HEADER    MEMBRANE PROTEIN                        27-AUG-22   8EA0              
TITLE     CRYOEM STRUCTURE OF MINIGQ-COUPLED HM3R IN COMPLEX WITH IPEROXO (LOCAL
TITLE    2 REFINEMENT)                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M3;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 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: CHRM3;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GPCR, IXO, ACTIVE STATE, MEMBRANE PROTEIN, HM3R, IPEROXO              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.ZHANG,J.F.FAY,B.L.ROTH                                              
REVDAT   3   21-DEC-22 8EA0    1       JRNL                                     
REVDAT   2   14-DEC-22 8EA0    1       JRNL                                     
REVDAT   1   30-NOV-22 8EA0    0                                                
JRNL        AUTH   S.ZHANG,R.H.GUMPPER,X.P.HUANG,Y.LIU,B.E.KRUMM,C.CAO,J.F.FAY, 
JRNL        AUTH 2 B.L.ROTH                                                     
JRNL        TITL   MOLECULAR BASIS FOR SELECTIVE ACTIVATION OF DREADD-BASED     
JRNL        TITL 2 CHEMOGENETICS.                                               
JRNL        REF    NATURE                        V. 612   354 2022              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   36450989                                                     
JRNL        DOI    10.1038/S41586-022-05489-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.56 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
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)  : 2.560                          
REMARK   3   NUMBER OF PARTICLES               : 591814                         
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 8EA0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-22.                  
REMARK 100 THE DEPOSITION ID IS D_1000266370.                                   
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                 : HM3R                              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 2858                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TALOS ARCTICA              
REMARK 245   DETECTOR TYPE                     : GATAN K3 (6K X 4K)             
REMARK 245   MINIMUM DEFOCUS (NM)              : 300.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2100.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 5900.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     PHE A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     THR A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     ASP A    57                                                      
REMARK 465     ASP A    58                                                      
REMARK 465     ALA A   446                                                      
REMARK 465     GLY A   447                                                      
REMARK 465     LEU A   448                                                      
REMARK 465     GLN A   449                                                      
REMARK 465     ALA A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     GLY A   452                                                      
REMARK 465     THR A   453                                                      
REMARK 465     GLU A   454                                                      
REMARK 465     ALA A   455                                                      
REMARK 465     GLU A   456                                                      
REMARK 465     THR A   457                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     ASN A   459                                                      
REMARK 465     PHE A   460                                                      
REMARK 465     VAL A   461                                                      
REMARK 465     HIS A   462                                                      
REMARK 465     PRO A   463                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     LYS A   465                                                      
REMARK 465     ARG A   466                                                      
REMARK 465     PHE A   467                                                      
REMARK 465     ALA A   468                                                      
REMARK 465     LEU A   469                                                      
REMARK 465     LYS A   470                                                      
REMARK 465     THR A   471                                                      
REMARK 465     ARG A   472                                                      
REMARK 465     SER A   473                                                      
REMARK 465     GLN A   474                                                      
REMARK 465     ILE A   475                                                      
REMARK 465     THR A   476                                                      
REMARK 465     LYS A   477                                                      
REMARK 465     ARG A   478                                                      
REMARK 465     LYS A   479                                                      
REMARK 465     ARG A   480                                                      
REMARK 465     MET A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     LEU A   483                                                      
REMARK 465     VAL A   484                                                      
REMARK 465     LYS A   485                                                      
REMARK 465     ASP A   564                                                      
REMARK 465     LYS A   565                                                      
REMARK 465     LYS A   566                                                      
REMARK 465     LYS A   567                                                      
REMARK 465     ARG A   568                                                      
REMARK 465     ARG A   569                                                      
REMARK 465     LYS A   570                                                      
REMARK 465     GLN A   571                                                      
REMARK 465     GLN A   572                                                      
REMARK 465     TYR A   573                                                      
REMARK 465     GLN A   574                                                      
REMARK 465     GLN A   575                                                      
REMARK 465     ARG A   576                                                      
REMARK 465     GLN A   577                                                      
REMARK 465     SER A   578                                                      
REMARK 465     VAL A   579                                                      
REMARK 465     ILE A   580                                                      
REMARK 465     PHE A   581                                                      
REMARK 465     HIS A   582                                                      
REMARK 465     LYS A   583                                                      
REMARK 465     ARG A   584                                                      
REMARK 465     ALA A   585                                                      
REMARK 465     PRO A   586                                                      
REMARK 465     GLU A   587                                                      
REMARK 465     GLN A   588                                                      
REMARK 465     ALA A   589                                                      
REMARK 465     LEU A   590                                                      
REMARK 465     GLY A   591                                                      
REMARK 465     GLY A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 465     GLY A   594                                                      
REMARK 465     GLY A   595                                                      
REMARK 465     GLY A   596                                                      
REMARK 465     GLY A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     GLY A   599                                                      
REMARK 465     GLY A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     SER A   602                                                      
REMARK 465     SER A   603                                                      
REMARK 465     GLY A   604                                                      
REMARK 465     GLY A   605                                                      
REMARK 465     GLY A   606                                                      
REMARK 465     GLY A   607                                                      
REMARK 465     SER A   608                                                      
REMARK 465     GLY A   609                                                      
REMARK 465     GLY A   610                                                      
REMARK 465     GLY A   611                                                      
REMARK 465     GLY A   612                                                      
REMARK 465     SER A   613                                                      
REMARK 465     GLY A   614                                                      
REMARK 465     GLY A   615                                                      
REMARK 465     SER A   616                                                      
REMARK 465     SER A   617                                                      
REMARK 465     SER A   618                                                      
REMARK 465     GLY A   619                                                      
REMARK 465     GLY A   620                                                      
REMARK 465     VAL A   621                                                      
REMARK 465     PHE A   622                                                      
REMARK 465     THR A   623                                                      
REMARK 465     LEU A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     ASP A   626                                                      
REMARK 465     PHE A   627                                                      
REMARK 465     VAL A   628                                                      
REMARK 465     GLY A   629                                                      
REMARK 465     ASP A   630                                                      
REMARK 465     TRP A   631                                                      
REMARK 465     GLU A   632                                                      
REMARK 465     GLN A   633                                                      
REMARK 465     THR A   634                                                      
REMARK 465     ALA A   635                                                      
REMARK 465     ALA A   636                                                      
REMARK 465     TYR A   637                                                      
REMARK 465     ASN A   638                                                      
REMARK 465     LEU A   639                                                      
REMARK 465     ASP A   640                                                      
REMARK 465     GLN A   641                                                      
REMARK 465     VAL A   642                                                      
REMARK 465     LEU A   643                                                      
REMARK 465     GLU A   644                                                      
REMARK 465     GLN A   645                                                      
REMARK 465     GLY A   646                                                      
REMARK 465     GLY A   647                                                      
REMARK 465     VAL A   648                                                      
REMARK 465     SER A   649                                                      
REMARK 465     SER A   650                                                      
REMARK 465     LEU A   651                                                      
REMARK 465     LEU A   652                                                      
REMARK 465     GLN A   653                                                      
REMARK 465     ASN A   654                                                      
REMARK 465     LEU A   655                                                      
REMARK 465     ALA A   656                                                      
REMARK 465     VAL A   657                                                      
REMARK 465     SER A   658                                                      
REMARK 465     VAL A   659                                                      
REMARK 465     THR A   660                                                      
REMARK 465     PRO A   661                                                      
