125.229 115.781 155.616  1.00 68.39           O  
ATOM   1514  OE2 GLU A 196     124.954 114.481 153.875  1.00 72.76           O  
ATOM   1515  N   PHE A 197     129.755 117.885 156.069  1.00 61.06           N  
ATOM   1516  CA  PHE A 197     129.956 119.285 156.418  1.00 52.04           C  
ATOM   1517  C   PHE A 197     131.324 119.772 155.957  1.00 60.84           C  
ATOM   1518  O   PHE A 197     131.423 120.729 155.184  1.00 67.59           O  
ATOM   1519  CB  PHE A 197     129.796 119.508 157.915  1.00 54.33           C  
ATOM   1520  CG  PHE A 197     130.075 120.919 158.329  1.00 56.74           C  
ATOM   1521  CD1 PHE A 197     129.369 121.963 157.762  1.00 55.38           C  
ATOM   1522  CD2 PHE A 197     131.053 121.207 159.259  1.00 61.43           C  
ATOM   1523  CE1 PHE A 197     129.624 123.264 158.123  1.00 54.17           C  
ATOM   1524  CE2 PHE A 197     131.313 122.507 159.625  1.00 59.11           C  
ATOM   1525  CZ  PHE A 197     130.597 123.537 159.055  1.00 58.03           C  
ATOM   1526  N   PHE A 198     132.392 119.104 156.402  1.00 60.30           N  
ATOM   1527  CA  PHE A 198     133.736 119.667 156.289  1.00 59.16           C  
ATOM   1528  C   PHE A 198     134.174 119.837 154.838  1.00 66.61           C  
ATOM   1529  O   PHE A 198     134.461 120.956 154.396  1.00 67.38           O  
ATOM   1530  CB  PHE A 198     134.734 118.796 157.052  1.00 57.19           C  
ATOM   1531  CG  PHE A 198     135.042 119.299 158.429  1.00 59.84           C  
ATOM   1532  CD1 PHE A 198     134.283 120.305 158.995  1.00 57.37           C  
ATOM   1533  CD2 PHE A 198     136.096 118.773 159.154  1.00 65.63           C  
ATOM   1534  CE1 PHE A 198     134.561 120.775 160.259  1.00 62.40           C  
ATOM   1535  CE2 PHE A 198     136.382 119.239 160.421  1.00 62.80           C  
ATOM   1536  CZ  PHE A 198     135.613 120.242 160.974  1.00 64.17           C  
ATOM   1537  N   LEU A 199     134.246 118.740 154.084  1.00 63.33           N  
ATOM   1538  CA  LEU A 199     134.852 118.818 152.755  1.00 61.56           C  
ATOM   1539  C   LEU A 199     134.102 119.768 151.830  1.00 62.77           C  
ATOM   1540  O   LEU A 199     134.750 120.640 151.222  1.00 64.42           O  
ATOM   1541  CB  LEU A 199     134.981 117.410 152.162  1.00 58.69           C  
ATOM   1542  CG  LEU A 199     136.350 116.741 152.254  1.00 65.23           C  
ATOM   1543  CD1 LEU A 199     136.251 115.293 151.814  1.00 61.47           C  
ATOM   1544  CD2 LEU A 199     137.359 117.493 151.406  1.00 66.53           C  
ATOM   1545  N   PRO A 200     132.775 119.681 151.674  1.00 53.17           N  
ATOM   1546  CA  PRO A 200     132.081 120.738 150.928  1.00 42.72           C  
ATOM   1547  C   PRO A 200     132.241 122.112 151.543  1.00 42.49           C  
ATOM   1548  O   PRO A 200     132.276 123.092 150.796  1.00 58.04           O  
ATOM   1549  CB  PRO A 200     130.617 120.288 150.932  1.00 46.14           C  
ATOM   1550  CG  PRO A 200     130.626 118.879 151.277  1.00 54.24           C  
ATOM   1551  CD  PRO A 200     131.916 118.505 151.890  1.00 55.75           C  
ATOM   1552  N   LEU A 201     132.336 122.231 152.871  1.00 37.21           N  
ATOM   1553  CA  LEU A 201     132.587 123.548 153.450  1.00 45.22           C  
ATOM   1554  C   LEU A 201     133.931 124.092 152.998  1.00 45.61           C  
ATOM   1555  O   LEU A 201     134.039 125.264 152.627  1.00 54.90           O  
ATOM   1556  CB  LEU A 201     132.538 123.505 154.975  1.00 50.57           C  
ATOM   1557  CG  LEU A 201     133.070 124.776 155.644  1.00 46.13           C  
ATOM   1558  CD1 LEU A 201     132.097 125.926 155.456  1.00 44.74           C  
ATOM   1559  CD2 LEU A 201     133.366 124.556 157.117  1.00 48.43           C  
ATOM   1560  N   GLY A 202     134.967 123.254 153.019  1.00 37.14           N  
ATOM   1561  CA  GLY A 202     136.267 123.703 152.553  1.00 45.76           C  
ATOM   1562  C   GLY A 202     136.243 124.113 151.095  1.00 43.38           C  
ATOM   1563  O   GLY A 202     136.769 125.165 150.722  1.00 31.03           O  
ATOM   1564  N   ILE A 203     135.610 123.295 150.250  1.00 52.71           N  
ATOM   1565  CA  ILE A 203     135.565 123.605 148.824  1.00 44.97           C  
ATOM   1566  C   ILE A 203     134.780 124.887 148.576  1.00 40.13           C  
ATOM   1567  O   ILE A 203     135.198 125.742 147.788  1.00 48.61           O  
ATOM   1568  CB  ILE A 203     134.981 122.423 148.032  1.00 46.17           C  
ATOM   1569  CG1 ILE A 203     135.843 121.175 148.223  1.00 52.11           C  
ATOM   1570  CG2 ILE A 203     134.898 122.771 146.562  1.00 44.11           C  
ATOM   1571  CD1 ILE A 203     135.088 119.881 148.043  1.00 40.91           C  
ATOM   1572  N   ILE A 204     133.635 125.045 149.245  1.00 39.93           N  
ATOM   1573  CA  ILE A 204     132.806 126.230 149.056  1.00 33.97           C  
ATOM   1574  C   ILE A 204     133.529 127.477 149.545  1.00 50.37           C  
ATOM   1575  O   ILE A 204     133.514 128.517 148.878  1.00 56.49           O  
ATOM   1576  CB  ILE A 204     131.452 126.047 149.764  1.00 28.58           C  
ATOM   1577  CG1 ILE A 204     130.546 125.124 148.954  1.00 39.73           C  
ATOM   1578  CG2 ILE A 204     130.773 127.382 149.976  1.00 35.23           C  
ATOM   1579  CD1 ILE A 204     129.243 124.797 149.645  1.00 44.63           C  
ATOM   1580  N   LEU A 205     134.166 127.400 150.716  1.00 48.65           N  
ATOM   1581  CA  LEU A 205     134.896 128.547 151.242  1.00 38.47           C  
ATOM   1582  C   LEU A 205     136.049 128.931 150.329  1.00 48.84           C  
ATOM   1583  O   LEU A 205     136.249 130.115 150.035  1.00 55.35           O  
ATOM   1584  CB  LEU A 205     135.402 128.235 152.650  1.00 43.47           C  
ATOM   1585  CG  LEU A 205     136.344 129.239 153.310  1.00 56.98           C  
ATOM   1586  CD1 LEU A 205     135.837 129.597 154.692  1.00 57.61           C  
ATOM   1587  CD2 LEU A 205     137.755 128.676 153.391  1.00 52.38           C  
ATOM   1588  N   PHE A 206     136.812 127.942 149.858  1.00 51.97           N  
ATOM   1589  CA  PHE A 206     137.921 128.226 148.954  1.00 59.74           C  
ATOM   1590  C   PHE A 206     137.423 128.847 147.657  1.00 46.30           C  
ATOM   1591  O   PHE A 206     137.993 129.833 147.174  1.00 39.96           O  
ATOM   1592  CB  PHE A 206     138.701 126.935 148.696  1.00 64.09           C  
ATOM   1593  CG  PHE A 206     139.786 127.055 147.662  1.00 57.44           C  
ATOM   1594  CD1 PHE A 206     139.497 126.990 146.312  1.00 49.99           C  
ATOM   1595  CD2 PHE A 206     141.101 127.219 148.050  1.00 56.08           C  
ATOM   1596  CE1 PHE A 206     140.496 127.092 145.373  1.00 52.08           C  
ATOM   1597  CE2 PHE A 206     142.104 127.323 147.114  1.00 55.68           C  
ATOM   1598  CZ  PHE A 206     141.800 127.260 145.773  1.00 55.24           C  
ATOM   1599  N   CYS A 207     136.355 128.289 147.081  1.00 47.96           N  
ATOM   1600  CA  CYS A 207     135.825 128.819 145.832  1.00 51.31           C  
ATOM   1601  C   CYS A 207     135.318 130.242 146.006  1.00 63.67           C  
ATOM   1602  O   CYS A 207     135.599 131.112 145.175  1.00 73.08           O  
ATOM   1603  CB  CYS A 207     134.714 127.910 145.312  1.00 48.07           C  
ATOM   1604  SG  CYS A 207     135.302 126.329 144.669  1.00 58.73           S  
ATOM   1605  N   SER A 208     134.576 130.505 147.084  1.00 59.58           N  
ATOM   1606  CA  SER A 208     134.055 131.848 147.312  1.00 54.69           C  
ATOM   1607  C   SER A 208     135.181 132.846 147.543  1.00 52.94           C  
ATOM   1608  O   SER A 208     135.147 133.963 147.011  1.00 55.85           O  
ATOM   1609  CB  SER A 208     133.090 131.840 148.494  1.00 56.32           C  
ATOM   1610  OG  SER A 208     132.140 130.798 148.360  1.00 57.70           O  
ATOM   1611  N   ALA A 209     136.192 132.462 148.326  1.00 41.31           N  
ATOM   1612  CA  ALA A 209     137.316 133.358 148.568  1.00 46.64           C  
ATOM   1613  C   ALA A 209     138.068 133.660 147.280  1.00 57.58           C  
ATOM   1614  O   ALA A 209     138.426 134.815 147.019  1.00 60.68           O  
ATOM   1615  CB  ALA A 209     138.257 132.751 149.606  1.00 49.10           C  
ATOM   1616  N   ARG A 210     138.311 132.638 146.457  1.00 57.32           N  
ATOM   1617  CA  ARG A 210     139.012 132.862 145.198  1.00 50.98           C  
ATOM   1618  C   ARG A 210     138.195 133.743 144.265  1.00 46.49           C  
ATOM   1619  O   ARG A 210     138.744 134.634 143.607  1.00 52.94           O  
ATOM   1620  CB  ARG A 210     139.336 131.529 144.531  1.00 48.58           C  
ATOM   1621  CG  ARG A 210     140.411 130.728 145.239  1.00 52.79           C  
ATOM   1622  CD  ARG A 210     141.678 130.662 144.413  1.00 48.50           C  
ATOM   1623  NE  ARG A 210     142.306 131.970 144.286  1.00 49.57           N  
ATOM   1624  CZ  ARG A 210     143.095 132.511 145.203  1.00 55.33           C  
ATOM   1625  NH1 ARG A 210     143.371 131.884 146.335  1.00 53.15           N  
ATOM   1626  NH2 ARG A 210     143.622 133.711 144.979  1.00 55.74           N  
ATOM   1627  N   ILE A 211     136.882 133.515 144.197  1.00 40.62           N  
ATOM   1628  CA  ILE A 211     136.029 134.338 143.345  1.00 44.56           C  
ATOM   1629  C   ILE A 211     136.094 135.793 143.786  1.00 52.08           C  
ATOM   1630  O   ILE A 211     136.281 136.702 142.967  1.00 56.33           O  
ATOM   1631  CB  ILE A 211     134.582 133.816 143.365  1.00 45.30           C  
ATOM   1632  CG1 ILE A 211     134.475 132.482 142.632  1.00 49.01           C  
ATOM   1633  CG2 ILE A 211     133.649 134.831 142.738  1.00 46.49           C  
ATOM   1634  CD1 ILE A 211     133.215 131.721 142.961  1.00 51.52           C  
ATOM   1635  N   ILE A 212     135.949 136.032 145.090  1.00 56.37           N  
ATOM   1636  CA  ILE A 212     135.947 137.399 145.600  1.00 52.15           C  
ATOM   1637  C   ILE A 212     137.287 138.068 145.330  1.00 55.16           C  
ATOM   1638  O   ILE A 212     137.346 139.212 144.866  1.00 56.01           O  
ATOM   1639  CB  ILE A 212     135.603 137.412 147.099  1.00 57.29           C  
ATOM   1640  CG1 ILE A 212     134.154 136.977 147.316  1.00 59.06           C  
ATOM   1641  CG2 ILE A 212     135.840 138.788 147.687  1.00 58.66           C  
ATOM   1642  CD1 ILE A 212     133.154 137.822 146.580  1.00 56.54           C  
ATOM   1643  N   TRP A 213     138.385 137.359 145.605  1.00 66.76           N  
ATOM   1644  CA  TRP A 213     139.707 137.949 145.422  1.00 70.28           C  
ATOM   1645  C   TRP A 213     139.983 138.258 143.956  1.00 71.60           C  
ATOM   1646  O   TRP A 213     140.508 139.328 143.630  1.00 66.47           O  
ATOM   1647  CB  TRP A 213     140.778 137.017 145.986  1.00 65.77           C  
ATOM   1648  CG  TRP A 213     142.041 137.722 146.356  1.00 69.82           C  
ATOM   1649  CD1 TRP A 213     142.329 139.041 146.161  1.00 70.89           C  
ATOM   1650  CD2 TRP A 213     143.191 137.148 146.987  1.00 73.97           C  
ATOM   1651  NE1 TRP A 213     143.588 139.324 146.631  1.00 77.39           N  
ATOM   1652  CE2 TRP A 213     144.139 138.179 147.143  1.00 77.70           C  
ATOM   1653  CE3 TRP A 213     143.512 135.864 147.434  1.00 70.45           C  
ATOM   1654  CZ2 TRP A 213     145.385 137.964 147.728  1.00 72.28           C  
ATOM   1655  CZ3 TRP A 213     144.751 135.653 148.014  1.00 70.54           C  
ATOM   1656  CH2 TRP A 213     145.671 136.698 148.156  1.00 69.80           C  
ATOM   1657  N   SER A 214     139.638 137.335 143.055  1.00 70.39           N  
ATOM   1658  CA  SER A 214     139.881 137.566 141.637  1.00 63.27           C  
ATOM   1659  C   SER A 214     139.021 138.704 141.107  1.00 63.26           C  
ATOM   1660  O   SER A 214     139.494 139.527 140.315  1.00 69.10           O  
ATOM   1661  CB  SER A 214     139.624 136.287 140.843  1.00 63.41           C  
ATOM   1662  OG  SER A 214     138.253 135.938 140.876  1.00 67.47           O  
ATOM   1663  N   LEU A 215     137.755 138.769 141.526  1.00 58.40           N  
ATOM   1664  CA  LEU A 215     136.893 139.849 141.062  1.00 60.85           C  
ATOM   1665  C   LEU A 215     137.363 141.198 141.589  1.00 65.83           C  
ATOM   1666  O   LEU A 215     137.353 142.193 140.854  1.00 69.56           O  
ATOM   1667  CB  LEU A 215     135.448 139.579 141.473  1.00 61.24           C  
ATOM   1668  CG  LEU A 215     134.657 138.700 140.504  1.00 58.94           C  
ATOM   1669  CD1 LEU A 215     133.331 138.273 141.112  1.00 65.50           C  
ATOM   1670  CD2 LEU A 215     134.437 139.433 139.194  1.00 58.49           C  
ATOM   1671  N   ARG A 216     137.783 141.257 142.854  1.00 70.41           N  
ATOM   1672  CA  ARG A 216     138.216 142.529 143.421  1.00 73.32           C  
ATOM   1673  C   ARG A 216     139.543 142.981 142.827  1.00 72.83           C  
ATOM   1674  O   ARG A 216     139.721 144.167 142.527  1.00 72.49           O  
ATOM   1675  CB  ARG A 216     138.313 142.421 144.942  1.00 75.94           C  
ATOM   1676  CG  ARG A 216     136.967 142.341 145.639  1.00 74.12           C  
ATOM   1677  CD  ARG A 216     136.950 143.179 146.902  1.00 70.18           C  
ATOM   1678  NE  ARG A 216     137.593 142.493 148.015  1.00 73.15           N  
ATOM   1679  CZ  ARG A 216     136.950 142.018 149.073  1.00 77.13           C  
ATOM   1680  NH1 ARG A 216     135.637 142.133 149.192  1.00 74.78           N  
ATOM   1681  NH2 ARG A 216     137.641 141.413 150.034  1.00 78.40           N  
ATOM   1682  N   GLN A 217     140.488 142.055 142.648  1.00 79.83           N  
ATOM   1683  CA  GLN A 217     141.776 142.430 142.075  1.00 83.21           C  
ATOM   1684  C   GLN A 217     141.642 142.837 140.615  1.00 81.06           C  
ATOM   1685  O   GLN A 217     142.410 143.678 140.135  1.00 81.97           O  
ATOM   1686  CB  GLN A 217     142.777 141.284 142.214  1.00 81.22           C  
ATOM   1687  CG  GLN A 217     144.229 141.731 142.163  1.00 79.88           C  
ATOM   1688  CD  GLN A 217     144.796 141.723 140.759  1.00 82.69           C  
ATOM   1689  OE1 GLN A 217     144.124 141.328 139.807  1.00 81.87           O  
ATOM   1690  NE2 GLN A 217     146.042 142.159 140.622  1.00 80.23           N  
ATOM   1691  N   ARG A 218     140.687 142.252 139.892  1.00 68.82           N  
ATOM   1692  CA  ARG A 218     140.437 142.672 138.521  1.00 70.56           C  
ATOM   1693  C   ARG A 218     139.811 144.056 138.440  1.00 71.06           C  
ATOM   1694  O   ARG A 218     139.719 144.609 137.339  1.00 73.38           O  
ATOM   1695  CB  ARG A 218     139.542 141.659 137.811  1.00 71.22           C  
ATOM   1696  CG  ARG A 218     140.297 140.501 137.186  1.00 66.90           C  
ATOM   1697  CD  ARG A 218     139.344 139.430 136.692  1.00 65.33           C  
ATOM   1698  NE  ARG A 218     140.046 138.210 136.316  1.00 68.29           N  
ATOM   1699  CZ  ARG A 218     139.454 137.124 135.842  1.00 71.51           C  
ATOM   1700  NH1 ARG A 218     138.145 137.073 135.661  1.00 67.24           N  
ATOM   1701  NH2 ARG A 218     140.195 136.062 135.537  1.00 70.52           N  
ATOM   1702  N   GLN A 219     139.370 144.615 139.567  1.00 81.36           N  
ATOM   1703  CA  GLN A 219     138.809 145.962 139.647  1.00 85.12           C  
ATOM   1704  C   GLN A 219     137.555 146.124 138.796  1.00 84.97           C  
ATOM   1705  O   GLN A 219     137.187 147.246 138.437  1.00 86.92           O  
ATOM   1706  CB  GLN A 219     139.850 147.024 139.263  1.00 84.44           C  
ATOM   1707  CG  GLN A 219     141.164 147.044 140.076  1.00 85.96           C  
ATOM   1708  CD  GLN A 219     141.017 146.969 141.602  1.00 87.84           C  
ATOM   1709  OE1 GLN A 219     139.919 146.908 142.153  1.00 89.93           O  
ATOM   1710  NE2 GLN A 219     142.154 146.969 142.288  1.00 85.45           N  
ATOM   1711  N   MET A 220     136.886 145.024 138.465  1.00 82.29           N  
ATOM   1712  CA  MET A 220     135.620 145.081 137.750  1.00 83.95           C  
ATOM   1713  C   MET A 220     134.422 145.083 138.686  1.00 87.23           C  
ATOM   1714  O   MET A 220     133.282 145.029 138.213  1.00 88.06           O  
ATOM   1715  CB  MET A 220     135.507 143.910 136.767  1.00 85.40           C  
ATOM   1716  CG  MET A 220     136.074 142.600 137.280  1.00 84.92           C  
ATOM   1717  SD  MET A 220     135.606 141.198 136.249  1.00 87.64           S  
ATOM   1718  CE  MET A 220     135.705 141.930 134.619  1.00 84.79           C  
ATOM   1719  N   ASP A 221     134.652 145.142 139.999  1.00 93.24           N  
ATOM   1720  CA  ASP A 221     133.564 145.172 140.966  1.00 95.19           C  
ATOM   1721  C   ASP A 221     132.810 146.496 140.973  1.00 94.69           C  
ATOM   1722  O   ASP A 221     131.754 146.583 141.609  1.00 91.57           O  
ATOM   1723  CB  ASP A 221     134.106 144.882 142.366  1.00 90.93           C  
ATOM   1724  CG  ASP A 221     135.176 145.865 142.786  1.00 91.23           C  
ATOM   1725  OD1 ASP A 221     135.785 146.494 141.897  1.00 91.87           O  
ATOM   1726  OD2 ASP A 221     135.404 146.014 144.004  1.00 92.41           O  
ATOM   1727  N   ARG A 222     133.322 147.523 140.288  1.00 93.23           N  
ATOM   1728  CA  ARG A 222     132.655 148.819 140.276  1.00 92.48           C  
ATOM   1729  C   ARG A 222     131.297 148.772 139.588  1.00 93.82           C  
ATOM   1730  O   ARG A 222     130.495 149.693 139.771  1.00 96.66           O  
ATOM   1731  CB  ARG A 222     133.543 149.862 139.596  1.00 91.94           C  
ATOM   1732  CG  ARG A 222     133.586 149.751 138.081  1.00 93.06           C  