REMARK 465     ILE A   662                                                      
REMARK 465     GLN A   663                                                      
REMARK 465     ARG A   664                                                      
REMARK 465     ILE A   665                                                      
REMARK 465     VAL A   666                                                      
REMARK 465     ARG A   667                                                      
REMARK 465     SER A   668                                                      
REMARK 465     GLY A   669                                                      
REMARK 465     GLU A   670                                                      
REMARK 465     ASN A   671                                                      
REMARK 465     ALA A   672                                                      
REMARK 465     LEU A   673                                                      
REMARK 465     LYS A   674                                                      
REMARK 465     ILE A   675                                                      
REMARK 465     ASP A   676                                                      
REMARK 465     ILE A   677                                                      
REMARK 465     HIS A   678                                                      
REMARK 465     VAL A   679                                                      
REMARK 465     ILE A   680                                                      
REMARK 465     ILE A   681                                                      
REMARK 465     PRO A   682                                                      
REMARK 465     TYR A   683                                                      
REMARK 465     GLU A   684                                                      
REMARK 465     GLY A   685                                                      
REMARK 465     LEU A   686                                                      
REMARK 465     SER A   687                                                      
REMARK 465     ALA A   688                                                      
REMARK 465     ASP A   689                                                      
REMARK 465     GLN A   690                                                      
REMARK 465     MET A   691                                                      
REMARK 465     ALA A   692                                                      
REMARK 465     GLN A   693                                                      
REMARK 465     ILE A   694                                                      
REMARK 465     GLU A   695                                                      
REMARK 465     GLU A   696                                                      
REMARK 465     VAL A   697                                                      
REMARK 465     PHE A   698                                                      
REMARK 465     LYS A   699                                                      
REMARK 465     VAL A   700                                                      
REMARK 465     VAL A   701                                                      
REMARK 465     TYR A   702                                                      
REMARK 465     PRO A   703                                                      
REMARK 465     VAL A   704                                                      
REMARK 465     ASP A   705                                                      
REMARK 465     ASP A   706                                                      
REMARK 465     HIS A   707                                                      
REMARK 465     HIS A   708                                                      
REMARK 465     PHE A   709                                                      
REMARK 465     LYS A   710                                                      
REMARK 465     VAL A   711                                                      
REMARK 465     ILE A   712                                                      
REMARK 465     LEU A   713                                                      
REMARK 465     PRO A   714                                                      
REMARK 465     TYR A   715                                                      
REMARK 465     GLY A   716                                                      
REMARK 465     THR A   717                                                      
REMARK 465     LEU A   718                                                      
REMARK 465     VAL A   719                                                      
REMARK 465     ILE A   720                                                      
REMARK 465     ASP A   721                                                      
REMARK 465     GLY A   722                                                      
REMARK 465     VAL A   723                                                      
REMARK 465     THR A   724                                                      
REMARK 465     PRO A   725                                                      
REMARK 465     ASN A   726                                                      
REMARK 465     MET A   727                                                      
REMARK 465     LEU A   728                                                      
REMARK 465     ASN A   729                                                      
REMARK 465     TYR A   730                                                      
REMARK 465     PHE A   731                                                      
REMARK 465     GLY A   732                                                      
REMARK 465     ARG A   733                                                      
REMARK 465     PRO A   734                                                      
REMARK 465     TYR A   735                                                      
REMARK 465     GLU A   736                                                      
REMARK 465     GLY A   737                                                      
REMARK 465     ILE A   738                                                      
REMARK 465     ALA A   739                                                      
REMARK 465     VAL A   740                                                      
REMARK 465     PHE A   741                                                      
REMARK 465     ASP A   742                                                      
REMARK 465     GLY A   743                                                      
REMARK 465     LYS A   744                                                      
REMARK 465     LYS A   745                                                      
REMARK 465     ILE A   746                                                      
REMARK 465     THR A   747                                                      
REMARK 465     VAL A   748                                                      
REMARK 465     THR A   749                                                      
REMARK 465     GLY A   750                                                      
REMARK 465     THR A   751                                                      
REMARK 465     LEU A   752                                                      
REMARK 465     TRP A   753                                                      
REMARK 465     ASN A   754                                                      
REMARK 465     GLY A   755                                                      
REMARK 465     ASN A   756                                                      
REMARK 465     LYS A   757                                                      
REMARK 465     ILE A   758                                                      
REMARK 465     ILE A   759                                                      
REMARK 465     ASP A   760                                                      
REMARK 465     GLU A   761                                                      
REMARK 465     ARG A   762                                                      
REMARK 465     LEU A   763                                                      
REMARK 465     ILE A   764                                                      
REMARK 465     THR A   765                                                      
REMARK 465     PRO A   766                                                      
REMARK 465     ASP A   767                                                      
REMARK 465     GLY A   768                                                      
REMARK 465     SER A   769                                                      
REMARK 465     MET A   770                                                      
REMARK 465     LEU A   771                                                      
REMARK 465     PHE A   772                                                      
REMARK 465     ARG A   773                                                      
REMARK 465     VAL A   774                                                      
REMARK 465     THR A   775                                                      
REMARK 465     ILE A   776                                                      
REMARK 465     ASN A   777                                                      
REMARK 465     SER A   778                                                      
REMARK 465     GLY A   779                                                      
REMARK 465     GLY A   780                                                      
REMARK 465     SER A   781                                                      
REMARK 465     GLY A   782                                                      
REMARK 465     GLY A   783                                                      
REMARK 465     HIS A   784                                                      
REMARK 465     HIS A   785                                                      
REMARK 465     HIS A   786                                                      
REMARK 465     HIS A   787                                                      
REMARK 465     HIS A   788                                                      
REMARK 465     HIS A   789                                                      
REMARK 465     HIS A   790                                                      
REMARK 465     HIS A   791                                                      
REMARK 465     HIS A   792                                                      
REMARK 465     HIS A   793                                                      
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     HIS A  63    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP A  66    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  66    CZ3  CH2                                            
REMARK 470     LEU A 136    CG   CD1  CD2                                       
REMARK 470     LYS A 183    CG   CD   CE   NZ                                   
REMARK 470     LYS A 213    CG   CD   CE   NZ                                   
REMARK 470     GLN A 224    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 487    CG   CD   CE   NZ                                   
REMARK 470     ASP A 518    CG   OD1  OD2                                       
REMARK 470     LYS A 549    CG   CD   CE   NZ                                   
REMARK 470     LYS A 556    CG   CD   CE   NZ                                   
REMARK 470     MET A 557    CG   SD   CE                                        
REMARK 470     LEU A 559    CG   CD1  CD2                                       
REMARK 470     LEU A 560    CG   CD1  CD2                                       
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    LEU A  60      -97.82     54.30                                   
REMARK 500    ILE A 129      -60.64    -90.84                                   
REMARK 500    LEU A 139       46.94    -89.68                                   
REMARK 500    LEU A 199      -25.21   -140.49                                   
REMARK 500    GLN A 224       -5.78     78.27                                   
REMARK 500    PRO A 229       42.83    -84.76                                   
REMARK 500    THR A 230      -53.43   -120.44                                   
REMARK 500    SER A 519       26.09   -142.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-27970   RELATED DB: EMDB                             
REMARK 900 CRYOEM STRUCTURE OF GQ-COUPLED HM3R IN COMPLEX WITH IPEROXO          
DBREF  8EA0 A   46   463  UNP    P20309   ACM3_HUMAN      46    283             
DBREF  8EA0 A  464   590  UNP    P20309   ACM3_HUMAN     464    590             