ATOM   1733  CD  ARG A 222     134.719 150.582 137.498  1.00 93.53           C  
ATOM   1734  NE  ARG A 222     135.309 149.950 136.324  1.00 95.92           N  
ATOM   1735  CZ  ARG A 222     136.515 149.400 136.297  1.00 94.13           C  
ATOM   1736  NH1 ARG A 222     137.296 149.392 137.364  1.00 93.43           N  
ATOM   1737  NH2 ARG A 222     136.949 148.843 135.170  1.00 90.36           N  
ATOM   1738  N   HIS A 223     131.025 147.731 138.805  1.00 88.94           N  
ATOM   1739  CA  HIS A 223     129.735 147.608 138.142  1.00 89.20           C  
ATOM   1740  C   HIS A 223     128.624 147.430 139.168  1.00 90.06           C  
ATOM   1741  O   HIS A 223     128.811 146.791 140.207  1.00 87.94           O  
ATOM   1742  CB  HIS A 223     129.749 146.428 137.173  1.00 86.88           C  
ATOM   1743  CG  HIS A 223     130.745 146.569 136.066  1.00 87.70           C  
ATOM   1744  ND1 HIS A 223     131.750 145.652 135.849  1.00 88.91           N  
ATOM   1745  CD2 HIS A 223     130.891 147.520 135.114  1.00 89.48           C  
ATOM   1746  CE1 HIS A 223     132.472 146.031 134.810  1.00 90.01           C  
ATOM   1747  NE2 HIS A 223     131.972 147.162 134.346  1.00 91.60           N  
ATOM   1748  N   ALA A 224     127.456 148.001 138.871  1.00 80.80           N  
ATOM   1749  CA  ALA A 224     126.344 147.967 139.810  1.00 78.19           C  
ATOM   1750  C   ALA A 224     125.724 146.584 139.953  1.00 79.15           C  
ATOM   1751  O   ALA A 224     124.976 146.360 140.909  1.00 80.60           O  
ATOM   1752  CB  ALA A 224     125.270 148.970 139.389  1.00 79.14           C  
ATOM   1753  N   LYS A 225     126.008 145.660 139.037  1.00 77.72           N  
ATOM   1754  CA  LYS A 225     125.454 144.313 139.094  1.00 77.11           C  
ATOM   1755  C   LYS A 225     126.426 143.308 139.698  1.00 80.25           C  
ATOM   1756  O   LYS A 225     126.000 142.331 140.321  1.00 83.65           O  
ATOM   1757  CB  LYS A 225     125.036 143.855 137.693  1.00 78.00           C  
ATOM   1758  CG  LYS A 225     123.689 143.151 137.646  1.00 79.54           C  
ATOM   1759  CD  LYS A 225     123.049 143.285 136.276  1.00 80.75           C  
ATOM   1760  CE  LYS A 225     121.992 142.220 136.052  1.00 76.52           C  
ATOM   1761  NZ  LYS A 225     121.447 142.271 134.669  1.00 74.22           N  
ATOM   1762  N   ILE A 226     127.727 143.531 139.524  1.00 82.07           N  
ATOM   1763  CA  ILE A 226     128.754 142.659 140.081  1.00 80.66           C  
ATOM   1764  C   ILE A 226     128.669 142.700 141.599  1.00 81.56           C  
ATOM   1765  O   ILE A 226     128.917 141.695 142.273  1.00 82.68           O  
ATOM   1766  CB  ILE A 226     130.154 143.063 139.586  1.00 79.42           C  
ATOM   1767  CG1 ILE A 226     130.235 142.912 138.070  1.00 79.94           C  
ATOM   1768  CG2 ILE A 226     131.223 142.219 140.246  1.00 78.39           C  
ATOM   1769  CD1 ILE A 226     129.862 141.533 137.584  1.00 79.62           C  
ATOM   1770  N   LYS A 227     128.315 143.864 142.147  1.00 79.45           N  
ATOM   1771  CA  LYS A 227     128.170 143.984 143.593  1.00 79.08           C  
ATOM   1772  C   LYS A 227     127.069 143.070 144.117  1.00 75.87           C  
ATOM   1773  O   LYS A 227     127.227 142.436 145.166  1.00 74.77           O  
ATOM   1774  CB  LYS A 227     127.897 145.439 143.972  1.00 78.75           C  
ATOM   1775  CG  LYS A 227     129.059 146.374 143.668  1.00 76.66           C  
ATOM   1776  CD  LYS A 227     128.614 147.825 143.601  1.00 79.17           C  
ATOM   1777  CE  LYS A 227     129.692 148.699 142.978  1.00 75.20           C  
ATOM   1778  NZ  LYS A 227     129.560 150.127 143.379  1.00 74.31           N  
ATOM   1779  N   ARG A 228     125.946 142.985 143.399  1.00 78.29           N  
ATOM   1780  CA  ARG A 228     124.873 142.086 143.813  1.00 80.77           C  
ATOM   1781  C   ARG A 228     125.316 140.629 143.748  1.00 79.58           C  
ATOM   1782  O   ARG A 228     125.004 139.835 144.643  1.00 86.47           O  
ATOM   1783  CB  ARG A 228     123.634 142.310 142.947  1.00 83.21           C  
ATOM   1784  CG  ARG A 228     122.569 141.237 143.095  1.00 79.59           C  
ATOM   1785  CD  ARG A 228     121.300 141.609 142.345  1.00 78.56           C  
ATOM   1786  NE  ARG A 228     120.473 142.539 143.103  1.00 78.80           N  
ATOM   1787  CZ  ARG A 228     119.415 143.170 142.613  1.00 79.98           C  
ATOM   1788  NH1 ARG A 228     119.020 142.990 141.364  1.00 80.99           N  
ATOM   1789  NH2 ARG A 228     118.736 144.003 143.397  1.00 80.99           N  
ATOM   1790  N   ALA A 229     126.048 140.257 142.695  1.00 74.64           N  
ATOM   1791  CA  ALA A 229     126.543 138.889 142.591  1.00 77.51           C  
ATOM   1792  C   ALA A 229     127.504 138.564 143.725  1.00 77.70           C  
ATOM   1793  O   ALA A 229     127.462 137.465 144.290  1.00 78.58           O  
ATOM   1794  CB  ALA A 229     127.220 138.678 141.238  1.00 79.40           C  
ATOM   1795  N   ILE A 230     128.380 139.507 144.071  1.00 66.93           N  
ATOM   1796  CA  ILE A 230     129.326 139.286 145.161  1.00 68.55           C  
ATOM   1797  C   ILE A 230     128.584 139.141 146.483  1.00 69.42           C  
ATOM   1798  O   ILE A 230     128.877 138.246 147.289  1.00 73.40           O  
ATOM   1799  CB  ILE A 230     130.362 140.423 145.208  1.00 66.17           C  
ATOM   1800  CG1 ILE A 230     131.528 140.117 144.269  1.00 65.51           C  
ATOM   1801  CG2 ILE A 230     130.868 140.640 146.624  1.00 66.06           C  
ATOM   1802  CD1 ILE A 230     132.405 141.308 143.985  1.00 69.94           C  
ATOM   1803  N   THR A 231     127.604 140.015 146.726  1.00 66.33           N  
ATOM   1804  CA  THR A 231     126.870 139.927 147.980  1.00 66.84           C  
ATOM   1805  C   THR A 231     126.059 138.643 148.055  1.00 57.31           C  
ATOM   1806  O   THR A 231     125.889 138.091 149.142  1.00 57.59           O  
ATOM   1807  CB  THR A 231     125.978 141.159 148.181  1.00 67.10           C  
ATOM   1808  OG1 THR A 231     125.783 141.377 149.584  1.00 69.43           O  
ATOM   1809  CG2 THR A 231     124.621 140.987 147.524  1.00 61.84           C  
ATOM   1810  N   PHE A 232     125.603 138.113 146.918  1.00 58.74           N  
ATOM   1811  CA  PHE A 232     124.850 136.866 146.978  1.00 62.42           C  
ATOM   1812  C   PHE A 232     125.758 135.649 147.090  1.00 63.72           C  
ATOM   1813  O   PHE A 232     125.361 134.649 147.691  1.00 73.17           O  
ATOM   1814  CB  PHE A 232     123.918 136.745 145.774  1.00 64.91           C  
ATOM   1815  CG  PHE A 232     122.524 137.217 146.060  1.00 63.18           C  
ATOM   1816  CD1 PHE A 232     121.794 136.659 147.094  1.00 63.25           C  
ATOM   1817  CD2 PHE A 232     121.955 138.235 145.321  1.00 64.05           C  
ATOM   1818  CE1 PHE A 232     120.520 137.094 147.375  1.00 62.33           C  
ATOM   1819  CE2 PHE A 232     120.678 138.675 145.599  1.00 67.50           C  
ATOM   1820  CZ  PHE A 232     119.962 138.104 146.629  1.00 65.65           C  
ATOM   1821  N   ILE A 233     126.973 135.711 146.546  1.00 63.50           N  
ATOM   1822  CA  ILE A 233     127.951 134.658 146.815  1.00 66.67           C  
ATOM   1823  C   ILE A 233     128.272 134.617 148.304  1.00 73.68           C  
ATOM   1824  O   ILE A 233     128.284 133.550 148.938  1.00 75.73           O  
ATOM   1825  CB  ILE A 233     129.217 134.874 145.968  1.00 60.78           C  
ATOM   1826  CG1 ILE A 233     128.994 134.366 144.546  1.00 65.17           C  
ATOM   1827  CG2 ILE A 233     130.411 134.187 146.603  1.00 63.63           C  
ATOM   1828  CD1 ILE A 233     130.144 134.642 143.617  1.00 65.84           C  
ATOM   1829  N   MET A 234     128.506 135.792 148.893  1.00 75.28           N  
ATOM   1830  CA  MET A 234     128.719 135.854 150.333  1.00 69.98           C  
ATOM   1831  C   MET A 234     127.503 135.329 151.084  1.00 72.75           C  
ATOM   1832  O   MET A 234     127.643 134.562 152.042  1.00 69.87           O  
ATOM   1833  CB  MET A 234     129.034 137.287 150.758  1.00 73.14           C  
ATOM   1834  CG  MET A 234     130.466 137.709 150.502  1.00 75.05           C  
ATOM   1835  SD  MET A 234     130.805 139.357 151.143  1.00 84.26           S  
ATOM   1836  CE  MET A 234     130.720 139.053 152.905  1.00 72.06           C  
ATOM   1837  N   VAL A 235     126.302 135.706 150.640  1.00 66.50           N  
ATOM   1838  CA  VAL A 235     125.076 135.279 151.306  1.00 63.26           C  
ATOM   1839  C   VAL A 235     124.942 133.766 151.267  1.00 64.36           C  
ATOM   1840  O   VAL A 235     124.554 133.143 152.261  1.00 64.39           O  
ATOM   1841  CB  VAL A 235     123.857 135.975 150.672  1.00 60.90           C  
ATOM   1842  CG1 VAL A 235     122.611 135.113 150.806  1.00 58.01           C  
ATOM   1843  CG2 VAL A 235     123.629 137.329 151.323  1.00 65.15           C  
ATOM   1844  N   VAL A 236     125.246 133.149 150.123  1.00 66.76           N  
ATOM   1845  CA  VAL A 236     125.119 131.700 150.031  1.00 68.87           C  
ATOM   1846  C   VAL A 236     126.144 131.025 150.934  1.00 69.77           C  
ATOM   1847  O   VAL A 236     125.838 130.012 151.582  1.00 71.39           O  
ATOM   1848  CB  VAL A 236     125.212 131.224 148.566  1.00 67.26           C  
ATOM   1849  CG1 VAL A 236     126.650 131.043 148.113  1.00 66.06           C  
ATOM   1850  CG2 VAL A 236     124.426 129.939 148.386  1.00 67.74           C  
ATOM   1851  N   ALA A 237     127.346 131.599 151.050  1.00 67.11           N  
ATOM   1852  CA  ALA A 237     128.316 131.055 151.995  1.00 66.68           C  
ATOM   1853  C   ALA A 237     127.782 131.116 153.424  1.00 71.01           C  
ATOM   1854  O   ALA A 237     127.834 130.123 154.166  1.00 68.11           O  
ATOM   1855  CB  ALA A 237     129.640 131.807 151.876  1.00 63.81           C  
ATOM   1856  N   ILE A 238     127.238 132.271 153.821  1.00 70.63           N  
ATOM   1857  CA  ILE A 238     126.775 132.418 155.200  1.00 67.43           C  
ATOM   1858  C   ILE A 238     125.568 131.533 155.479  1.00 66.52           C  
ATOM   1859  O   ILE A 238     125.430 131.013 156.586  1.00 66.93           O  
ATOM   1860  CB  ILE A 238     126.487 133.887 155.569  1.00 65.77           C  
ATOM   1861  CG1 ILE A 238     127.459 134.841 154.888  1.00 69.72           C  
ATOM   1862  CG2 ILE A 238     126.538 134.070 157.075  1.00 65.74           C  
ATOM   1863  CD1 ILE A 238     126.967 136.266 154.819  1.00 68.96           C  
ATOM   1864  N   VAL A 239     124.662 131.358 154.513  1.00 66.22           N  
ATOM   1865  CA  VAL A 239     123.506 130.511 154.804  1.00 65.94           C  
ATOM   1866  C   VAL A 239     123.942 129.056 154.894  1.00 68.64           C  
ATOM   1867  O   VAL A 239     123.458 128.304 155.748  1.00 71.76           O  
ATOM   1868  CB  VAL A 239     122.368 130.699 153.780  1.00 61.66           C  
ATOM   1869  CG1 VAL A 239     122.872 130.658 152.375  1.00 65.86           C  
ATOM   1870  CG2 VAL A 239     121.276 129.660 153.991  1.00 61.82           C  
ATOM   1871  N   PHE A 240     124.870 128.633 154.028  1.00 69.06           N  
ATOM   1872  CA  PHE A 240     125.425 127.291 154.169  1.00 68.71           C  
ATOM   1873  C   PHE A 240     125.976 127.088 155.574  1.00 68.68           C  
ATOM   1874  O   PHE A 240     125.654 126.100 156.249  1.00 64.23           O  
ATOM   1875  CB  PHE A 240     126.515 127.063 153.121  1.00 64.65           C  
ATOM   1876  CG  PHE A 240     127.127 125.690 153.165  1.00 66.18           C  
ATOM   1877  CD1 PHE A 240     128.204 125.419 153.994  1.00 67.78           C  
ATOM   1878  CD2 PHE A 240     126.631 124.673 152.370  1.00 61.04           C  
ATOM   1879  CE1 PHE A 240     128.766 124.159 154.033  1.00 64.06           C  
ATOM   1880  CE2 PHE A 240     127.191 123.413 152.405  1.00 62.20           C  
ATOM   1881  CZ  PHE A 240     128.259 123.156 153.237  1.00 64.08           C  
ATOM   1882  N   VAL A 241     126.781 128.044 156.046  1.00 66.43           N  
ATOM   1883  CA  VAL A 241     127.356 127.926 157.384  1.00 68.20           C  
ATOM   1884  C   VAL A 241     126.259 127.918 158.444  1.00 68.69           C  
ATOM   1885  O   VAL A 241     126.280 127.100 159.367  1.00 70.60           O  
ATOM   1886  CB  VAL A 241     128.380 129.047 157.629  1.00 69.07           C  
ATOM   1887  CG1 VAL A 241     128.929 128.955 159.037  1.00 68.74           C  
ATOM   1888  CG2 VAL A 241     129.509 128.952 156.624  1.00 69.33           C  
ATOM   1889  N   ILE A 242     125.268 128.800 158.310  1.00 63.92           N  
ATOM   1890  CA  ILE A 242     124.233 128.939 159.331  1.00 65.46           C  
ATOM   1891  C   ILE A 242     123.439 127.647 159.469  1.00 70.39           C  
ATOM   1892  O   ILE A 242     123.146 127.196 160.582  1.00 76.50           O  
ATOM   1893  CB  ILE A 242     123.316 130.132 159.007  1.00 64.52           C  
ATOM   1894  CG1 ILE A 242     123.973 131.443 159.437  1.00 64.14           C  
ATOM   1895  CG2 ILE A 242     121.958 129.971 159.674  1.00 62.54           C  
ATOM   1896  CD1 ILE A 242     123.188 132.672 159.041  1.00 64.59           C  
ATOM   1897  N   CYS A 243     123.067 127.035 158.344  1.00 69.95           N  
ATOM   1898  CA  CYS A 243     122.286 125.805 158.427  1.00 67.77           C  
ATOM   1899  C   CYS A 243     123.121 124.584 158.794  1.00 69.85           C  
ATOM   1900  O   CYS A 243     122.580 123.639 159.378  1.00 69.14           O  
ATOM   1901  CB  CYS A 243     121.529 125.535 157.125  1.00 60.94           C  
ATOM   1902  SG  CYS A 243     120.927 126.974 156.241  1.00 78.92           S  
ATOM   1903  N   PHE A 244     124.416 124.557 158.481  1.00 67.81           N  
ATOM   1904  CA  PHE A 244     125.141 123.310 158.702  1.00 65.16           C  
ATOM   1905  C   PHE A 244     126.026 123.307 159.945  1.00 61.75           C  
ATOM   1906  O   PHE A 244     126.172 122.259 160.576  1.00 60.03           O  
ATOM   1907  CB  PHE A 244     125.967 122.961 157.463  1.00 65.10           C  
ATOM   1908  CG  PHE A 244     125.127 122.527 156.297  1.00 60.78           C  
ATOM   1909  CD1 PHE A 244     124.430 121.334 156.345  1.00 57.76           C  
ATOM   1910  CD2 PHE A 244     125.011 123.319 155.169  1.00 62.19           C  
ATOM   1911  CE1 PHE A 244     123.644 120.934 155.286  1.00 65.41           C  
ATOM   1912  CE2 PHE A 244     124.226 122.922 154.106  1.00 62.85           C  
ATOM   1913  CZ  PHE A 244     123.542 121.730 154.166  1.00 67.46           C  
ATOM   1914  N   LEU A 245     126.608 124.441 160.329  1.00 58.66           N  
ATOM   1915  CA  LEU A 245     127.494 124.466 161.489  1.00 63.15           C  
ATOM   1916  C   LEU A 245     126.848 124.005 162.794  1.00 72.53           C  
ATOM   1917  O   LEU A 245     127.517 123.275 163.544  1.00 78.01           O  
ATOM   1918  CB  LEU A 245     128.079 125.875 161.653  1.00 62.65           C  
ATOM   1919  CG  LEU A 245     129.392 126.007 162.428  1.00 65.67           C  
ATOM   1920  CD1 LEU A 245     130.268 124.788 162.232  1.00 63.00           C  
ATOM   1921  CD2 LEU A 245     130.132 127.267 162.016  1.00 66.70           C  
ATOM   1922  N   PRO A 246     125.615 124.396 163.148  1.00 63.08           N  
ATOM   1923  CA  PRO A 246     125.103 124.023 164.483  1.00 58.47           C  
ATOM   1924  C   PRO A 246     125.015 122.524 164.728  1.00 63.46           C  
ATOM   1925  O   PRO A 246     125.515 122.035 165.752  1.00 62.21           O  
ATOM   1926  CB  PRO A 246     123.723 124.692 164.516  1.00 55.78           C  
ATOM   1927  CG  PRO A 246     123.837 125.821 163.582  1.00 54.81           C  
ATOM   1928  CD  PRO A 246     124.699 125.328 162.471  1.00 55.86           C  
ATOM   1929  N   SER A 247     124.380 121.774 163.826  1.00 57.45           N  
ATOM   1930  CA  SER A 247     124.250 120.338 164.047  1.00 50.76           C  
ATOM   1931  C   SER A 247     125.615 119.670 164.101  1.00 57.58           C  
ATOM   1932  O   SER A 247     125.843 118.764 164.911  1.00 65.54           O  
ATOM   1933  CB  SER A 247     123.391 119.708 162.955  1.00 54.42           C  
ATOM   1934  OG  SER A 247     123.514 118.298 162.981  1.00 59.41           O  
ATOM   1935  N   VAL A 248     126.544 120.117 163.256  1.00 50.01           N  
ATOM   1936  CA  VAL A 248     127.873 119.520 163.244  1.00 50.29           C  
ATOM   1937  C   VAL A 248     128.616 119.814 164.539  1.00 52.71           C  
ATOM   1938  O   VAL A 248     129.315 118.947 165.067  1.00 57.97           O  
ATOM   1939  CB  VAL A 248     128.660 119.992 162.013  1.00 48.69           C  
ATOM   1940  CG1 VAL A 248     130.000 119.291 161.954  1.00 56.98           C  
ATOM   1941  CG2 VAL A 248     127.867 119.690 160.769  1.00 49.69           C  
ATOM   1942  N   VAL A 249     128.498 121.034 165.070  1.00 51.95           N  
ATOM   1943  CA  VAL A 249     129.206 121.314 166.317  1.00 56.04           C  
ATOM   1944  C   VAL A 249     128.588 120.534 167.469  1.00 61.94           C  
ATOM   1945  O   VAL A 249     129.305 120.093 168.374  1.00 66.57           O  
ATOM   1946  CB  VAL A 249     129.279 122.824 166.624  1.00 52.49           C  
ATOM   1947  CG1 VAL A 249     129.979 123.562 165.504  1.00 48.18           C  
ATOM   1948  CG2 VAL A 249     127.915 123.413 166.895  1.00 56.81           C  
ATOM   1949  N   VAL A 250     127.266 120.330 167.462  1.00 53.17           N  
ATOM   1950  CA  VAL A 250     126.694 119.468 168.497  1.00 49.82           C  
ATOM   1951  C   VAL A 250     127.175 118.030 168.340  1.00 55.43           C  