SEQADV 8EA0 GLY A  591  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  592  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  593  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  594  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  595  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  596  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  597  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  598  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  599  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  600  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  601  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  602  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  603  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  604  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  605  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  606  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  607  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  608  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  609  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  610  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  611  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  612  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  613  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  614  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  615  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  616  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  617  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  618  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  619  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  620  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  621  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  622  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  623  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  624  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  625  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  626  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  627  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  628  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  629  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  630  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TRP A  631  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  632  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  633  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  634  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  635  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  636  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TYR A  637  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  638  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  639  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  640  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  641  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  642  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  643  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  644  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  645  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  646  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  647  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  648  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  649  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  650  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  651  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  652  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  653  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  654  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  655  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  656  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  657  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  658  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  659  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  660  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  661  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  662  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  663  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ARG A  664  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  665  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  666  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ARG A  667  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  668  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  669  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  670  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  671  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  672  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  673  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LYS A  674  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  675  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  676  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  677  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  678  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  679  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  680  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  681  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  682  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TYR A  683  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  684  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  685  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  686  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  687  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  688  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  689  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  690  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 MET A  691  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  692  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLN A  693  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  694  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  695  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  696  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  697  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  698  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LYS A  699  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  700  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  701  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TYR A  702  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  703  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  704  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  705  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  706  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  707  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  708  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  709  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LYS A  710  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  711  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  712  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  713  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  714  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TYR A  715  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  716  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  717  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  718  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  719  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  720  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  721  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  722  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  723  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  724  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  725  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  726  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 MET A  727  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  728  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  729  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TYR A  730  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  731  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  732  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ARG A  733  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  734  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TYR A  735  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  736  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  737  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  738  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ALA A  739  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  740  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  741  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  742  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  743  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LYS A  744  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LYS A  745  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  746  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  747  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  748  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  749  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  750  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  751  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  752  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 TRP A  753  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  754  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  755  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  756  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LYS A  757  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  758  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  759  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  760  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLU A  761  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ARG A  762  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  763  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  764  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  765  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PRO A  766  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASP A  767  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  768  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  769  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 MET A  770  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 LEU A  771  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 PHE A  772  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ARG A  773  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 VAL A  774  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 THR A  775  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ILE A  776  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 ASN A  777  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  778  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  779  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  780  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 SER A  781  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  782  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 GLY A  783  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  784  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  785  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  786  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  787  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  788  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  789  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  790  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  791  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  792  UNP  P20309              EXPRESSION TAG                 
SEQADV 8EA0 HIS A  793  UNP  P20309              EXPRESSION TAG                 
SEQRES   1 A  568  ALA GLY ASN PHE SER SER PRO ASP GLY THR THR ASP ASP          
SEQRES   2 A  568  PRO LEU GLY GLY HIS THR VAL TRP GLN VAL VAL PHE ILE          
SEQRES   3 A  568  ALA PHE LEU THR GLY ILE LEU ALA LEU VAL THR ILE ILE          
SEQRES   4 A  568  GLY ASN ILE LEU VAL ILE VAL SER PHE LYS VAL ASN LYS          
SEQRES   5 A  568  GLN LEU LYS THR VAL ASN ASN TYR PHE LEU LEU SER LEU          
SEQRES   6 A  568  ALA CYS ALA ASP LEU ILE ILE GLY VAL ILE SER MET ASN          
SEQRES   7 A  568  LEU PHE THR THR TYR ILE ILE MET ASN ARG TRP ALA LEU          
SEQRES   8 A  568  GLY ASN LEU ALA CYS ASP LEU TRP LEU ALA ILE ASP TYR          
SEQRES   9 A  568  VAL ALA SER ASN ALA SER VAL MET ASN LEU LEU VAL ILE          
SEQRES  10 A  568  SER PHE ASP ARG TYR PHE SER ILE THR ARG PRO LEU THR          
SEQRES  11 A  568  TYR ARG ALA LYS ARG THR THR LYS ARG ALA GLY VAL MET          
SEQRES  12 A  568  ILE GLY LEU ALA TRP VAL ILE SER PHE VAL LEU TRP ALA          
SEQRES  13 A  568  PRO ALA ILE LEU PHE TRP GLN TYR PHE VAL GLY LYS ARG          
SEQRES  14 A  568  THR VAL PRO PRO GLY GLU CYS PHE ILE GLN PHE LEU SER          
SEQRES  15 A  568  GLU PRO THR ILE THR PHE GLY THR ALA ILE ALA ALA PHE          