ATOM   1952  O   VAL A 250     127.418 117.339 169.337  1.00 66.61           O  
ATOM   1953  CB  VAL A 250     125.159 119.539 168.515  1.00 48.59           C  
ATOM   1954  CG1 VAL A 250     124.639 118.955 169.812  1.00 49.13           C  
ATOM   1955  CG2 VAL A 250     124.706 120.969 168.417  1.00 63.03           C  
ATOM   1956  N   ARG A 251     127.321 117.551 167.103  1.00 62.86           N  
ATOM   1957  CA  ARG A 251     127.843 116.202 166.901  1.00 65.38           C  
ATOM   1958  C   ARG A 251     129.284 116.091 167.387  1.00 61.09           C  
ATOM   1959  O   ARG A 251     129.665 115.092 168.005  1.00 61.05           O  
ATOM   1960  CB  ARG A 251     127.737 115.813 165.427  1.00 65.68           C  
ATOM   1961  CG  ARG A 251     127.415 114.349 165.202  1.00 62.02           C  
ATOM   1962  CD  ARG A 251     126.166 113.952 165.966  1.00 59.95           C  
ATOM   1963  NE  ARG A 251     125.592 112.704 165.479  1.00 62.44           N  
ATOM   1964  CZ  ARG A 251     124.672 112.003 166.126  1.00 66.88           C  
ATOM   1965  NH1 ARG A 251     124.206 112.392 167.301  1.00 64.89           N  
ATOM   1966  NH2 ARG A 251     124.213 110.879 165.584  1.00 63.69           N  
ATOM   1967  N   ILE A 252     130.100 117.111 167.117  1.00 59.58           N  
ATOM   1968  CA  ILE A 252     131.477 117.117 167.602  1.00 58.10           C  
ATOM   1969  C   ILE A 252     131.505 117.120 169.123  1.00 55.59           C  
ATOM   1970  O   ILE A 252     132.306 116.413 169.745  1.00 61.24           O  
ATOM   1971  CB  ILE A 252     132.254 118.313 167.021  1.00 57.74           C  
ATOM   1972  CG1 ILE A 252     132.232 118.283 165.494  1.00 59.59           C  
ATOM   1973  CG2 ILE A 252     133.682 118.318 167.530  1.00 62.24           C  
ATOM   1974  CD1 ILE A 252     133.217 119.228 164.850  1.00 55.02           C  
ATOM   1975  N   ARG A 253     130.637 117.917 169.746  1.00 62.97           N  
ATOM   1976  CA  ARG A 253     130.590 117.962 171.203  1.00 70.32           C  
ATOM   1977  C   ARG A 253     130.192 116.610 171.782  1.00 73.87           C  
ATOM   1978  O   ARG A 253     130.788 116.138 172.759  1.00 78.87           O  
ATOM   1979  CB  ARG A 253     129.622 119.054 171.660  1.00 63.98           C  
ATOM   1980  CG  ARG A 253     129.576 119.251 173.164  1.00 68.21           C  
ATOM   1981  CD  ARG A 253     129.358 120.712 173.516  1.00 71.28           C  
ATOM   1982  NE  ARG A 253     130.064 121.095 174.732  1.00 75.28           N  
ATOM   1983  CZ  ARG A 253     130.681 122.257 174.904  1.00 76.58           C  
ATOM   1984  NH1 ARG A 253     130.702 123.176 173.954  1.00 74.09           N  
ATOM   1985  NH2 ARG A 253     131.292 122.502 176.060  1.00 73.94           N  
ATOM   1986  N   ILE A 254     129.180 115.968 171.195  1.00 73.19           N  
ATOM   1987  CA  ILE A 254     128.751 114.686 171.741  1.00 73.39           C  
ATOM   1988  C   ILE A 254     129.814 113.620 171.502  1.00 80.83           C  
ATOM   1989  O   ILE A 254     130.009 112.739 172.344  1.00 82.80           O  
ATOM   1990  CB  ILE A 254     127.373 114.276 171.190  1.00 69.24           C  
ATOM   1991  CG1 ILE A 254     126.806 113.134 172.028  1.00 75.04           C  
ATOM   1992  CG2 ILE A 254     127.454 113.854 169.743  1.00 68.71           C  
ATOM   1993  CD1 ILE A 254     126.990 113.327 173.511  1.00 76.70           C  
ATOM   1994  N   PHE A 255     130.544 113.698 170.385  1.00 83.07           N  
ATOM   1995  CA  PHE A 255     131.699 112.825 170.192  1.00 77.16           C  
ATOM   1996  C   PHE A 255     132.743 113.059 171.274  1.00 73.69           C  
ATOM   1997  O   PHE A 255     133.336 112.109 171.797  1.00 69.45           O  
ATOM   1998  CB  PHE A 255     132.313 113.067 168.814  1.00 75.60           C  
ATOM   1999  CG  PHE A 255     131.783 112.165 167.744  1.00 76.79           C  
ATOM   2000  CD1 PHE A 255     131.860 110.791 167.875  1.00 80.85           C  
ATOM   2001  CD2 PHE A 255     131.213 112.693 166.599  1.00 75.99           C  
ATOM   2002  CE1 PHE A 255     131.373 109.960 166.885  1.00 81.86           C  
ATOM   2003  CE2 PHE A 255     130.725 111.869 165.608  1.00 78.78           C  
ATOM   2004  CZ  PHE A 255     130.806 110.501 165.751  1.00 79.87           C  
ATOM   2005  N   TRP A 256     132.982 114.326 171.613  1.00 88.34           N  
ATOM   2006  CA  TRP A 256     133.982 114.672 172.615  1.00 88.79           C  
ATOM   2007  C   TRP A 256     133.623 114.062 173.965  1.00 92.47           C  
ATOM   2008  O   TRP A 256     134.439 113.367 174.581  1.00 97.45           O  
ATOM   2009  CB  TRP A 256     134.095 116.202 172.681  1.00 86.97           C  
ATOM   2010  CG  TRP A 256     134.798 116.855 173.863  1.00 95.02           C  
ATOM   2011  CD1 TRP A 256     135.189 116.279 175.041  1.00 94.52           C  
ATOM   2012  CD2 TRP A 256     135.178 118.234 173.954  1.00 96.38           C  
ATOM   2013  NE1 TRP A 256     135.788 117.210 175.851  1.00 91.30           N  
ATOM   2014  CE2 TRP A 256     135.794 118.419 175.207  1.00 96.04           C  
ATOM   2015  CE3 TRP A 256     135.057 119.329 173.093  1.00 90.82           C  
ATOM   2016  CZ2 TRP A 256     136.287 119.654 175.619  1.00 92.98           C  
ATOM   2017  CZ3 TRP A 256     135.547 120.553 173.504  1.00 90.86           C  
ATOM   2018  CH2 TRP A 256     136.154 120.706 174.756  1.00 92.51           C  
ATOM   2019  N   LEU A 257     132.397 114.300 174.436  1.00 92.24           N  
ATOM   2020  CA  LEU A 257     132.007 113.736 175.729  1.00 95.51           C  
ATOM   2021  C   LEU A 257     131.817 112.222 175.677  1.00 95.44           C  
ATOM   2022  O   LEU A 257     131.933 111.559 176.714  1.00 95.13           O  
ATOM   2023  CB  LEU A 257     130.755 114.416 176.297  1.00 94.64           C  
ATOM   2024  CG  LEU A 257     130.746 115.898 176.711  1.00 94.82           C  
ATOM   2025  CD1 LEU A 257     131.823 116.138 177.764  1.00 92.79           C  
ATOM   2026  CD2 LEU A 257     130.893 116.897 175.590  1.00 93.40           C  
ATOM   2027  N   LEU A 258     131.531 111.648 174.507  1.00 93.10           N  
ATOM   2028  CA  LEU A 258     131.487 110.194 174.410  1.00 95.71           C  
ATOM   2029  C   LEU A 258     132.880 109.593 174.550  1.00 95.16           C  
ATOM   2030  O   LEU A 258     133.060 108.573 175.226  1.00 91.84           O  
ATOM   2031  CB  LEU A 258     130.851 109.776 173.085  1.00 96.33           C  
ATOM   2032  CG  LEU A 258     130.322 108.344 172.991  1.00 95.84           C  
ATOM   2033  CD1 LEU A 258     129.557 107.960 174.247  1.00 94.17           C  
ATOM   2034  CD2 LEU A 258     129.450 108.188 171.758  1.00 96.19           C  
ATOM   2035  N   HIS A 259     133.875 110.213 173.915  1.00101.15           N  
ATOM   2036  CA  HIS A 259     135.245 109.723 174.014  1.00 99.07           C  
ATOM   2037  C   HIS A 259     135.789 109.909 175.425  1.00 97.49           C  
ATOM   2038  O   HIS A 259     136.376 108.987 176.003  1.00 98.90           O  
ATOM   2039  CB  HIS A 259     136.125 110.447 172.993  1.00101.28           C  
ATOM   2040  CG  HIS A 259     137.473 109.824 172.798  1.00101.78           C  
ATOM   2041  ND1 HIS A 259     138.298 110.157 171.745  1.00101.42           N  
ATOM   2042  CD2 HIS A 259     138.137 108.885 173.512  1.00101.65           C  
ATOM   2043  CE1 HIS A 259     139.414 109.454 171.822  1.00100.75           C  
ATOM   2044  NE2 HIS A 259     139.341 108.674 172.886  1.00102.18           N  
ATOM   2045  N   THR A 260     135.596 111.097 175.998  1.00 98.92           N  
ATOM   2046  CA  THR A 260     136.169 111.387 177.308  1.00101.85           C  
ATOM   2047  C   THR A 260     135.453 110.619 178.412  1.00103.54           C  
ATOM   2048  O   THR A 260     136.096 110.006 179.273  1.00101.67           O  
ATOM   2049  CB  THR A 260     136.116 112.890 177.581  1.00101.29           C  
ATOM   2050  OG1 THR A 260     134.760 113.344 177.496  1.00 99.55           O  
ATOM   2051  CG2 THR A 260     136.964 113.644 176.568  1.00100.38           C  
ATOM   2052  N   SER A 261     134.121 110.633 178.403  1.00101.84           N  
ATOM   2053  CA  SER A 261     133.336 110.074 179.499  1.00101.36           C  
ATOM   2054  C   SER A 261     132.826 108.670 179.189  1.00101.78           C  
ATOM   2055  O   SER A 261     133.114 107.724 179.928  1.00 99.95           O  
ATOM   2056  CB  SER A 261     132.164 111.008 179.829  1.00 99.03           C  
ATOM   2057  OG  SER A 261     132.589 112.358 179.878  1.00 95.71           O  
ATOM   2058  N   GLY A 262     132.076 108.516 178.108  1.00113.41           N  
ATOM   2059  CA  GLY A 262     131.469 107.249 177.760  1.00113.46           C  
ATOM   2060  C   GLY A 262     129.977 107.246 178.045  1.00114.34           C  