SEQRES  16 A  568  TYR MET PRO VAL THR ILE MET THR ILE LEU TYR TRP ARG          
SEQRES  17 A  568  ILE TYR LYS GLU THR GLU LYS ARG THR LYS GLU LEU ALA          
SEQRES  18 A  568  GLY LEU GLN ALA SER GLY THR GLU ALA GLU THR GLU ASN          
SEQRES  19 A  568  PHE VAL HIS PRO ALA LYS ARG PHE ALA LEU LYS THR ARG          
SEQRES  20 A  568  SER GLN ILE THR LYS ARG LYS ARG MET SER LEU VAL LYS          
SEQRES  21 A  568  GLU LYS LYS ALA ALA GLN THR LEU SER ALA ILE LEU LEU          
SEQRES  22 A  568  ALA PHE ILE ILE THR TRP THR PRO TYR ASN ILE MET VAL          
SEQRES  23 A  568  LEU VAL ASN THR PHE CYS ASP SER CYS ILE PRO LYS THR          
SEQRES  24 A  568  PHE TRP ASN LEU GLY TYR TRP LEU CYS TYR ILE ASN SER          
SEQRES  25 A  568  THR VAL ASN PRO VAL CYS TYR ALA LEU CYS ASN LYS THR          
SEQRES  26 A  568  PHE ARG THR THR PHE LYS MET LEU LEU LEU CYS GLN CYS          
SEQRES  27 A  568  ASP LYS LYS LYS ARG ARG LYS GLN GLN TYR GLN GLN ARG          
SEQRES  28 A  568  GLN SER VAL ILE PHE HIS LYS ARG ALA PRO GLU GLN ALA          
SEQRES  29 A  568  LEU GLY GLY SER GLY GLY GLY GLY SER GLY GLY SER SER          
SEQRES  30 A  568  SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY          
SEQRES  31 A  568  SER SER SER GLY GLY VAL PHE THR LEU GLU ASP PHE VAL          
SEQRES  32 A  568  GLY ASP TRP GLU GLN THR ALA ALA TYR ASN LEU ASP GLN          
SEQRES  33 A  568  VAL LEU GLU GLN GLY GLY VAL SER SER LEU LEU GLN ASN          
SEQRES  34 A  568  LEU ALA VAL SER VAL THR PRO ILE GLN ARG ILE VAL ARG          
SEQRES  35 A  568  SER GLY GLU ASN ALA LEU LYS ILE ASP ILE HIS VAL ILE          
SEQRES  36 A  568  ILE PRO TYR GLU GLY LEU SER ALA ASP GLN MET ALA GLN          
SEQRES  37 A  568  ILE GLU GLU VAL PHE LYS VAL VAL TYR PRO VAL ASP ASP          
SEQRES  38 A  568  HIS HIS PHE LYS VAL ILE LEU PRO TYR GLY THR LEU VAL          
SEQRES  39 A  568  ILE ASP GLY VAL THR PRO ASN MET LEU ASN TYR PHE GLY          
SEQRES  40 A  568  ARG PRO TYR GLU GLY ILE ALA VAL PHE ASP GLY LYS LYS          
SEQRES  41 A  568  ILE THR VAL THR GLY THR LEU TRP ASN GLY ASN LYS ILE          
SEQRES  42 A  568  ILE ASP GLU ARG LEU ILE THR PRO ASP GLY SER MET LEU          
SEQRES  43 A  568  PHE ARG VAL THR ILE ASN SER GLY GLY SER GLY GLY HIS          
SEQRES  44 A  568  HIS HIS HIS HIS HIS HIS HIS HIS HIS                          
HET    IXO  A 801      14                                                       
HET    Y01  A 802      35                                                       
HETNAM     IXO 4-(4,5-DIHYDRO-1,2-OXAZOL-3-YLOXY)-N,N,N-TRIMETHYLBUT-           
HETNAM   2 IXO  2-YN-1-AMINIUM                                                  
HETNAM     Y01 CHOLESTEROL HEMISUCCINATE                                        
HETSYN     IXO IPEROXO                                                          
FORMUL   2  IXO    C10 H17 N2 O2 1+                                             
FORMUL   3  Y01    C31 H50 O4                                                   
HELIX    1 AA1 THR A   64  ASN A   96  1                                  33    
HELIX    2 AA2 THR A  101  ASN A  103  5                                   3    
HELIX    3 AA3 ASN A  104  ILE A  120  1                                  17    
HELIX    4 AA4 ILE A  120  MET A  131  1                                  12    
HELIX    5 AA5 GLY A  137  ARG A  172  1                                  36    
HELIX    6 AA6 THR A  175  ARG A  180  1                                   6    
HELIX    7 AA7 THR A  181  VAL A  211  1                                  31    
HELIX    8 AA8 THR A  230  PHE A  240  1                                  11    
HELIX    9 AA9 PHE A  240  LEU A  265  1                                  26    
HELIX   10 AB1 LYS A  488  THR A  503  1                                  16    
HELIX   11 AB2 TRP A  504  CYS A  517  1                                  14    
HELIX   12 AB3 PRO A  522  TYR A  534  1                                  13    
HELIX   13 AB4 TYR A  534  ALA A  545  1                                  12    
HELIX   14 AB5 ASN A  548  CYS A  561  1                                  14    
SSBOND   1 CYS A  141    CYS A  221                          1555   1555  2.03  
SSBOND   2 CYS A  517    CYS A  520                          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   PRO A  59     103.541 118.115 163.414  1.00 76.11           N  
ATOM      2  CA  PRO A  59     104.258 118.814 164.485  1.00 76.11           C  
ATOM      3  C   PRO A  59     104.837 117.856 165.520  1.00 76.11           C  
ATOM      4  O   PRO A  59     105.961 118.060 165.979  1.00 76.11           O  
ATOM      5  CB  PRO A  59     103.178 119.702 165.109  1.00 76.11           C  
ATOM      6  CG  PRO A  59     102.184 119.907 164.019  1.00 76.11           C  
ATOM      7  CD  PRO A  59     102.172 118.628 163.236  1.00 76.11           C  
ATOM      8  N   LEU A  60     104.066 116.825 165.872  1.00 76.61           N  
ATOM      9  CA  LEU A  60     104.479 115.821 166.847  1.00 76.61           C  
ATOM     10  C   LEU A  60     104.897 116.474 168.160  1.00 76.61           C  
ATOM     11  O   LEU A  60     104.049 116.808 168.994  1.00 76.61           O  
ATOM     12  CB  LEU A  60     105.619 114.963 166.289  1.00 76.61           C  
ATOM     13  CG  LEU A  60     105.257 113.754 165.419  1.00 76.61           C  
ATOM     14  CD1 LEU A  60     104.430 112.749 166.207  1.00 76.61           C  
ATOM     15  CD2 LEU A  60     104.536 114.166 164.140  1.00 76.61           C  
ATOM     16  N   GLY A  61     106.202 116.662 168.349  1.00 84.35           N  
ATOM     17  CA  GLY A  61     106.721 117.313 169.532  1.00 84.35           C  
ATOM     18  C   GLY A  61     106.723 118.822 169.495  1.00 84.35           C  
ATOM     19  O   GLY A  61     107.096 119.457 170.485  1.00 84.35           O  
ATOM     20  N   GLY A  62     106.320 119.419 168.377  1.00 85.20           N  
ATOM     21  CA  GLY A  62     106.273 120.862 168.254  1.00 85.20           C  
ATOM     22  C   GLY A  62     105.006 121.467 168.822  1.00 85.20           C  
ATOM     23  O   GLY A  62     104.102 121.846 168.071  1.00 85.20           O  
ATOM     24  N   HIS A  63     104.928 121.558 170.148  1.00 88.98           N  
ATOM     25  CA  HIS A  63     103.746 122.108 170.795  1.00 88.98           C  
ATOM     26  C   HIS A  63     103.577 123.584 170.441  1.00 88.98           C  
ATOM     27  O   HIS A  63     104.510 124.255 169.989  1.00 88.98           O  
ATOM     28  CB  HIS A  63     103.838 121.937 172.311  1.00 88.98           C  
ATOM     29  N   THR A  64     102.357 124.085 170.652  1.00 88.27           N  
ATOM     30  CA  THR A  64     101.969 125.454 170.305  1.00 88.27           C  
ATOM     31  C   THR A  64     102.203 125.715 168.812  1.00 88.27           C  
ATOM     32  O   THR A  64     103.031 126.532 168.403  1.00 88.27           O  
ATOM     33  CB  THR A  64     102.707 126.481 171.174  1.00 88.27           C  
ATOM     34  OG1 THR A  64     104.077 126.565 170.764  1.00 88.27           O  
ATOM     35  CG2 THR A  64     102.642 126.082 172.640  1.00 88.27           C  
ATOM     36  N   VAL A  65     101.437 124.975 168.005  1.00 86.75           N  
ATOM     37  CA  VAL A  65     101.585 125.022 166.555  1.00 86.75           C  
ATOM     38  C   VAL A  65     101.234 126.388 165.984  1.00 86.75           C  
ATOM     39  O   VAL A  65     101.644 126.711 164.864  1.00 86.75           O  
ATOM     40  CB  VAL A  65     100.724 123.923 165.898  1.00 86.75           C  
ATOM     41  CG1 VAL A  65     101.151 122.551 166.391  1.00 86.75           C  
ATOM     42  CG2 VAL A  65      99.249 124.165 166.181  1.00 86.75           C  
ATOM     43  N   TRP A  66     100.482 127.204 166.727  1.00 88.26           N  
ATOM     44  CA  TRP A  66     100.081 128.513 166.224  1.00 88.26           C  
ATOM     45  C   TRP A  66     101.267 129.447 166.022  1.00 88.26           C  
ATOM     46  O   TRP A  66     101.136 130.451 165.313  1.00 88.26           O  
ATOM     47  CB  TRP A  66      99.070 129.153 167.177  1.00 88.26           C  
ATOM     48  N   GLN A  67     102.417 129.145 166.625  1.00 86.62           N  
ATOM     49  CA  GLN A  67     103.600 129.979 166.496  1.00 86.62           C  
ATOM     50  C   GLN A  67     104.757 129.303 165.773  1.00 86.62           C  
ATOM     51  O   GLN A  67     105.712 129.994 165.401  1.00 86.62           O  
ATOM     52  CB  GLN A  67     104.081 130.443 167.881  1.00 86.62           C  
ATOM     53  CG  GLN A  67     103.258 131.575 168.480  1.00 86.62           C  
ATOM     54  CD  GLN A  67     101.925 131.103 169.031  1.00 86.62           C  
ATOM     55  OE1 GLN A  67     101.673 129.902 169.140  1.00 86.62           O  
ATOM     56  NE2 GLN A  67     101.062 132.050 169.382  1.00 86.62           N  
ATOM     57  N   VAL A  68     104.706 127.983 165.561  1.00 80.51           N  
ATOM     58  CA  VAL A  68     105.780 127.286 164.860  1.00 80.51           C  
ATOM     59  C   VAL A  68     105.568 127.255 163.354  1.00 80.51           C  
ATOM     60  O   VAL A  68     106.445 126.775 162.625  1.00 80.51           O  
ATOM     61  CB  VAL A  68     105.948 125.844 165.379  1.00 80.51           C  
ATOM     62  CG1 VAL A  68     106.061 125.836 166.897  1.00 80.51           C  
ATOM     63  CG2 VAL A  68     104.797 124.970 164.907  1.00 80.51           C  
ATOM     64  N   VAL A  69     104.426 127.744 162.864  1.00 75.47           N  
ATOM     65  CA  VAL A  69     104.212 127.834 161.424  1.00 75.47           C  
ATOM     66  C   VAL A  69     105.112 128.892 160.799  1.00 75.47           C  
ATOM     67  O   VAL A  69     105.311 128.893 159.578  1.00 75.47           O  
ATOM     68  CB  VAL A  69     102.726 128.115 161.126  1.00 75.47           C  
ATOM     69  CG1 VAL A  69     102.364 129.545 161.504  1.00 75.47           C  
ATOM     70  CG2 VAL A  69     102.396 127.829 159.665  1.00 75.47           C  
ATOM     71  N   PHE A  70     105.672 129.792 161.612  1.00 70.87           N  
ATOM     72  CA  PHE A  70     106.553 130.829 161.086  1.00 70.87           C  
ATOM     73  C   PHE A  70     107.804 130.228 160.456  1.00 70.87           C  
ATOM     74  O   PHE A  70     108.240 130.668 159.386  1.00 70.87           O  
ATOM     75  CB  PHE A  70     106.929 131.809 162.197  1.00 70.87           C  
ATOM     76  CG  PHE A  70     107.454 133.123 161.696  1.00 70.87           C  
ATOM     77  CD1 PHE A  70     106.593 134.077 161.179  1.00 70.87           C  
ATOM     78  CD2 PHE A  70     108.809 133.406 161.743  1.00 70.87           C  
ATOM     79  CE1 PHE A  70     107.073 135.288 160.716  1.00 70.87           C  
ATOM     80  CE2 PHE A  70     109.295 134.613 161.281  1.00 70.87           C  
ATOM     81  CZ  PHE A  70     108.426 135.556 160.767  1.00 70.87           C  
ATOM     82  N   ILE A  71     108.399 129.225 161.105  1.00 66.59           N  
ATOM     83  CA  ILE A  71     109.592 128.597 160.545  1.00 66.59           C  
ATOM     84  C   ILE A  71     109.236 127.746 159.331  1.00 66.59           C  
ATOM     85  O   ILE A  71     110.034 127.627 158.393  1.00 66.59           O  
ATOM     86  CB  ILE A  71     110.333 127.784 161.625  1.00 66.59           C  
ATOM     87  CG1 ILE A  71     109.550 126.526 162.009  1.00 66.59           C  
ATOM     88  CG2 ILE A  71     110.592 128.644 162.856  1.00 66.59           C  
ATOM     89  CD1 ILE A  71     110.244 125.665 163.041  1.00 66.59           C  
ATOM     90  N   ALA A  72     108.045 127.143 159.323  1.00 63.55           N  
ATOM     91  CA  ALA A  72     107.606 126.369 158.167  1.00 63.55           C  
ATOM     92  C   ALA A  72     107.328 127.269 156.972  1.00 63.55           C  
ATOM     93  O   ALA A  72     107.708 126.949 155.840  1.00 63.55           O  
ATOM     94  CB  ALA A  72     106.358 125.565 158.524  1.00 63.55           C  
ATOM     95  N   PHE A  73     106.654 128.396 157.206  1.00 62.33           N  
ATOM     96  CA  PHE A  73     106.330 129.310 156.118  1.00 62.33           C  
ATOM     97  C   PHE A  73     107.585 129.941 155.529  1.00 62.33           C  
ATOM     98  O   PHE A  73     107.716 130.050 154.304  1.00 62.33           O  
ATOM     99  CB  PHE A  73     105.368 130.382 156.623  1.00 62.33           C  
ATOM    100  CG  PHE A  73     104.827 131.261 155.546  1.00 62.33           C  
ATOM    101  CD1 PHE A  73     105.306 132.548 155.384  1.00 62.33           C  
ATOM    102  CD2 PHE A  73     103.840 130.803 154.691  1.00 62.33           C  
ATOM    103  CE1 PHE A  73     104.810 133.363 154.392  1.00 62.33           C  
ATOM    104  CE2 PHE A  73     103.340 131.614 153.694  1.00 62.33           C  
ATOM    105  CZ  PHE A  73     103.827 132.896 153.544  1.00 62.33           C  
ATOM    106  N   LEU A  74     108.517 130.368 156.386  1.00 57.42           N  
ATOM    107  CA  LEU A  74     109.762 130.952 155.900  1.00 57.42           C  
ATOM    108  C   LEU A  74     110.583 129.932 155.122  1.00 57.42           C  
ATOM    109  O   LEU A  74     111.171 130.257 154.084  1.00 57.42           O  
ATOM    110  CB  LEU A  74     110.570 131.505 157.073  1.00 57.42           C  
ATOM    111  CG  LEU A  74     111.876 132.207 156.705  1.00 57.42           C  
ATOM    112  CD1 LEU A  74     111.599 133.432 155.850  1.00 57.42           C  
ATOM    113  CD2 LEU A  74     112.650 132.583 157.956  1.00 57.42           C  
ATOM    114  N   THR A  75     110.634 128.693 155.612  1.00 52.73           N  
ATOM    115  CA  THR A  75     111.394 127.650 154.931  1.00 52.73           C  
ATOM    116  C   THR A  75     110.827 127.361 153.547  1.00 52.73           C  
ATOM    117  O   THR A  75     111.581 127.180 152.584  1.00 52.73           O  
ATOM    118  CB  THR A  75     111.408 126.381 155.781  1.00 52.73           C  
ATOM    119  OG1 THR A  75     112.104 126.634 157.008  1.00 52.73           O  
ATOM    120  CG2 THR A  75     112.085 125.255 155.039  1.00 52.73           C  
ATOM    121  N   GLY A  76     109.499 127.312 153.428  1.00 51.75           N  
ATOM    122  CA  GLY A  76     108.892 127.068 152.130  1.00 51.75           C  
ATOM    123  C   GLY A  76     109.197 128.162 151.127  1.00 51.75           C  
ATOM    124  O   GLY A  76     109.409 127.890 149.942  1.00 51.75           O  
ATOM    125  N   ILE A  77     109.216 129.416 151.584  1.00 50.53           N  
ATOM    126  CA  ILE A  77     109.546 130.529 150.697  1.00 50.53           C  
ATOM    127  C   ILE A  77     110.979 130.402 150.196  1.00 50.53           C  
ATOM    128  O   ILE A  77     111.255 130.562 149.001  1.00 50.53           O  
ATOM    129  CB  ILE A  77     109.314 131.873 151.413  1.00 50.53           C  
ATOM    130  CG1 ILE A  77     107.834 132.252 151.370  1.00 50.53           C  
ATOM    131  CG2 ILE A  77     110.160 132.973 150.789  1.00 50.53           C  
ATOM    132  CD1 ILE A  77     107.513 133.511 152.133  1.00 50.53           C  
ATOM    133  N   LEU A  78     111.911 130.101 151.102  1.00 45.80           N  
ATOM    134  CA  LEU A  78     113.312 129.980 150.713  1.00 45.80           C  
ATOM    135  C   LEU A  78     113.541 128.788 149.794  1.00 45.80           C  
ATOM    136  O   LEU A  78     114.382 128.858 148.890  1.00 45.80           O  
ATOM    137  CB  LEU A  78     114.192 129.878 151.956  1.00 45.80           C  
ATOM    138  CG  LEU A  78     114.353 131.176 152.752  1.00 45.80           C  
ATOM    139  CD1 LEU A  78     115.595 131.124 153.618  1.00 45.80           C  
ATOM    140  CD2 LEU A  78     114.396 132.380 151.821  1.00 45.80           C  
ATOM    141  N   ALA A  79     112.818 127.688 150.011  1.00 44.44           N  
ATOM    142  CA  ALA A  79     112.916 126.552 149.101  1.00 44.44           C  
ATOM    143  C   ALA A  79     112.379 126.903 147.720  1.00 44.44           C  
ATOM    144  O   ALA A  79     112.944 126.483 146.704  1.00 44.44           O  
ATOM    145  CB  ALA A  79     112.174 125.348 149.679  1.00 44.44           C  
ATOM    146  N   LEU A  80     111.285 127.667 147.662  1.00 44.39           N  
ATOM    147  CA  LEU A  80     110.722 128.061 146.374  1.00 44.39           C  
ATOM    148  C   LEU A  80     111.678 128.960 145.600  1.00 44.39           C  
ATOM    149  O   LEU A  80     111.830 128.812 144.383  1.00 44.39           O  
ATOM    150  CB  LEU A  80     109.380 128.763 146.579  1.00 44.39           C  
ATOM    151  CG  LEU A  80     108.177 127.867 146.872  1.00 44.39           C  
ATOM    152  CD1 LEU A  80     106.935 128.707 147.125  1.00 44.39           C  
ATOM    153  CD2 LEU A  80     107.946 126.891 145.731  1.00 44.39           C  
ATOM    154  N   VAL A  81     112.325 129.903 146.289  1.00 41.84           N  
ATOM    155  CA  VAL A  81     113.239 130.825 145.619  1.00 41.84           C  
ATOM    156  C   VAL A  81     114.421 130.070 145.026  1.00 41.84           C  
ATOM    157  O   VAL A  81     114.848 130.343 143.897  1.00 41.84           O  
ATOM    158  CB  VAL A  81     113.697 131.925 146.595  1.00 41.84           C  
ATOM    159  CG1 VAL A  81     114.801 132.764 145.973  1.00 41.84           C  
ATOM    160  CG2 VAL A  81     112.522 132.801 146.992  1.00 41.84           C  
ATOM    161  N   THR A  82     114.970 129.110 145.774  1.00 39.43           N  
ATOM    162  CA  THR A  82     116.098 128.331 145.272  1.00 39.43           C  
ATOM    163  C   THR A  82     115.714 127.540 144.028  1.00 39.43           C  
ATOM    164  O   THR A  82     116.476 127.488 143.056  1.00 39.43           O  
ATOM    165  CB  THR A  82     116.616 127.392 146.361  1.00 39.43           C  
ATOM    166  OG1 THR A  82     116.834 128.131 147.568  1.00 39.43           O  
ATOM    167  CG2 THR A  82     117.920 126.742 145.929  1.00 39.43           C  
ATOM    168  N   ILE A  83     114.535 126.915 144.040  1.00 39.62           N  
ATOM    169  CA  ILE A  83     114.088 126.160 142.874  1.00 39.62           C  
ATOM    170  C   ILE A  83     113.774 127.098 141.715  1.00 39.62           C  
ATOM    171  O   ILE A  83     114.170 126.845 140.571  1.00 39.62           O  
ATOM    172  CB  ILE A  83     112.877 125.283 143.239  1.00 39.62           C  
ATOM    173  CG1 ILE A  83     113.240 124.312 144.362  1.00 39.62           C  
ATOM    174  CG2 ILE A  83     112.383 124.520 142.023  1.00 39.62           C  
ATOM    175  CD1 ILE A  83     112.067 123.503 144.870  1.00 39.62           C  
ATOM    176  N   ILE A  84     113.062 128.192 141.987  1.00 40.47           N  
ATOM    177  CA  ILE A  84     112.696 129.129 140.929  1.00 40.47           C  
ATOM    178  C   ILE A  84     113.939 129.796 140.350  1.00 40.47           C  
ATOM    179  O   ILE A  84     114.093 129.906 139.129  1.00 40.47           O  
ATOM    180  CB  ILE A  84     111.690 130.168 141.457  1.00 40.47           C  
ATOM    181  CG1 ILE A  84     110.286 129.566 141.521  1.00 40.47           C  
ATOM    182  CG2 ILE A  84     111.693 131.417 140.589  1.00 40.47           C  
ATOM    183  CD1 ILE A  84     109.289 130.422 142.269  1.00 40.47           C  
ATOM    184  N   GLY A  85     114.847 130.244 141.219  1.00 38.55           N  
ATOM    185  CA  GLY A  85     116.027 130.946 140.744  1.00 38.55           C  
ATOM    186  C   GLY A  85     116.957 130.069 139.927  1.00 38.55           C  
ATOM    187  O   GLY A  85     117.467 130.492 138.887  1.00 38.55           O  
ATOM    188  N   ASN A  86     117.189 128.837 140.382  1.00 37.56           N  
ATOM    189  CA  ASN A  86     118.126 127.957 139.693  1.00 37.56           C  
ATOM    190  C   ASN A  86     117.550 127.393 138.401  1.00 37.56           C  
ATOM    191  O   ASN A  86     118.301 127.160 137.448  1.00 37.56           O  
ATOM    192  CB  ASN A  86     118.558 126.821 140.620  1.00 37.56           C  
ATOM    193  CG  ASN A  86     119.626 127.251 141.604  1.00 37.56           C  
ATOM    194  OD1 ASN A  86     119.392 127.297 142.811  1.00 37.56           O  
ATOM    195  ND2 ASN A  86     120.806 127.574 141.090  1.00 37.56           N  
ATOM    196  N   ILE A  87     116.237 127.160 138.349  1.00 37.15           N  
ATOM    197  CA  ILE A  87     115.614 126.720 137.103  1.00 37.15           C  
ATOM    198  C   ILE A  87     115.733 127.806 136.043  1.00 37.15           C  
ATOM    199  O   ILE A  87     115.958 127.519 134.860  1.00 37.15           O  
ATOM    200  CB  ILE A  87     114.146 126.319 137.348  1.00 37.15           C  
ATOM    201  CG1 ILE A  87     114.072 124.936 137.994  1.00 37.15           C  
ATOM    202  CG2 ILE A  87     113.351 126.334 136.051  1.00 37.15           C  
ATOM    203  CD1 ILE A  87     112.672 124.526 138.386  1.00 37.15           C  
ATOM    204  N   LEU A  88     115.606 129.072 136.453  1.00 38.80           N  
ATOM    205  CA  LEU A  88     115.727 130.177 135.508  1.00 38.80           C  
ATOM    206  C   LEU A  88     117.101 130.194 134.850  1.00 38.80           C  
ATOM    207  O   LEU A  88     117.220 130.498 133.658  1.00 38.80           O  
ATOM    208  CB  LEU A  88     115.453 131.504 136.214  1.00 38.80           C  
ATOM    209  CG  LEU A  88     113.984 131.843 136.468  1.00 38.80           C  
ATOM    210  CD1 LEU A  88     113.859 133.186 137.167  1.00 38.80           C  
ATOM    211  CD2 LEU A  88     113.196 131.834 135.169  1.00 38.80           C  
ATOM    212  N   VAL A  89     118.150 129.875 135.611  1.00 36.88           N  
ATOM    213  CA  VAL A  89     119.490 129.789 135.035  1.00 36.88           C  
ATOM    214  C   VAL A  89     119.543 128.694 133.977  1.00 36.88           C  
ATOM    215  O   VAL A  89     120.152 128.864 132.914  1.00 36.88           O  
ATOM    216  CB  VAL A  89     120.534 129.556 136.143  1.00 36.88           C  
ATOM    217  CG1 VAL A  89     121.919 129.366 135.543  1.00 36.88           C  
ATOM    218  CG2 VAL A  89     120.530 130.709 137.132  1.00 36.88           C  
ATOM    219  N   ILE A  90     118.908 127.555 134.252  1.00 35.70           N  
ATOM    220  CA  ILE A  90     118.954 126.429 133.325  1.00 35.70           C  
ATOM    221  C   ILE A  90     118.186 126.749 132.048  1.00 35.70           C  
ATOM    222  O   ILE A  90     118.675 126.518 130.936  1.00 35.70           O  
ATOM    223  CB  ILE A  90     118.417 125.156 134.004  1.00 35.70           C  
ATOM    224  CG1 ILE A  90     119.255 124.816 135.236  1.00 35.70           C  
ATOM    225  CG2 ILE A  90     118.407 123.992 133.028  1.00 35.70           C  
ATOM    226  CD1 ILE A  90     118.679 123.705 136.082  1.00 35.70           C  
ATOM    227  N   VAL A  91     116.972 127.285 132.184  1.00 38.73           N  
ATOM    228  CA  VAL A  91     116.146 127.528 131.005  1.00 38.73           C  
ATOM    229  C   VAL A  91     116.650 128.725 130.206  1.00 38.73           C  
ATOM    230  O   VAL A  91     116.493 128.762 128.980  1.00 38.73           O  
ATOM    231  CB  VAL A  91     114.669 127.693 131.401  1.00 38.73           C  
ATOM    232  CG1 VAL A  91     114.142 126.406 132.018  1.00 38.73           C  
ATOM    233  CG2 VAL A  91     114.492 128.857 132.356  1.00 38.73           C  
ATOM    234  N   SER A  92     117.250 129.719 130.867  1.00 39.72           N  
ATOM    235  CA  SER A  92     117.829 130.843 130.138  1.00 39.72           C  
ATOM    236  C   SER A  92     118.987 130.388 129.261  1.00 39.72           C  
ATOM    237  O   SER A  92     119.178 130.908 128.156  1.00 39.72           O  
ATOM    238  CB  SER A  92     118.290 131.924 131.112  1.00 39.72           C  
ATOM    239  OG  SER A  92     117.270 132.229 132.042  1.00 39.72           O  
ATOM    240  N   PHE A  93     119.771 129.422 129.742  1.00 38.12           N  
ATOM    241  CA  PHE A  93     120.856 128.871 128.939  1.00 38.12           C  
ATOM    242  C   PHE A  93     120.325 128.224 127.666  1.00 38.12           C  
ATOM    243  O   PHE A  93     120.907 128.386 126.588  1.00 38.12           O  
ATOM    244  CB  PHE A  93     121.649 127.862 129.772  1.00 38.12           C  
ATOM    245  CG  PHE A  93     122.880 127.337 129.091  1.00 38.12           C  
ATOM    246  CD1 PHE A  93     122.823 126.194 128.310  1.00 38.12           C  
ATOM    247  CD2 PHE A  93     124.097 127.976 129.246  1.00 38.12           C  
ATOM    248  CE1 PHE A  93     123.954 125.707 127.687  1.00 38.12           C  
ATOM    249  CE2 PHE A  93     125.232 127.491 128.627  1.00 38.12           C  
ATOM    250  CZ  PHE A  93     125.159 126.356 127.846  1.00 38.12           C  
ATOM    251  N   LYS A  94     119.215 127.490 127.771  1.00 43.28           N  
ATOM    252  CA  LYS A  94     118.689 126.770 126.616  1.00 43.28           C  
ATOM    253  C   LYS A  94     118.091 127.718 125.582  1.00 43.28           C  
ATOM    254  O   LYS A  94     118.293 127.534 124.377  1.00 43.28           O  
ATOM    255  CB  LYS A  94     117.646 125.748 127.068  1.00 43.28           C  
ATOM    256  CG  LYS A  94     118.223 124.559 127.817  1.00 43.28           C  
ATOM    257  CD  LYS A  94     118.404 123.362 126.899  1.00 43.28           C  
ATOM    258  CE  LYS A  94     119.145 122.234 127.600  1.00 43.28           C  
ATOM    259  NZ  LYS A  94     120.622 122.375 127.479  1.00 43.28           N  
ATOM    260  N   VAL A  95     117.354 128.737 126.028  1.00 42.45           N  
ATOM    261  CA  VAL A  95     116.602 129.573 125.097  1.00 42.45           C  
ATOM    262  C   VAL A  95     117.416 130.724 124.514  1.00 42.45           C  
ATOM    263  O   VAL A  95     117.025 131.281 123.479  1.00 42.45           O  
ATOM    264  CB  VAL A  95     115.332 130.132 125.766  1.00 42.45           C  
ATOM    265  CG1 VAL A  95     114.515 129.003 126.379  1.00 42.45           C  
ATOM    266  CG2 VAL A  95     115.690 131.173 126.814  1.00 42.45           C  
ATOM    267  N   ASN A  96     118.529 131.097 125.138  1.00 43.04           N  
ATOM    268  CA  ASN A  96     119.366 132.189 124.656  1.00 43.04           C  
ATOM    269  C   ASN A  96     120.569 131.606 123.926  1.00 43.04           C  
ATOM    270  O   ASN A  96     121.384 130.900 124.530  1.00 43.04           O  
ATOM    271  CB  ASN A  96     119.815 133.085 125.810  1.00 43.04           C  
ATOM    272  CG  ASN A  96     120.232 134.468 125.346  1.00 43.04           C  
ATOM    273  OD1 ASN A  96     120.969 134.613 124.371  1.00 43.04           O  