ATOM   2061  O   GLY A 262     129.357 108.278 178.317  1.00114.06           O  
ATOM   2062  N   THR A 263     129.399 106.045 177.980  1.00119.76           N  
ATOM   2063  CA  THR A 263     127.968 105.851 178.179  1.00120.27           C  
ATOM   2064  C   THR A 263     127.647 105.232 179.535  1.00120.48           C  
ATOM   2065  O   THR A 263     126.593 104.606 179.691  1.00116.75           O  
ATOM   2066  CB  THR A 263     127.388 104.989 177.058  1.00119.24           C  
ATOM   2067  OG1 THR A 263     126.060 104.580 177.408  1.00118.63           O  
ATOM   2068  CG2 THR A 263     128.249 103.756 176.840  1.00119.48           C  
ATOM   2069  N   GLN A 264     128.538 105.387 180.518  1.00130.38           N  
ATOM   2070  CA  GLN A 264     128.271 104.845 181.847  1.00129.64           C  
ATOM   2071  C   GLN A 264     127.041 105.493 182.469  1.00129.90           C  
ATOM   2072  O   GLN A 264     126.200 104.807 183.063  1.00129.00           O  
ATOM   2073  CB  GLN A 264     129.494 105.037 182.747  1.00128.56           C  
ATOM   2074  CG  GLN A 264     130.530 103.919 182.666  1.00129.20           C  
ATOM   2075  CD  GLN A 264     131.182 103.790 181.297  1.00129.50           C  
ATOM   2076  OE1 GLN A 264     131.010 104.642 180.424  1.00128.53           O  
ATOM   2077  NE2 GLN A 264     131.938 102.716 181.106  1.00129.69           N  
ATOM   2078  N   ASN A 265     126.917 106.811 182.341  1.00119.45           N  
ATOM   2079  CA  ASN A 265     125.740 107.545 182.782  1.00117.58           C  
ATOM   2080  C   ASN A 265     125.111 108.205 181.565  1.00117.58           C  
ATOM   2081  O   ASN A 265     125.789 108.928 180.828  1.00116.90           O  
ATOM   2082  CB  ASN A 265     126.104 108.583 183.854  1.00115.69           C  
ATOM   2083  CG  ASN A 265     125.123 109.747 183.921  1.00115.15           C  
ATOM   2084  OD1 ASN A 265     125.082 110.604 183.036  1.00113.72           O  
ATOM   2085  ND2 ASN A 265     124.324 109.779 184.980  1.00115.71           N  
ATOM   2086  N   CYS A 266     123.822 107.956 181.356  1.00110.31           N  
ATOM   2087  CA  CYS A 266     123.118 108.465 180.189  1.00108.98           C  
ATOM   2088  C   CYS A 266     122.453 109.814 180.430  1.00110.52           C  
ATOM   2089  O   CYS A 266     121.882 110.379 179.493  1.00110.10           O  
ATOM   2090  CB  CYS A 266     122.065 107.452 179.727  1.00106.71           C  
ATOM   2091  N   GLU A 267     122.517 110.348 181.647  1.00112.54           N  
ATOM   2092  CA  GLU A 267     121.840 111.600 181.961  1.00110.45           C  
ATOM   2093  C   GLU A 267     122.667 112.833 181.623  1.00109.99           C  
ATOM   2094  O   GLU A 267     122.187 113.953 181.830  1.00109.69           O  
ATOM   2095  CB  GLU A 267     121.448 111.626 183.440  1.00110.67           C  
ATOM   2096  CG  GLU A 267     120.503 110.504 183.837  1.00111.55           C  
ATOM   2097  CD  GLU A 267     119.454 110.227 182.776  1.00112.14           C  
ATOM   2098  OE1 GLU A 267     118.534 111.056 182.616  1.00111.87           O  
ATOM   2099  OE2 GLU A 267     119.550 109.181 182.100  1.00110.68           O  
ATOM   2100  N   VAL A 268     123.881 112.662 181.105  1.00101.73           N  
ATOM   2101  CA  VAL A 268     124.733 113.792 180.750  1.00 99.03           C  
ATOM   2102  C   VAL A 268     124.546 114.108 179.273  1.00 96.84           C  
ATOM   2103  O   VAL A 268     125.379 114.785 178.661  1.00 93.87           O  
ATOM   2104  CB  VAL A 268     126.212 113.505 181.071  1.00 98.06           C  
ATOM   2105  CG1 VAL A 268     126.457 113.590 182.568  1.00 97.83           C  
ATOM   2106  CG2 VAL A 268     126.614 112.143 180.538  1.00 98.90           C  
ATOM   2107  N   TYR A 269     123.451 113.615 178.692  1.00 91.96           N  
ATOM   2108  CA  TYR A 269     123.199 113.767 177.267  1.00 93.90           C  
ATOM   2109  C   TYR A 269     121.985 114.621 176.933  1.00 93.27           C  
ATOM   2110  O   TYR A 269     121.936 115.176 175.830  1.00 90.58           O  
ATOM   2111  CB  TYR A 269     123.017 112.390 176.609  1.00 94.27           C  
ATOM   2112  CG  TYR A 269     124.234 111.496 176.680  1.00 93.25           C  
ATOM   2113  CD1 TYR A 269     124.534 110.785 177.832  1.00 91.57           C  
ATOM   2114  CD2 TYR A 269     125.077 111.357 175.589  1.00 93.65           C  
ATOM   2115  CE1 TYR A 269     125.643 109.967 177.896  1.00 92.81           C  
ATOM   2116  CE2 TYR A 269     126.189 110.542 175.644  1.00 92.15           C  
ATOM   2117  CZ  TYR A 269     126.468 109.850 176.800  1.00 94.45           C  
ATOM   2118  OH  TYR A 269     127.576 109.035 176.860  1.00 99.71           O  
ATOM   2119  N   ARG A 270     121.024 114.750 177.854  1.00 90.14           N  
ATOM   2120  CA  ARG A 270     119.724 115.343 177.549  1.00 87.50           C  
ATOM   2121  C   ARG A 270     119.842 116.599 176.697  1.00 86.02           C  
ATOM   2122  O   ARG A 270     119.396 116.628 175.543  1.00 91.98           O  
ATOM   2123  CB  ARG A 270     118.982 115.657 178.852  1.00 85.50           C  
ATOM   2124  CG  ARG A 270     118.253 114.476 179.456  1.00 89.08           C  
ATOM   2125  CD  ARG A 270     117.398 114.911 180.634  1.00 89.40           C  
ATOM   2126  NE  ARG A 270     115.996 115.057 180.263  1.00 93.31           N  
ATOM   2127  CZ  ARG A 270     115.020 114.271 180.697  1.00 91.86           C  
ATOM   2128  NH1 ARG A 270     115.257 113.268 181.526  1.00 86.21           N  
ATOM   2129  NH2 ARG A 270     113.775 114.497 180.288  1.00 90.74           N  
ATOM   2130  N   SER A 271     120.491 117.630 177.240  1.00 74.32           N  
ATOM   2131  CA  SER A 271     120.625 118.885 176.510  1.00 72.66           C  
ATOM   2132  C   SER A 271     121.267 118.656 175.150  1.00 69.28           C  
ATOM   2133  O   SER A 271     120.690 119.006 174.112  1.00 70.33           O  
ATOM   2134  CB  SER A 271     121.444 119.881 177.331  1.00 74.72           C  
ATOM   2135  OG  SER A 271     121.056 119.862 178.693  1.00 73.77           O  
ATOM   2136  N   VAL A 272     122.428 117.998 175.131  1.00 69.97           N  
ATOM   2137  CA  VAL A 272     123.162 117.828 173.889  1.00 71.95           C  
ATOM   2138  C   VAL A 272     122.386 116.996 172.887  1.00 72.13           C  
ATOM   2139  O   VAL A 272     122.734 116.979 171.703  1.00 75.89           O  
ATOM   2140  CB  VAL A 272     124.553 117.206 174.148  1.00 82.61           C  
ATOM   2141  CG1 VAL A 272     125.208 117.843 175.367  1.00 82.51           C  
ATOM   2142  CG2 VAL A 272     124.462 115.702 174.291  1.00 76.96           C  
ATOM   2143  N   ASP A 273     121.334 116.309 173.331  1.00 75.00           N  
ATOM   2144  CA  ASP A 273     120.453 115.626 172.395  1.00 76.75           C  
ATOM   2145  C   ASP A 273     119.431 116.617 171.845  1.00 72.96           C  
ATOM   2146  O   ASP A 273     119.335 116.815 170.628  1.00 68.32           O  
ATOM   2147  CB  ASP A 273     119.788 114.434 173.103  1.00 74.40           C  
ATOM   2148  CG  ASP A 273     118.489 113.953 172.443  1.00 74.53           C  
ATOM   2149  OD1 ASP A 273     117.867 113.042 173.027  1.00 79.14           O  
ATOM   2150  OD2 ASP A 273     118.113 114.385 171.335  1.00 72.44           O  
ATOM   2151  N   LEU A 274     118.698 117.285 172.741  1.00 72.75           N  
ATOM   2152  CA  LEU A 274     117.506 118.028 172.340  1.00 69.54           C  
ATOM   2153  C   LEU A 274     117.837 119.062 171.274  1.00 70.43           C  
ATOM   2154  O   LEU A 274     117.405 118.949 170.119  1.00 73.02           O  
ATOM   2155  CB  LEU A 274     116.876 118.700 173.561  1.00 69.85           C  
ATOM   2156  CG  LEU A 274     115.350 118.790 173.585  1.00 75.43           C  
ATOM   2157  CD1 LEU A 274     114.736 117.405 173.476  1.00 72.79           C  
ATOM   2158  CD2 LEU A 274     114.866 119.499 174.840  1.00 76.12           C  
ATOM   2159  N   ALA A 275     118.656 120.052 171.635  1.00 70.30           N  
ATOM   2160  CA  ALA A 275     119.022 121.097 170.690  1.00 71.85           C  
ATOM   2161  C   ALA A 275     119.599 120.511 169.414  1.00 68.22           C  
ATOM   2162  O   ALA A 275     119.405 121.077 168.332  1.00 70.97           O  
ATOM   2163  CB  ALA A 275     120.022 122.062 171.328  1.00 69.75           C  
ATOM   2164  N   PHE A 276     120.283 119.366 169.517  1.00 55.71           N  
ATOM   2165  CA  PHE A 276     120.817 118.705 168.333  1.00 52.43           C  
ATOM   2166  C   PHE A 276     119.752 118.601 167.253  1.00 54.57           C  
ATOM   2167  O   PHE A 276     119.920 119.118 166.142  1.00 61.43           O  
ATOM   2168  CB  PHE A 276     121.350 117.318 168.696  1.00 52.19           C  
ATOM   2169  CG  PHE A 276     121.799 116.511 167.508  1.00 53.17           C  
ATOM   2170  CD1 PHE A 276     122.444 117.114 166.441  1.00 54.83           C  