ATOM    274  ND2 ASN A  96     119.759 135.492 126.044  1.00 43.04           N  
ATOM    275  N   LYS A  97     120.675 131.903 122.629  1.00 43.82           N  
ATOM    276  CA  LYS A  97     121.772 131.367 121.829  1.00 43.82           C  
ATOM    277  C   LYS A  97     123.117 131.924 122.278  1.00 43.82           C  
ATOM    278  O   LYS A  97     124.102 131.182 122.367  1.00 43.82           O  
ATOM    279  CB  LYS A  97     121.536 131.664 120.347  1.00 43.82           C  
ATOM    280  CG  LYS A  97     120.254 131.065 119.763  1.00 43.82           C  
ATOM    281  CD  LYS A  97     120.336 129.545 119.613  1.00 43.82           C  
ATOM    282  CE  LYS A  97     119.685 128.807 120.781  1.00 43.82           C  
ATOM    283  NZ  LYS A  97     119.701 127.335 120.584  1.00 43.82           N  
ATOM    284  N   GLN A  98     123.180 133.226 122.566  1.00 42.54           N  
ATOM    285  CA  GLN A  98     124.445 133.847 122.942  1.00 42.54           C  
ATOM    286  C   GLN A  98     124.964 133.356 124.287  1.00 42.54           C  
ATOM    287  O   GLN A  98     126.159 133.499 124.565  1.00 42.54           O  
ATOM    288  CB  GLN A  98     124.296 135.367 122.967  1.00 42.54           C  
ATOM    289  CG  GLN A  98     124.212 136.000 121.591  1.00 42.54           C  
ATOM    290  CD  GLN A  98     123.541 137.356 121.615  1.00 42.54           C  
ATOM    291  OE1 GLN A  98     123.744 138.143 122.538  1.00 42.54           O  
ATOM    292  NE2 GLN A  98     122.736 137.637 120.598  1.00 42.54           N  
ATOM    293  N   LEU A  99     124.100 132.785 125.125  1.00 40.73           N  
ATOM    294  CA  LEU A  99     124.512 132.270 126.423  1.00 40.73           C  
ATOM    295  C   LEU A  99     125.047 130.846 126.360  1.00 40.73           C  
ATOM    296  O   LEU A  99     125.579 130.357 127.362  1.00 40.73           O  
ATOM    297  CB  LEU A  99     123.343 132.328 127.410  1.00 40.73           C  
ATOM    298  CG  LEU A  99     123.035 133.705 127.997  1.00 40.73           C  
ATOM    299  CD1 LEU A  99     121.805 133.650 128.887  1.00 40.73           C  
ATOM    300  CD2 LEU A  99     124.234 134.235 128.762  1.00 40.73           C  
ATOM    301  N   LYS A 100     124.927 130.174 125.216  1.00 41.52           N  
ATOM    302  CA  LYS A 100     125.371 128.792 125.090  1.00 41.52           C  
ATOM    303  C   LYS A 100     126.859 128.716 124.776  1.00 41.52           C  
ATOM    304  O   LYS A 100     127.261 128.090 123.790  1.00 41.52           O  
ATOM    305  CB  LYS A 100     124.566 128.071 124.008  1.00 41.52           C  
ATOM    306  CG  LYS A 100     123.114 127.833 124.379  1.00 41.52           C  
ATOM    307  CD  LYS A 100     122.330 127.245 123.220  1.00 41.52           C  
ATOM    308  CE  LYS A 100     122.740 125.810 122.945  1.00 41.52           C  
ATOM    309  NZ  LYS A 100     121.895 125.193 121.887  1.00 41.52           N  
ATOM    310  N   THR A 101     127.681 129.348 125.606  1.00 40.45           N  
ATOM    311  CA  THR A 101     129.125 129.331 125.454  1.00 40.45           C  
ATOM    312  C   THR A 101     129.744 128.413 126.498  1.00 40.45           C  
ATOM    313  O   THR A 101     129.101 128.020 127.474  1.00 40.45           O  
ATOM    314  CB  THR A 101     129.713 130.741 125.584  1.00 40.45           C  
ATOM    315  OG1 THR A 101     129.194 131.369 126.761  1.00 40.45           O  
ATOM    316  CG2 THR A 101     129.352 131.579 124.369  1.00 40.45           C  
ATOM    317  N   VAL A 102     131.013 128.066 126.276  1.00 38.00           N  
ATOM    318  CA  VAL A 102     131.702 127.193 127.215  1.00 38.00           C  
ATOM    319  C   VAL A 102     131.936 127.893 128.551  1.00 38.00           C  
ATOM    320  O   VAL A 102     132.151 127.225 129.569  1.00 38.00           O  
ATOM    321  CB  VAL A 102     133.014 126.688 126.591  1.00 38.00           C  
ATOM    322  CG1 VAL A 102     133.803 125.850 127.591  1.00 38.00           C  
ATOM    323  CG2 VAL A 102     132.733 125.906 125.311  1.00 38.00           C  
ATOM    324  N   ASN A 103     131.897 129.230 128.573  1.00 37.84           N  
ATOM    325  CA  ASN A 103     132.006 129.963 129.833  1.00 37.84           C  
ATOM    326  C   ASN A 103     130.843 129.640 130.762  1.00 37.84           C  
ATOM    327  O   ASN A 103     131.035 129.463 131.971  1.00 37.84           O  
ATOM    328  CB  ASN A 103     132.068 131.469 129.559  1.00 37.84           C  
ATOM    329  CG  ASN A 103     132.388 132.290 130.808  1.00 37.84           C  
ATOM    330  OD1 ASN A 103     132.545 131.752 131.903  1.00 37.84           O  
ATOM    331  ND2 ASN A 103     132.477 133.605 130.640  1.00 37.84           N  
ATOM    332  N   ASN A 104     129.632 129.551 130.218  1.00 37.38           N  
ATOM    333  CA  ASN A 104     128.437 129.351 131.028  1.00 37.38           C  
ATOM    334  C   ASN A 104     128.187 127.891 131.381  1.00 37.38           C  
ATOM    335  O   ASN A 104     127.204 127.602 132.070  1.00 37.38           O  
ATOM    336  CB  ASN A 104     127.215 129.924 130.306  1.00 37.38           C  
ATOM    337  CG  ASN A 104     127.263 131.433 130.191  1.00 37.38           C  
ATOM    338  OD1 ASN A 104     127.786 132.118 131.070  1.00 37.38           O  
ATOM    339  ND2 ASN A 104     126.719 131.960 129.102  1.00 37.38           N  
ATOM    340  N   TYR A 105     129.037 126.968 130.925  1.00 35.66           N  
ATOM    341  CA  TYR A 105     128.878 125.568 131.306  1.00 35.66           C  
ATOM    342  C   TYR A 105     129.042 125.389 132.809  1.00 35.66           C  
ATOM    343  O   TYR A 105     128.322 124.599 133.431  1.00 35.66           O  
ATOM    344  CB  TYR A 105     129.883 124.696 130.553  1.00 35.66           C  
ATOM    345  CG  TYR A 105     129.589 124.521 129.079  1.00 35.66           C  
ATOM    346  CD1 TYR A 105     128.408 124.989 128.522  1.00 35.66           C  
ATOM    347  CD2 TYR A 105     130.497 123.882 128.246  1.00 35.66           C  
ATOM    348  CE1 TYR A 105     128.141 124.829 127.175  1.00 35.66           C  
ATOM    349  CE2 TYR A 105     130.239 123.718 126.899  1.00 35.66           C  
ATOM    350  CZ  TYR A 105     129.060 124.193 126.369  1.00 35.66           C  
ATOM    351  OH  TYR A 105     128.800 124.031 125.028  1.00 35.66           O  
ATOM    352  N   PHE A 106     129.993 126.109 133.408  1.00 33.16           N  
ATOM    353  CA  PHE A 106     130.194 126.027 134.851  1.00 33.16           C  
ATOM    354  C   PHE A 106     128.986 126.559 135.611  1.00 33.16           C  
ATOM    355  O   PHE A 106     128.608 126.005 136.650  1.00 33.16           O  
ATOM    356  CB  PHE A 106     131.458 126.790 135.244  1.00 33.16           C  
ATOM    357  CG  PHE A 106     132.646 126.476 134.381  1.00 33.16           C  
ATOM    358  CD1 PHE A 106     133.292 125.257 134.488  1.00 33.16           C  
ATOM    359  CD2 PHE A 106     133.112 127.397 133.460  1.00 33.16           C  
ATOM    360  CE1 PHE A 106     134.383 124.964 133.695  1.00 33.16           C  
ATOM    361  CE2 PHE A 106     134.203 127.109 132.663  1.00 33.16           C  
ATOM    362  CZ  PHE A 106     134.839 125.891 132.782  1.00 33.16           C  
ATOM    363  N   LEU A 107     128.376 127.639 135.118  1.00 33.11           N  
ATOM    364  CA  LEU A 107     127.172 128.164 135.755  1.00 33.11           C  
ATOM    365  C   LEU A 107     126.021 127.171 135.660  1.00 33.11           C  
ATOM    366  O   LEU A 107     125.243 127.021 136.610  1.00 33.11           O  
ATOM    367  CB  LEU A 107     126.784 129.501 135.125  1.00 33.11           C  
ATOM    368  CG  LEU A 107     127.809 130.629 135.249  1.00 33.11           C  
ATOM    369  CD1 LEU A 107     127.280 131.906 134.620  1.00 33.11           C  
ATOM    370  CD2 LEU A 107     128.181 130.858 136.704  1.00 33.11           C  
ATOM    371  N   LEU A 108     125.889 126.492 134.518  1.00 32.27           N  
ATOM    372  CA  LEU A 108     124.866 125.461 134.381  1.00 32.27           C  
ATOM    373  C   LEU A 108     125.124 124.302 135.335  1.00 32.27           C  
ATOM    374  O   LEU A 108     124.188 123.761 135.935  1.00 32.27           O  
ATOM    375  CB  LEU A 108     124.811 124.969 132.935  1.00 32.27           C  
ATOM    376  CG  LEU A 108     123.610 124.108 132.544  1.00 32.27           C  
ATOM    377  CD1 LEU A 108     122.320 124.901 132.660  1.00 32.27           C  
ATOM    378  CD2 LEU A 108     123.782 123.564 131.136  1.00 32.27           C  
ATOM    379  N   SER A 109     126.389 123.901 135.481  1.00 31.33           N  
ATOM    380  CA  SER A 109     126.729 122.847 136.431  1.00 31.33           C  
ATOM    381  C   SER A 109     126.486 123.298 137.866  1.00 31.33           C  
ATOM    382  O   SER A 109     126.051 122.503 138.708  1.00 31.33           O  
ATOM    383  CB  SER A 109     128.183 122.419 136.240  1.00 31.33           C  
ATOM    384  OG  SER A 109     128.644 121.660 137.343  1.00 31.33           O  
ATOM    385  N   LEU A 110     126.769 124.567 138.164  1.00 30.20           N  
ATOM    386  CA  LEU A 110     126.514 125.096 139.500  1.00 30.20           C  
ATOM    387  C   LEU A 110     125.022 125.109 139.813  1.00 30.20           C  
ATOM    388  O   LEU A 110     124.618 124.824 140.946  1.00 30.20           O  
ATOM    389  CB  LEU A 110     127.105 126.499 139.627  1.00 30.20           C  
ATOM    390  CG  LEU A 110     126.859 127.254 140.934  1.00 30.20           C  
ATOM    391  CD1 LEU A 110     127.598 126.592 142.084  1.00 30.20           C  
ATOM    392  CD2 LEU A 110     127.273 128.709 140.796  1.00 30.20           C  
ATOM    393  N   ALA A 111     124.190 125.441 138.823  1.00 32.41           N  
ATOM    394  CA  ALA A 111     122.749 125.475 139.044  1.00 32.41           C  
ATOM    395  C   ALA A 111     122.171 124.078 139.232  1.00 32.41           C  
ATOM    396  O   ALA A 111     121.181 123.913 139.953  1.00 32.41           O  
ATOM    397  CB  ALA A 111     122.054 126.183 137.882  1.00 32.41           C  
ATOM    398  N   CYS A 112     122.760 123.068 138.587  1.00 33.60           N  
ATOM    399  CA  CYS A 112     122.271 121.703 138.750  1.00 33.60           C  
ATOM    400  C   CYS A 112     122.453 121.218 140.183  1.00 33.60           C  
ATOM    401  O   CYS A 112     121.554 120.587 140.751  1.00 33.60           O  
ATOM    402  CB  CYS A 112     122.984 120.769 137.773  1.00 33.60           C  
ATOM    403  SG  CYS A 112     122.321 120.799 136.093  1.00 33.60           S  
ATOM    404  N   ALA A 113     123.612 121.498 140.781  1.00 32.46           N  
ATOM    405  CA  ALA A 113     123.839 121.116 142.171  1.00 32.46           C  
ATOM    406  C   ALA A 113     122.910 121.871 143.112  1.00 32.46           C  
ATOM    407  O   ALA A 113     122.376 121.290 144.064  1.00 32.46           O  
ATOM    408  CB  ALA A 113     125.299 121.358 142.551  1.00 32.46           C  
ATOM    409  N   ASP A 114     122.706 123.166 142.863  1.00 33.43           N  
ATOM    410  CA  ASP A 114     121.832 123.957 143.722  1.00 33.43           C  
ATOM    411  C   ASP A 114     120.371 123.551 143.570  1.00 33.43           C  
ATOM    412  O   ASP A 114     119.593 123.682 144.521  1.00 33.43           O  
ATOM    413  CB  ASP A 114     122.004 125.444 143.418  1.00 33.43           C  
ATOM    414  CG  ASP A 114     123.294 126.007 143.975  1.00 33.43           C  
ATOM    415  OD1 ASP A 114     123.800 125.461 144.977  1.00 33.43           O  
ATOM    416  OD2 ASP A 114     123.804 126.997 143.412  1.00 33.43           O  
ATOM    417  N   LEU A 115     119.980 123.072 142.387  1.00 32.74           N  
ATOM    418  CA  LEU A 115     118.612 122.601 142.195  1.00 32.74           C  
ATOM    419  C   LEU A 115     118.322 121.375 143.054  1.00 32.74           C  
ATOM    420  O   LEU A 115     117.237 121.260 143.635  1.00 32.74           O  
ATOM    421  CB  LEU A 115     118.366 122.293 140.719  1.00 32.74           C  
ATOM    422  CG  LEU A 115     116.921 121.994 140.321  1.00 32.74           C  
ATOM    423  CD1 LEU A 115     116.021 123.174 140.648  1.00 32.74           C  
ATOM    424  CD2 LEU A 115     116.835 121.642 138.846  1.00 32.74           C  
ATOM    425  N   ILE A 116     119.279 120.449 143.142  1.00 32.42           N  
ATOM    426  CA  ILE A 116     119.105 119.269 143.986  1.00 32.42           C  
ATOM    427  C   ILE A 116     118.974 119.677 145.447  1.00 32.42           C  
ATOM    428  O   ILE A 116     118.140 119.140 146.186  1.00 32.42           O  
ATOM    429  CB  ILE A 116     120.271 118.285 143.774  1.00 32.42           C  
ATOM    430  CG1 ILE A 116     120.307 117.805 142.322  1.00 32.42           C  
ATOM    431  CG2 ILE A 116     120.159 117.106 144.726  1.00 32.42           C  
ATOM    432  CD1 ILE A 116     121.661 117.300 141.883  1.00 32.42           C  
ATOM    433  N   ILE A 117     119.798 120.630 145.885  1.00 33.00           N  
ATOM    434  CA  ILE A 117     119.730 121.107 147.263  1.00 33.00           C  
ATOM    435  C   ILE A 117     118.376 121.748 147.542  1.00 33.00           C  
ATOM    436  O   ILE A 117     117.756 121.499 148.583  1.00 33.00           O  