ATOM   2171  CD2 PHE A 276     121.569 115.150 167.456  1.00 54.92           C  
ATOM   2172  CE1 PHE A 276     122.851 116.373 165.350  1.00 48.87           C  
ATOM   2173  CE2 PHE A 276     121.976 114.407 166.367  1.00 54.75           C  
ATOM   2174  CZ  PHE A 276     122.618 115.020 165.315  1.00 52.73           C  
ATOM   2175  N   PHE A 277     118.620 117.979 167.584  1.00 56.28           N  
ATOM   2176  CA  PHE A 277     117.584 117.793 166.576  1.00 60.47           C  
ATOM   2177  C   PHE A 277     117.045 119.133 166.100  1.00 62.31           C  
ATOM   2178  O   PHE A 277     116.735 119.298 164.914  1.00 61.24           O  
ATOM   2179  CB  PHE A 277     116.473 116.902 167.123  1.00 54.27           C  
ATOM   2180  CG  PHE A 277     116.902 115.481 167.333  1.00 55.05           C  
ATOM   2181  CD1 PHE A 277     117.786 114.880 166.455  1.00 56.21           C  
ATOM   2182  CD2 PHE A 277     116.436 114.750 168.409  1.00 59.67           C  
ATOM   2183  CE1 PHE A 277     118.191 113.576 166.641  1.00 59.19           C  
ATOM   2184  CE2 PHE A 277     116.838 113.443 168.600  1.00 57.99           C  
ATOM   2185  CZ  PHE A 277     117.717 112.857 167.714  1.00 58.84           C  
ATOM   2186  N   ILE A 278     116.963 120.115 167.001  1.00 63.18           N  
ATOM   2187  CA  ILE A 278     116.578 121.460 166.585  1.00 62.20           C  
ATOM   2188  C   ILE A 278     117.588 122.001 165.585  1.00 60.00           C  
ATOM   2189  O   ILE A 278     117.222 122.511 164.518  1.00 60.17           O  
ATOM   2190  CB  ILE A 278     116.435 122.384 167.806  1.00 51.09           C  
ATOM   2191  CG1 ILE A 278     115.193 122.009 168.613  1.00 52.55           C  
ATOM   2192  CG2 ILE A 278     116.359 123.830 167.364  1.00 47.16           C  
ATOM   2193  CD1 ILE A 278     114.990 122.855 169.844  1.00 56.54           C  
ATOM   2194  N   THR A 279     118.880 121.859 165.896  1.00 59.68           N  
ATOM   2195  CA  THR A 279     119.905 122.226 164.927  1.00 53.34           C  
ATOM   2196  C   THR A 279     119.770 121.397 163.661  1.00 46.92           C  
ATOM   2197  O   THR A 279     120.067 121.883 162.563  1.00 54.45           O  
ATOM   2198  CB  THR A 279     121.300 122.050 165.525  1.00 60.21           C  
ATOM   2199  OG1 THR A 279     121.518 120.670 165.831  1.00 53.34           O  
ATOM   2200  CG2 THR A 279     121.451 122.875 166.790  1.00 60.12           C  
ATOM   2201  N   LEU A 280     119.295 120.157 163.792  1.00 48.93           N  
ATOM   2202  CA  LEU A 280     119.090 119.315 162.623  1.00 53.41           C  
ATOM   2203  C   LEU A 280     118.042 119.886 161.682  1.00 61.29           C  
ATOM   2204  O   LEU A 280     118.050 119.552 160.494  1.00 64.71           O  
ATOM   2205  CB  LEU A 280     118.692 117.904 163.052  1.00 47.71           C  
ATOM   2206  CG  LEU A 280     118.878 116.825 161.989  1.00 46.90           C  
ATOM   2207  CD1 LEU A 280     120.207 117.004 161.281  1.00 46.71           C  
ATOM   2208  CD2 LEU A 280     118.788 115.454 162.624  1.00 57.94           C  
ATOM   2209  N   SER A 281     117.136 120.731 162.176  1.00 56.16           N  
ATOM   2210  CA  SER A 281     116.181 121.364 161.277  1.00 46.16           C  
ATOM   2211  C   SER A 281     116.791 122.517 160.500  1.00 41.59           C  
ATOM   2212  O   SER A 281     116.254 122.892 159.451  1.00 46.77           O  
ATOM   2213  CB  SER A 281     114.964 121.855 162.054  1.00 41.28           C  
ATOM   2214  OG  SER A 281     114.203 120.755 162.503  1.00 51.74           O  
ATOM   2215  N   PHE A 282     117.912 123.064 160.973  1.00 61.08           N  
ATOM   2216  CA  PHE A 282     118.491 124.231 160.321  1.00 68.32           C  
ATOM   2217  C   PHE A 282     118.844 123.932 158.871  1.00 62.49           C  
ATOM   2218  O   PHE A 282     118.632 124.772 157.990  1.00 61.55           O  
ATOM   2219  CB  PHE A 282     119.722 124.706 161.093  1.00 64.38           C  
ATOM   2220  CG  PHE A 282     119.396 125.593 162.259  1.00 61.89           C  
ATOM   2221  CD1 PHE A 282     118.655 125.113 163.323  1.00 66.07           C  
ATOM   2222  CD2 PHE A 282     119.822 126.909 162.285  1.00 61.43           C  
ATOM   2223  CE1 PHE A 282     118.350 125.925 164.395  1.00 65.23           C  
ATOM   2224  CE2 PHE A 282     119.520 127.726 163.354  1.00 63.20           C  
ATOM   2225  CZ  PHE A 282     118.783 127.233 164.411  1.00 65.30           C  
ATOM   2226  N   THR A 283     119.364 122.733 158.602  1.00 59.83           N  
ATOM   2227  CA  THR A 283     119.717 122.385 157.231  1.00 68.65           C  
ATOM   2228  C   THR A 283     118.492 122.356 156.326  1.00 72.14           C  
ATOM   2229  O   THR A 283     118.595 122.678 155.136  1.00 75.71           O  
ATOM   2230  CB  THR A 283     120.452 121.044 157.192  1.00 64.55           C  
ATOM   2231  OG1 THR A 283     120.641 120.643 155.830  1.00 65.47           O  
ATOM   2232  CG2 THR A 283     119.674 119.978 157.925  1.00 59.24           C  
ATOM   2233  N   TYR A 284     117.322 122.004 156.867  1.00 58.99           N  
ATOM   2234  CA  TYR A 284     116.112 122.047 156.052  1.00 50.71           C  
ATOM   2235  C   TYR A 284     115.792 123.471 155.625  1.00 57.00           C  
ATOM   2236  O   TYR A 284     115.189 123.681 154.566  1.00 58.99           O  
ATOM   2237  CB  TYR A 284     114.934 121.437 156.810  1.00 50.03           C  
ATOM   2238  CG  TYR A 284     115.185 120.028 157.287  1.00 48.15           C  
ATOM   2239  CD1 TYR A 284     116.048 119.188 156.604  1.00 43.98           C  
ATOM   2240  CD2 TYR A 284     114.562 119.541 158.425  1.00 47.94           C  
ATOM   2241  CE1 TYR A 284     116.284 117.907 157.039  1.00 47.66           C  
ATOM   2242  CE2 TYR A 284     114.792 118.260 158.868  1.00 40.06           C  
ATOM   2243  CZ  TYR A 284     115.654 117.449 158.170  1.00 47.22           C  
ATOM   2244  OH  TYR A 284     115.886 116.169 158.608  1.00 57.77           O  
ATOM   2245  N   MET A 285     116.203 124.459 156.428  1.00 72.98           N  
ATOM   2246  CA  MET A 285     116.070 125.854 156.024  1.00 70.06           C  
ATOM   2247  C   MET A 285     116.713 126.087 154.668  1.00 68.15           C  
ATOM   2248  O   MET A 285     116.192 126.853 153.849  1.00 74.47           O  
ATOM   2249  CB  MET A 285     116.700 126.773 157.073  1.00 67.55           C  
ATOM   2250  CG  MET A 285     115.846 126.990 158.305  1.00 70.09           C  
ATOM   2251  SD  MET A 285     116.324 128.445 159.254  1.00 82.84           S  
ATOM   2252  CE  MET A 285     115.785 127.969 160.894  1.00 70.35           C  
ATOM   2253  N   ASN A 286     117.835 125.413 154.404  1.00 58.05           N  
ATOM   2254  CA  ASN A 286     118.487 125.551 153.110  1.00 57.00           C  
ATOM   2255  C   ASN A 286     117.512 125.252 151.982  1.00 60.10           C  
ATOM   2256  O   ASN A 286     117.431 126.006 151.005  1.00 66.84           O  
ATOM   2257  CB  ASN A 286     119.700 124.626 153.035  1.00 64.27           C  
ATOM   2258  CG  ASN A 286     120.644 124.995 151.911  1.00 70.05           C  
ATOM   2259  OD1 ASN A 286     120.713 126.152 151.499  1.00 69.85           O  
ATOM   2260  ND2 ASN A 286     121.379 124.011 151.409  1.00 68.90           N  
ATOM   2261  N   SER A 287     116.719 124.188 152.130  1.00 64.29           N  
ATOM   2262  CA  SER A 287     115.754 123.837 151.095  1.00 66.77           C  
ATOM   2263  C   SER A 287     114.767 124.970 150.854  1.00 69.11           C  
ATOM   2264  O   SER A 287     114.390 125.240 149.708  1.00 74.66           O  
ATOM   2265  CB  SER A 287     115.013 122.558 151.478  1.00 66.20           C  
ATOM   2266  OG  SER A 287     114.099 122.801 152.532  1.00 66.55           O  
ATOM   2267  N   MET A 288     114.340 125.650 151.916  1.00 72.95           N  
ATOM   2268  CA  MET A 288     113.422 126.770 151.771  1.00 68.32           C  
ATOM   2269  C   MET A 288     114.141 128.100 151.592  1.00 77.11           C  
ATOM   2270  O   MET A 288     113.477 129.119 151.380  1.00 81.57           O  
ATOM   2271  CB  MET A 288     112.468 126.833 152.972  1.00 67.33           C  
ATOM   2272  CG  MET A 288     113.089 127.274 154.291  1.00 71.93           C  
ATOM   2273  SD  MET A 288     113.166 129.059 154.539  1.00 83.24           S  
ATOM   2274  CE  MET A 288     111.566 129.364 155.281  1.00 77.08           C  
ATOM   2275  N   LEU A 289     115.475 128.119 151.661  1.00 80.22           N  
ATOM   2276  CA  LEU A 289     116.231 129.342 151.431  1.00 74.22           C  
ATOM   2277  C   LEU A 289     117.010 129.332 150.128  1.00 75.69           C  
ATOM   2278  O   LEU A 289     117.470 130.391 149.695  1.00 73.74           O  
ATOM   2279  CB  LEU A 289     117.209 129.603 152.586  1.00 69.48           C  