ATOM    437  CB  ILE A 117     120.890 122.081 147.544  1.00 33.00           C  
ATOM    438  CG1 ILE A 117     122.199 121.312 147.726  1.00 33.00           C  
ATOM    439  CG2 ILE A 117     120.594 122.937 148.763  1.00 33.00           C  
ATOM    440  CD1 ILE A 117     123.435 122.155 147.510  1.00 33.00           C  
ATOM    441  N   GLY A 118     117.894 122.577 146.616  1.00 34.74           N  
ATOM    442  CA  GLY A 118     116.627 123.257 146.834  1.00 34.74           C  
ATOM    443  C   GLY A 118     115.440 122.314 146.868  1.00 34.74           C  
ATOM    444  O   GLY A 118     114.502 122.513 147.645  1.00 34.74           O  
ATOM    445  N   VAL A 119     115.461 121.276 146.034  1.00 34.76           N  
ATOM    446  CA  VAL A 119     114.306 120.392 145.916  1.00 34.76           C  
ATOM    447  C   VAL A 119     114.263 119.390 147.063  1.00 34.76           C  
ATOM    448  O   VAL A 119     113.253 119.273 147.765  1.00 34.76           O  
ATOM    449  CB  VAL A 119     114.315 119.682 144.549  1.00 34.76           C  
ATOM    450  CG1 VAL A 119     113.319 118.533 144.542  1.00 34.76           C  
ATOM    451  CG2 VAL A 119     114.004 120.668 143.437  1.00 34.76           C  
ATOM    452  N   ILE A 120     115.350 118.657 147.274  1.00 36.32           N  
ATOM    453  CA  ILE A 120     115.370 117.536 148.210  1.00 36.32           C  
ATOM    454  C   ILE A 120     115.976 117.927 149.550  1.00 36.32           C  
ATOM    455  O   ILE A 120     115.388 117.673 150.601  1.00 36.32           O  
ATOM    456  CB  ILE A 120     116.119 116.336 147.589  1.00 36.32           C  
ATOM    457  CG1 ILE A 120     115.612 116.064 146.173  1.00 36.32           C  
ATOM    458  CG2 ILE A 120     115.963 115.104 148.460  1.00 36.32           C  
ATOM    459  CD1 ILE A 120     116.539 115.196 145.352  1.00 36.32           C  
ATOM    460  N   SER A 121     117.161 118.540 149.532  1.00 35.70           N  
ATOM    461  CA  SER A 121     117.868 118.822 150.778  1.00 35.70           C  
ATOM    462  C   SER A 121     117.104 119.815 151.647  1.00 35.70           C  
ATOM    463  O   SER A 121     117.001 119.631 152.865  1.00 35.70           O  
ATOM    464  CB  SER A 121     119.271 119.345 150.476  1.00 35.70           C  
ATOM    465  OG  SER A 121     119.990 118.435 149.662  1.00 35.70           O  
ATOM    466  N   MET A 122     116.563 120.873 151.043  1.00 37.41           N  
ATOM    467  CA  MET A 122     115.877 121.900 151.816  1.00 37.41           C  
ATOM    468  C   MET A 122     114.493 121.468 152.282  1.00 37.41           C  
ATOM    469  O   MET A 122     113.956 122.071 153.217  1.00 37.41           O  
ATOM    470  CB  MET A 122     115.766 123.190 150.999  1.00 37.41           C  
ATOM    471  CG  MET A 122     117.103 123.856 150.722  1.00 37.41           C  
ATOM    472  SD  MET A 122     116.982 125.329 149.691  1.00 37.41           S  
ATOM    473  CE  MET A 122     116.194 126.473 150.816  1.00 37.41           C  
ATOM    474  N   ASN A 123     113.909 120.445 151.663  1.00 37.80           N  
ATOM    475  CA  ASN A 123     112.572 119.981 152.015  1.00 37.80           C  
ATOM    476  C   ASN A 123     112.592 118.818 152.999  1.00 37.80           C  
ATOM    477  O   ASN A 123     111.844 118.826 153.981  1.00 37.80           O  
ATOM    478  CB  ASN A 123     111.804 119.585 150.749  1.00 37.80           C  
ATOM    479  CG  ASN A 123     111.519 120.770 149.849  1.00 37.80           C  
ATOM    480  OD1 ASN A 123     111.379 121.899 150.318  1.00 37.80           O  
ATOM    481  ND2 ASN A 123     111.433 120.519 148.548  1.00 37.80           N  
ATOM    482  N   LEU A 124     113.433 117.811 152.755  1.00 38.54           N  
ATOM    483  CA  LEU A 124     113.520 116.684 153.677  1.00 38.54           C  
ATOM    484  C   LEU A 124     114.096 117.103 155.023  1.00 38.54           C  
ATOM    485  O   LEU A 124     113.820 116.460 156.041  1.00 38.54           O  
ATOM    486  CB  LEU A 124     114.357 115.563 153.064  1.00 38.54           C  
ATOM    487  CG  LEU A 124     113.585 114.529 152.244  1.00 38.54           C  
ATOM    488  CD1 LEU A 124     114.537 113.552 151.577  1.00 38.54           C  
ATOM    489  CD2 LEU A 124     112.587 113.795 153.121  1.00 38.54           C  
ATOM    490  N   PHE A 125     114.897 118.170 155.049  1.00 39.99           N  
ATOM    491  CA  PHE A 125     115.397 118.689 156.316  1.00 39.99           C  
ATOM    492  C   PHE A 125     114.301 119.399 157.100  1.00 39.99           C  
ATOM    493  O   PHE A 125     114.343 119.429 158.335  1.00 39.99           O  
ATOM    494  CB  PHE A 125     116.575 119.630 156.064  1.00 39.99           C  
ATOM    495  CG  PHE A 125     117.057 120.347 157.292  1.00 39.99           C  
ATOM    496  CD1 PHE A 125     117.760 119.671 158.274  1.00 39.99           C  
ATOM    497  CD2 PHE A 125     116.813 121.699 157.460  1.00 39.99           C  
ATOM    498  CE1 PHE A 125     118.204 120.328 159.403  1.00 39.99           C  
ATOM    499  CE2 PHE A 125     117.254 122.362 158.586  1.00 39.99           C  
ATOM    500  CZ  PHE A 125     117.953 121.676 159.558  1.00 39.99           C  
ATOM    501  N   THR A 126     113.321 119.978 156.402  1.00 42.91           N  
ATOM    502  CA  THR A 126     112.227 120.669 157.077  1.00 42.91           C  
ATOM    503  C   THR A 126     111.337 119.690 157.824  1.00 42.91           C  
ATOM    504  O   THR A 126     110.888 119.972 158.941  1.00 42.91           O  
ATOM    505  CB  THR A 126     111.409 121.457 156.061  1.00 42.91           C  
ATOM    506  OG1 THR A 126     112.290 122.263 155.275  1.00 42.91           O  
ATOM    507  CG2 THR A 126     110.402 122.350 156.764  1.00 42.91           C  
ATOM    508  N   THR A 127     111.069 118.535 157.217  1.00 43.95           N  
ATOM    509  CA  THR A 127     110.303 117.501 157.893  1.00 43.95           C  
ATOM    510  C   THR A 127     111.034 116.997 159.133  1.00 43.95           C  
ATOM    511  O   THR A 127     110.398 116.582 160.106  1.00 43.95           O  
ATOM    512  CB  THR A 127     110.014 116.370 156.906  1.00 43.95           C  
ATOM    513  OG1 THR A 127     109.304 116.902 155.781  1.00 43.95           O  
ATOM    514  CG2 THR A 127     109.166 115.304 157.537  1.00 43.95           C  
ATOM    515  N   TYR A 128     112.368 117.061 159.130  1.00 45.28           N  
ATOM    516  CA  TYR A 128     113.149 116.682 160.302  1.00 45.28           C  
ATOM    517  C   TYR A 128     113.058 117.711 161.424  1.00 45.28           C  
ATOM    518  O   TYR A 128     113.329 117.372 162.580  1.00 45.28           O  
ATOM    519  CB  TYR A 128     114.611 116.470 159.901  1.00 45.28           C  
ATOM    520  CG  TYR A 128     115.475 115.862 160.981  1.00 45.28           C  
ATOM    521  CD1 TYR A 128     114.988 114.855 161.803  1.00 45.28           C  
ATOM    522  CD2 TYR A 128     116.780 116.292 161.176  1.00 45.28           C  
ATOM    523  CE1 TYR A 128     115.775 114.297 162.790  1.00 45.28           C  
ATOM    524  CE2 TYR A 128     117.574 115.739 162.160  1.00 45.28           C  
ATOM    525  CZ  TYR A 128     117.067 114.743 162.963  1.00 45.28           C  
ATOM    526  OH  TYR A 128     117.857 114.191 163.944  1.00 45.28           O  
ATOM    527  N   ILE A 129     112.677 118.952 161.117  1.00 46.55           N  
ATOM    528  CA  ILE A 129     112.640 120.017 162.116  1.00 46.55           C  
ATOM    529  C   ILE A 129     111.271 120.085 162.779  1.00 46.55           C  
ATOM    530  O   ILE A 129     111.154 119.923 163.999  1.00 46.55           O  
ATOM    531  CB  ILE A 129     113.007 121.375 161.492  1.00 46.55           C  
ATOM    532  CG1 ILE A 129     114.435 121.340 160.951  1.00 46.55           C  
ATOM    533  CG2 ILE A 129     112.842 122.493 162.510  1.00 46.55           C  
ATOM    534  CD1 ILE A 129     115.487 121.454 162.025  1.00 46.55           C  
ATOM    535  N   ILE A 130     110.230 120.337 161.981  1.00 54.03           N  
ATOM    536  CA  ILE A 130     108.877 120.446 162.523  1.00 54.03           C  
ATOM    537  C   ILE A 130     108.461 119.136 163.175  1.00 54.03           C  
ATOM    538  O   ILE A 130     107.967 119.110 164.308  1.00 54.03           O  
ATOM    539  CB  ILE A 130     107.890 120.850 161.415  1.00 54.03           C  
ATOM    540  CG1 ILE A 130     108.268 122.212 160.839  1.00 54.03           C  
ATOM    541  CG2 ILE A 130     106.467 120.861 161.953  1.00 54.03           C  
ATOM    542  CD1 ILE A 130     107.556 122.523 159.566  1.00 54.03           C  
ATOM    543  N   MET A 131     108.645 118.032 162.460  1.00 54.53           N  
ATOM    544  CA  MET A 131     108.461 116.692 163.005  1.00 54.53           C  
ATOM    545  C   MET A 131     109.800 116.284 163.603  1.00 54.53           C  
ATOM    546  O   MET A 131     110.729 115.911 162.882  1.00 54.53           O  
ATOM    547  CB  MET A 131     107.995 115.738 161.913  1.00 54.53           C  
ATOM    548  CG  MET A 131     107.721 114.330 162.369  1.00 54.53           C  
ATOM    549  SD  MET A 131     107.155 113.305 161.007  1.00 54.53           S  
ATOM    550  CE  MET A 131     108.679 113.143 160.097  1.00 54.53           C  
ATOM    551  N   ASN A 132     109.900 116.356 164.930  1.00 54.77           N  
ATOM    552  CA  ASN A 132     111.192 116.300 165.602  1.00 54.77           C  
ATOM    553  C   ASN A 132     111.692 114.867 165.748  1.00 54.77           C  
ATOM    554  O   ASN A 132     112.078 114.452 166.846  1.00 54.77           O  
ATOM    555  CB  ASN A 132     111.092 116.978 166.975  1.00 54.77           C  
ATOM    556  CG  ASN A 132     112.445 117.147 167.655  1.00 54.77           C  
ATOM    557  OD1 ASN A 132     113.479 116.737 167.127  1.00 54.77           O  
ATOM    558  ND2 ASN A 132     112.438 117.756 168.834  1.00 54.77           N  
ATOM    559  N   ARG A 133     111.696 114.114 164.645  1.00 53.41           N  
ATOM    560  CA  ARG A 133     112.325 112.798 164.569  1.00 53.41           C  
ATOM    561  C   ARG A 133     112.239 112.261 163.144  1.00 53.41           C  
ATOM    562  O   ARG A 133     111.315 112.600 162.398  1.00 53.41           O  
ATOM    563  CB  ARG A 133     111.700 111.814 165.572  1.00 53.41           C  
ATOM    564  CG  ARG A 133     110.399 111.148 165.163  1.00 53.41           C  
ATOM    565  CD  ARG A 133     109.229 112.116 165.133  1.00 53.41           C  
ATOM    566  NE  ARG A 133     107.978 111.436 164.835  1.00 53.41           N  
ATOM    567  CZ  ARG A 133     107.619 111.065 163.618  1.00 53.41           C  
ATOM    568  NH1 ARG A 133     108.431 111.216 162.591  1.00 53.41           N  
ATOM    569  NH2 ARG A 133     106.418 110.526 163.429  1.00 53.41           N  
ATOM    570  N   TRP A 134     113.212 111.444 162.752  1.00 46.34           N  
ATOM    571  CA  TRP A 134     113.202 110.852 161.423  1.00 46.34           C  
ATOM    572  C   TRP A 134     112.133 109.768 161.331  1.00 46.34           C  
ATOM    573  O   TRP A 134     111.989 108.938 162.233  1.00 46.34           O  
ATOM    574  CB  TRP A 134     114.580 110.275 161.099  1.00 46.34           C  
ATOM    575  CG  TRP A 134     114.798 110.027 159.647  1.00 46.34           C  
ATOM    576  CD1 TRP A 134     114.908 108.816 159.035  1.00 46.34           C  
ATOM    577  CD2 TRP A 134     114.933 111.013 158.617  1.00 46.34           C  
ATOM    578  NE1 TRP A 134     115.101 108.984 157.687  1.00 46.34           N  
ATOM    579  CE2 TRP A 134     115.121 110.324 157.404  1.00 46.34           C  
ATOM    580  CE3 TRP A 134     114.913 112.411 158.603  1.00 46.34           C  
ATOM    581  CZ2 TRP A 134     115.288 110.984 156.189  1.00 46.34           C  
ATOM    582  CZ3 TRP A 134     115.080 113.063 157.397  1.00 46.34           C  
ATOM    583  CH2 TRP A 134     115.265 112.350 156.207  1.00 46.34           C  
ATOM    584  N   ALA A 135     111.378 109.779 160.233  1.00 47.66           N  
ATOM    585  CA  ALA A 135     110.299 108.822 159.988  1.00 47.66           C  
ATOM    586  C   ALA A 135     110.380 108.264 158.578  1.00 47.66           C  
ATOM    587  O   ALA A 135     109.391 108.216 157.845  1.00 47.66           O  
ATOM    588  CB  ALA A 135     108.926 109.443 160.193  1.00 47.66           C  
ATOM    589  N   LEU A 136     111.568 107.834 158.170  1.00 46.96           N  
ATOM    590  CA  LEU A 136     111.737 107.242 156.853  1.00 46.96           C  
ATOM    591  C   LEU A 136     112.462 105.908 156.862  1.00 46.96           C  
ATOM    592  O   LEU A 136     112.322 105.151 155.894  1.00 46.96           O  
ATOM    593  CB  LEU A 136     112.480 108.209 155.921  1.00 46.96           C  
ATOM    594  N   GLY A 137     113.211 105.587 157.905  1.00 46.26           N  
ATOM    595  CA  GLY A 137     113.912 104.324 158.004  1.00 46.26           C  
ATOM    596  C   GLY A 137     115.414 104.494 157.857  1.00 46.26           C  
ATOM    597  O   GLY A 137     115.926 105.549 157.483  1.00 46.26           O  
ATOM    598  N   ASN A 138     116.122 103.407 158.171  1.00 48.77           N  
ATOM    599  CA  ASN A 138     117.579 103.429 158.110  1.00 48.77           C  