ATOM   2280  CG  LEU A 289     116.598 130.072 153.906  1.00 73.47           C  
ATOM   2281  CD1 LEU A 289     117.611 129.956 155.035  1.00 73.00           C  
ATOM   2282  CD2 LEU A 289     116.077 131.494 153.782  1.00 73.20           C  
ATOM   2283  N   ASP A 290     117.184 128.167 149.512  1.00 79.20           N  
ATOM   2284  CA  ASP A 290     117.830 128.103 148.206  1.00 75.06           C  
ATOM   2285  C   ASP A 290     117.084 128.860 147.111  1.00 72.82           C  
ATOM   2286  O   ASP A 290     117.755 129.527 146.304  1.00 72.57           O  
ATOM   2287  CB  ASP A 290     118.032 126.635 147.815  1.00 73.41           C  
ATOM   2288  CG  ASP A 290     119.329 126.071 148.349  1.00 78.54           C  
ATOM   2289  OD1 ASP A 290     120.175 126.862 148.815  1.00 78.65           O  
ATOM   2290  OD2 ASP A 290     119.498 124.836 148.322  1.00 76.48           O  
ATOM   2291  N   PRO A 291     115.749 128.790 146.995  1.00 73.93           N  
ATOM   2292  CA  PRO A 291     115.089 129.486 145.875  1.00 82.10           C  
ATOM   2293  C   PRO A 291     115.353 130.981 145.821  1.00 84.58           C  
ATOM   2294  O   PRO A 291     115.512 131.535 144.727  1.00 83.17           O  
ATOM   2295  CB  PRO A 291     113.603 129.186 146.111  1.00 79.35           C  
ATOM   2296  CG  PRO A 291     113.594 127.929 146.881  1.00 75.97           C  
ATOM   2297  CD  PRO A 291     114.776 128.015 147.786  1.00 69.43           C  
ATOM   2298  N   VAL A 292     115.405 131.655 146.972  1.00 79.09           N  
ATOM   2299  CA  VAL A 292     115.547 133.107 146.963  1.00 75.70           C  
ATOM   2300  C   VAL A 292     116.943 133.524 146.519  1.00 78.51           C  
ATOM   2301  O   VAL A 292     117.115 134.592 145.921  1.00 84.40           O  
ATOM   2302  CB  VAL A 292     115.191 133.691 148.343  1.00 79.06           C  
ATOM   2303  CG1 VAL A 292     113.786 133.274 148.746  1.00 77.12           C  
ATOM   2304  CG2 VAL A 292     116.198 133.261 149.391  1.00 80.60           C  
ATOM   2305  N   VAL A 293     117.958 132.705 146.791  1.00 68.91           N  
ATOM   2306  CA  VAL A 293     119.341 133.092 146.533  1.00 71.94           C  
ATOM   2307  C   VAL A 293     119.808 132.557 145.184  1.00 71.40           C  
ATOM   2308  O   VAL A 293     120.573 133.219 144.473  1.00 69.34           O  
ATOM   2309  CB  VAL A 293     120.263 132.615 147.673  1.00 70.10           C  
ATOM   2310  CG1 VAL A 293     119.990 131.167 148.010  1.00 71.99           C  
ATOM   2311  CG2 VAL A 293     121.726 132.809 147.307  1.00 68.57           C  
ATOM   2312  N   TYR A 294     119.343 131.367 144.809  1.00 65.73           N  
ATOM   2313  CA  TYR A 294     119.884 130.710 143.626  1.00 64.96           C  
ATOM   2314  C   TYR A 294     119.106 131.036 142.355  1.00 68.53           C  
ATOM   2315  O   TYR A 294     119.704 131.441 141.353  1.00 71.95           O  
ATOM   2316  CB  TYR A 294     119.931 129.197 143.845  1.00 66.32           C  
ATOM   2317  CG  TYR A 294     121.215 128.737 144.489  1.00 62.76           C  
ATOM   2318  CD1 TYR A 294     122.434 128.932 143.859  1.00 61.46           C  
ATOM   2319  CD2 TYR A 294     121.210 128.124 145.731  1.00 61.28           C  
ATOM   2320  CE1 TYR A 294     123.611 128.521 144.443  1.00 61.62           C  
ATOM   2321  CE2 TYR A 294     122.383 127.711 146.324  1.00 60.50           C  
ATOM   2322  CZ  TYR A 294     123.580 127.912 145.675  1.00 61.21           C  
ATOM   2323  OH  TYR A 294     124.752 127.499 146.263  1.00 62.80           O  
ATOM   2324  N   TYR A 295     117.784 130.871 142.369  1.00 66.04           N  
ATOM   2325  CA  TYR A 295     116.987 131.058 141.160  1.00 66.65           C  
ATOM   2326  C   TYR A 295     116.382 132.454 141.068  1.00 71.10           C  
ATOM   2327  O   TYR A 295     116.599 133.160 140.080  1.00 71.85           O  
ATOM   2328  CB  TYR A 295     115.880 129.999 141.071  1.00 72.42           C  
ATOM   2329  CG  TYR A 295     116.251 128.652 141.639  1.00 72.28           C  
ATOM   2330  CD1 TYR A 295     117.190 127.849 141.011  1.00 66.94           C  
ATOM   2331  CD2 TYR A 295     115.630 128.164 142.776  1.00 71.08           C  
ATOM   2332  CE1 TYR A 295     117.525 126.616 141.520  1.00 63.93           C  
ATOM   2333  CE2 TYR A 295     115.956 126.930 143.289  1.00 74.01           C  
ATOM   2334  CZ  TYR A 295     116.903 126.159 142.658  1.00 71.85           C  
ATOM   2335  OH  TYR A 295     117.229 124.928 143.169  1.00 73.45           O  
ATOM   2336  N   PHE A 296     115.629 132.870 142.088  1.00 84.00           N  
ATOM   2337  CA  PHE A 296     114.886 134.121 141.997  1.00 84.91           C  
ATOM   2338  C   PHE A 296     115.795 135.337 141.910  1.00 81.93           C  
ATOM   2339  O   PHE A 296     115.322 136.424 141.566  1.00 85.67           O  
ATOM   2340  CB  PHE A 296     113.947 134.265 143.194  1.00 84.62           C  
ATOM   2341  CG  PHE A 296     112.854 133.238 143.234  1.00 85.08           C  
ATOM   2342  CD1 PHE A 296     112.392 132.652 142.069  1.00 81.79           C  
ATOM   2343  CD2 PHE A 296     112.284 132.865 144.438  1.00 83.58           C  
ATOM   2344  CE1 PHE A 296     111.387 131.708 142.106  1.00 81.23           C  
ATOM   2345  CE2 PHE A 296     111.277 131.924 144.480  1.00 83.75           C  
ATOM   2346  CZ  PHE A 296     110.828 131.345 143.312  1.00 81.58           C  
ATOM   2347  N   SER A 297     117.078 135.182 142.211  1.00 71.68           N  
ATOM   2348  CA  SER A 297     118.032 136.274 142.118  1.00 74.51           C  
ATOM   2349  C   SER A 297     118.692 136.260 140.741  1.00 80.20           C  
ATOM   2350  O   SER A 297     118.247 135.567 139.822  1.00 84.33           O  
ATOM   2351  CB  SER A 297     119.049 136.171 143.248  1.00 76.28           C  
ATOM   2352  OG  SER A 297     118.493 136.659 144.453  1.00 76.53           O  
ATOM   2353  N   SER A 298     119.769 137.032 140.590  1.00 85.72           N  
ATOM   2354  CA  SER A 298     120.527 137.144 139.348  1.00 89.56           C  
ATOM   2355  C   SER A 298     119.618 137.515 138.182  1.00 88.17           C  
ATOM   2356  O   SER A 298     119.337 136.673 137.320  1.00 88.52           O  
ATOM   2357  CB  SER A 298     121.268 135.839 139.046  1.00 90.90           C  
ATOM   2358  OG  SER A 298     120.418 134.907 138.400  1.00 92.76           O  
ATOM   2359  N   PRO A 299     119.134 138.764 138.120  1.00 86.95           N  
ATOM   2360  CA  PRO A 299     118.237 139.196 137.044  1.00 88.90           C  
ATOM   2361  C   PRO A 299     118.946 139.298 135.697  1.00 88.33           C  
ATOM   2362  O   PRO A 299     118.275 139.234 134.667  1.00 89.24           O  
ATOM   2363  CB  PRO A 299     117.766 140.572 137.515  1.00 89.98           C  
ATOM   2364  CG  PRO A 299     118.873 141.073 138.368  1.00 87.40           C  
ATOM   2365  CD  PRO A 299     119.493 139.871 139.024  1.00 86.07           C  
TER    2366      PRO A 299                                                      
HETATM 2367  N   NIO A 401     115.356 113.276 161.841  1.00 33.08           N  
HETATM 2368  C1  NIO A 401     115.995 113.779 160.763  1.00 33.71           C  
HETATM 2369  C2  NIO A 401     116.979 113.040 160.134  1.00 29.60           C  
HETATM 2370  C3  NIO A 401     117.300 111.812 160.596  1.00 34.09           C  
HETATM 2371  C4  NIO A 401     116.659 111.309 161.676  1.00 35.07           C  
HETATM 2372  C5  NIO A 401     115.676 112.050 162.305  1.00 33.89           C  
HETATM 2373  C6  NIO A 401     117.702 113.604 158.919  1.00 34.18           C  
HETATM 2374  O1  NIO A 401     118.277 112.829 158.115  1.00 37.28           O  
HETATM 2375  O2  NIO A 401     117.733 114.844 158.722  1.00 38.79           O  
CONECT   86 1395                                                                
CONECT  754 1352                                                                
CONECT 1352  754                                                                
CONECT 1395   86                                                                
CONECT 2367 2368 2372                                                           
CONECT 2368 2367 2369                                                           
CONECT 2369 2368 2370 2373                                                      
CONECT 2370 2369 2371                                                           
CONECT 2371 2370 2372                                                           
CONECT 2372 2367 2371                                                           
CONECT 2373 2369 2374 2375                                                      
CONECT 2374 2373                                                                
CONECT 2375 2373                                                                
MASTER      335    0    1    9    2    0    0    6 2374    1   13   37          
END