ATOM    600  C   ASN A 138     118.067 103.592 156.676  1.00 48.77           C  
ATOM    601  O   ASN A 138     118.896 104.462 156.387  1.00 48.77           O  
ATOM    602  CB  ASN A 138     118.149 102.155 158.734  1.00 48.77           C  
ATOM    603  CG  ASN A 138     117.868 102.061 160.217  1.00 48.77           C  
ATOM    604  OD1 ASN A 138     117.216 102.931 160.794  1.00 48.77           O  
ATOM    605  ND2 ASN A 138     118.361 101.001 160.846  1.00 48.77           N  
ATOM    606  N   LEU A 139     117.562 102.768 155.761  1.00 51.44           N  
ATOM    607  CA  LEU A 139     117.946 102.890 154.354  1.00 51.44           C  
ATOM    608  C   LEU A 139     117.016 103.843 153.612  1.00 51.44           C  
ATOM    609  O   LEU A 139     116.524 103.562 152.520  1.00 51.44           O  
ATOM    610  CB  LEU A 139     117.962 101.515 153.695  1.00 51.44           C  
ATOM    611  CG  LEU A 139     119.220 100.661 153.879  1.00 51.44           C  
ATOM    612  CD1 LEU A 139     120.424 101.330 153.231  1.00 51.44           C  
ATOM    613  CD2 LEU A 139     119.487 100.368 155.351  1.00 51.44           C  
ATOM    614  N   ALA A 140     116.774 104.996 154.232  1.00 45.95           N  
ATOM    615  CA  ALA A 140     116.149 106.137 153.573  1.00 45.95           C  
ATOM    616  C   ALA A 140     116.776 107.466 153.951  1.00 45.95           C  
ATOM    617  O   ALA A 140     116.536 108.457 153.254  1.00 45.95           O  
ATOM    618  CB  ALA A 140     114.649 106.189 153.883  1.00 45.95           C  
ATOM    619  N   CYS A 141     117.566 107.530 155.022  1.00 45.71           N  
ATOM    620  CA  CYS A 141     118.287 108.733 155.409  1.00 45.71           C  
ATOM    621  C   CYS A 141     119.737 108.718 154.962  1.00 45.71           C  
ATOM    622  O   CYS A 141     120.319 109.785 154.747  1.00 45.71           O  
ATOM    623  CB  CYS A 141     118.239 108.917 156.928  1.00 45.71           C  
ATOM    624  SG  CYS A 141     118.533 110.608 157.477  1.00 45.71           S  
ATOM    625  N   ASP A 142     120.334 107.532 154.828  1.00 41.69           N  
ATOM    626  CA  ASP A 142     121.661 107.441 154.233  1.00 41.69           C  
ATOM    627  C   ASP A 142     121.642 107.951 152.800  1.00 41.69           C  
ATOM    628  O   ASP A 142     122.597 108.590 152.346  1.00 41.69           O  
ATOM    629  CB  ASP A 142     122.163 105.999 154.290  1.00 41.69           C  
ATOM    630  CG  ASP A 142     122.154 105.434 155.695  1.00 41.69           C  
ATOM    631  OD1 ASP A 142     122.016 106.224 156.653  1.00 41.69           O  
ATOM    632  OD2 ASP A 142     122.285 104.201 155.843  1.00 41.69           O  
ATOM    633  N   LEU A 143     120.557 107.675 152.072  1.00 40.22           N  
ATOM    634  CA  LEU A 143     120.386 108.254 150.745  1.00 40.22           C  
ATOM    635  C   LEU A 143     120.283 109.772 150.821  1.00 40.22           C  
ATOM    636  O   LEU A 143     120.872 110.484 149.999  1.00 40.22           O  
ATOM    637  CB  LEU A 143     119.144 107.669 150.070  1.00 40.22           C  
ATOM    638  CG  LEU A 143     119.278 106.354 149.295  1.00 40.22           C  
ATOM    639  CD1 LEU A 143     120.287 106.492 148.166  1.00 40.22           C  
ATOM    640  CD2 LEU A 143     119.642 105.195 150.213  1.00 40.22           C  
ATOM    641  N   TRP A 144     119.536 110.287 151.800  1.00 37.03           N  
ATOM    642  CA  TRP A 144     119.392 111.732 151.943  1.00 37.03           C  
ATOM    643  C   TRP A 144     120.715 112.383 152.325  1.00 37.03           C  
ATOM    644  O   TRP A 144     121.095 113.416 151.763  1.00 37.03           O  
ATOM    645  CB  TRP A 144     118.317 112.056 152.979  1.00 37.03           C  
ATOM    646  CG  TRP A 144     118.196 113.521 153.271  1.00 37.03           C  
ATOM    647  CD1 TRP A 144     117.866 114.507 152.389  1.00 37.03           C  
ATOM    648  CD2 TRP A 144     118.408 114.167 154.532  1.00 37.03           C  
ATOM    649  NE1 TRP A 144     117.858 115.725 153.021  1.00 37.03           N  
ATOM    650  CE2 TRP A 144     118.188 115.544 154.338  1.00 37.03           C  
ATOM    651  CE3 TRP A 144     118.764 113.714 155.806  1.00 37.03           C  
ATOM    652  CZ2 TRP A 144     118.310 116.472 155.369  1.00 37.03           C  
ATOM    653  CZ3 TRP A 144     118.884 114.637 156.828  1.00 37.03           C  
ATOM    654  CH2 TRP A 144     118.657 116.000 156.604  1.00 37.03           C  
ATOM    655  N   LEU A 145     121.430 111.795 153.287  1.00 35.22           N  
ATOM    656  CA  LEU A 145     122.709 112.360 153.706  1.00 35.22           C  
ATOM    657  C   LEU A 145     123.732 112.312 152.580  1.00 35.22           C  
ATOM    658  O   LEU A 145     124.489 113.267 152.379  1.00 35.22           O  
ATOM    659  CB  LEU A 145     123.235 111.620 154.935  1.00 35.22           C  
ATOM    660  CG  LEU A 145     122.438 111.768 156.230  1.00 35.22           C  
ATOM    661  CD1 LEU A 145     122.993 110.835 157.289  1.00 35.22           C  
ATOM    662  CD2 LEU A 145     122.455 113.207 156.714  1.00 35.22           C  
ATOM    663  N   ALA A 146     123.776 111.203 151.839  1.00 32.48           N  
ATOM    664  CA  ALA A 146     124.720 111.091 150.733  1.00 32.48           C  
ATOM    665  C   ALA A 146     124.403 112.094 149.632  1.00 32.48           C  
ATOM    666  O   ALA A 146     125.303 112.759 149.108  1.00 32.48           O  
ATOM    667  CB  ALA A 146     124.716 109.665 150.181  1.00 32.48           C  
ATOM    668  N   ILE A 147     123.125 112.219 149.268  1.00 32.37           N  
ATOM    669  CA  ILE A 147     122.742 113.135 148.197  1.00 32.37           C  
ATOM    670  C   ILE A 147     122.970 114.581 148.622  1.00 32.37           C  
ATOM    671  O   ILE A 147     123.522 115.388 147.865  1.00 32.37           O  
ATOM    672  CB  ILE A 147     121.280 112.891 147.781  1.00 32.37           C  
ATOM    673  CG1 ILE A 147     121.165 111.601 146.968  1.00 32.37           C  
ATOM    674  CG2 ILE A 147     120.743 114.068 146.983  1.00 32.37           C  
ATOM    675  CD1 ILE A 147     119.751 111.074 146.858  1.00 32.37           C  
ATOM    676  N   ASP A 148     122.551 114.927 149.841  1.00 32.74           N  
ATOM    677  CA  ASP A 148     122.685 116.303 150.312  1.00 32.74           C  
ATOM    678  C   ASP A 148     124.148 116.710 150.446  1.00 32.74           C  
ATOM    679  O   ASP A 148     124.524 117.823 150.063  1.00 32.74           O  
ATOM    680  CB  ASP A 148     121.950 116.469 151.643  1.00 32.74           C  
ATOM    681  CG  ASP A 148     122.111 117.854 152.235  1.00 32.74           C  
ATOM    682  OD1 ASP A 148     122.277 118.824 151.466  1.00 32.74           O  
ATOM    683  OD2 ASP A 148     122.063 117.974 153.476  1.00 32.74           O  
ATOM    684  N   TYR A 149     124.988 115.826 150.984  1.00 32.16           N  
ATOM    685  CA  TYR A 149     126.385 116.185 151.207  1.00 32.16           C  
ATOM    686  C   TYR A 149     127.170 116.222 149.902  1.00 32.16           C  
ATOM    687  O   TYR A 149     128.052 117.069 149.728  1.00 32.16           O  
ATOM    688  CB  TYR A 149     127.024 115.216 152.199  1.00 32.16           C  
ATOM    689  CG  TYR A 149     126.907 115.669 153.636  1.00 32.16           C  
ATOM    690  CD1 TYR A 149     125.688 115.634 154.298  1.00 32.16           C  
ATOM    691  CD2 TYR A 149     128.014 116.135 154.329  1.00 32.16           C  
ATOM    692  CE1 TYR A 149     125.576 116.052 155.609  1.00 32.16           C  
ATOM    693  CE2 TYR A 149     127.913 116.552 155.639  1.00 32.16           C  
ATOM    694  CZ  TYR A 149     126.693 116.508 156.275  1.00 32.16           C  
ATOM    695  OH  TYR A 149     126.590 116.922 157.582  1.00 32.16           O  
ATOM    696  N   VAL A 150     126.873 115.308 148.976  1.00 29.95           N  
ATOM    697  CA  VAL A 150     127.547 115.327 147.681  1.00 29.95           C  
ATOM    698  C   VAL A 150     127.152 116.569 146.891  1.00 29.95           C  
ATOM    699  O   VAL A 150     128.005 117.245 146.304  1.00 29.95           O  
ATOM    700  CB  VAL A 150     127.247 114.034 146.900  1.00 29.95           C  
ATOM    701  CG1 VAL A 150     127.527 114.224 145.418  1.00 29.95           C  
ATOM    702  CG2 VAL A 150     128.066 112.880 147.454  1.00 29.95           C  
ATOM    703  N   ALA A 151     125.857 116.893 146.865  1.00 29.32           N  
ATOM    704  CA  ALA A 151     125.402 118.075 146.140  1.00 29.32           C  
ATOM    705  C   ALA A 151     125.955 119.353 146.758  1.00 29.32           C  
ATOM    706  O   ALA A 151     126.349 120.276 146.036  1.00 29.32           O  
ATOM    707  CB  ALA A 151     123.875 118.114 146.100  1.00 29.32           C  
ATOM    708  N   SER A 152     125.985 119.430 148.090  1.00 30.60           N  
ATOM    709  CA  SER A 152     126.552 120.601 148.749  1.00 30.60           C  
ATOM    710  C   SER A 152     128.041 120.730 148.455  1.00 30.60           C  
ATOM    711  O   SER A 152     128.549 121.839 148.256  1.00 30.60           O  
ATOM    712  CB  SER A 152     126.304 120.529 150.255  1.00 30.60           C  
ATOM    713  OG  SER A 152     124.931 120.707 150.552  1.00 30.60           O  
ATOM    714  N   ASN A 153     128.757 119.605 148.433  1.00 30.52           N  
ATOM    715  CA  ASN A 153     130.165 119.631 148.052  1.00 30.52           C  
ATOM    716  C   ASN A 153     130.331 120.015 146.588  1.00 30.52           C  
ATOM    717  O   ASN A 153     131.284 120.715 146.229  1.00 30.52           O  
ATOM    718  CB  ASN A 153     130.809 118.273 148.328  1.00 30.52           C  
ATOM    719  CG  ASN A 153     132.295 118.378 148.592  1.00 30.52           C  
ATOM    720  OD1 ASN A 153     132.716 118.836 149.651  1.00 30.52           O  
ATOM    721  ND2 ASN A 153     133.100 117.954 147.628  1.00 30.52           N  
ATOM    722  N   ALA A 154     129.416 119.562 145.728  1.00 30.82           N  
ATOM    723  CA  ALA A 154     129.512 119.875 144.306  1.00 30.82           C  
ATOM    724  C   ALA A 154     129.369 121.371 144.055  1.00 30.82           C  
ATOM    725  O   ALA A 154     130.060 121.931 143.196  1.00 30.82           O  
ATOM    726  CB  ALA A 154     128.456 119.095 143.524  1.00 30.82           C  
ATOM    727  N   SER A 155     128.469 122.034 144.787  1.00 30.53           N  
ATOM    728  CA  SER A 155     128.301 123.475 144.621  1.00 30.53           C  
ATOM    729  C   SER A 155     129.572 124.226 144.990  1.00 30.53           C  
ATOM    730  O   SER A 155     129.986 125.148 144.279  1.00 30.53           O  
ATOM    731  CB  SER A 155     127.126 123.970 145.464  1.00 30.53           C  
ATOM    732  OG  SER A 155     125.897 123.455 144.986  1.00 30.53           O  
ATOM    733  N   VAL A 156     130.207 123.845 146.099  1.00 29.16           N  
ATOM    734  CA  VAL A 156     131.444 124.499 146.512  1.00 29.16           C  
ATOM    735  C   VAL A 156     132.565 124.196 145.527  1.00 29.16           C  
ATOM    736  O   VAL A 156     133.362 125.076 145.182  1.00 29.16           O  
ATOM    737  CB  VAL A 156     131.810 124.079 147.946  1.00 29.16           C  
ATOM    738  CG1 VAL A 156     133.151 124.668 148.352  1.00 29.16           C  
ATOM    739  CG2 VAL A 156     130.719 124.511 148.909  1.00 29.16           C  
ATOM    740  N   MET A 157     132.648 122.948 145.059  1.00 31.20           N  
ATOM    741  CA  MET A 157     133.655 122.595 144.066  1.00 31.20           C  
ATOM    742  C   MET A 157     133.413 123.310 142.742  1.00 31.20           C  
ATOM    743  O   MET A 157     134.372 123.645 142.038  1.00 31.20           O  
ATOM    744  CB  MET A 157     133.678 121.082 143.859  1.00 31.20           C  
ATOM    745  CG  MET A 157     134.228 120.308 145.043  1.00 31.20           C  
ATOM    746  SD  MET A 157     136.006 120.513 145.220  1.00 31.20           S  
ATOM    747  CE  MET A 157     136.564 119.784 143.685  1.00 31.20           C  
ATOM    748  N   ASN A 158     132.148 123.541 142.383  1.00 30.10           N  
ATOM    749  CA  ASN A 158     131.851 124.310 141.179  1.00 30.10           C  
ATOM    750  C   ASN A 158     132.322 125.752 141.316  1.00 30.10           C  
ATOM    751  O   ASN A 158     132.831 126.338 140.353  1.00 30.10           O  
ATOM    752  CB  ASN A 158     130.353 124.259 140.879  1.00 30.10           C  
ATOM    753  CG  ASN A 158     129.990 123.145 139.919  1.00 30.10           C  
ATOM    754  OD1 ASN A 158     130.277 123.220 138.726  1.00 30.10           O  
ATOM    755  ND2 ASN A 158     129.356 122.101 140.438  1.00 30.10           N  
ATOM    756  N   LEU A 159     132.156 126.343 142.502  1.00 29.70           N  
ATOM    757  CA  LEU A 159     132.648 127.698 142.731  1.00 29.70           C  
ATOM    758  C   LEU A 159     134.165 127.760 142.614  1.00 29.70           C  
ATOM    759  O   LEU A 159     134.715 128.734 142.089  1.00 29.70           O  
ATOM    760  CB  LEU A 159     132.198 128.199 144.103  1.00 29.70           C  
ATOM    761  CG  LEU A 159     130.691 128.281 144.347  1.00 29.70           C  
ATOM    762  CD1 LEU A 159     130.399 128.819 145.738  1.00 29.70           C  
ATOM    763  CD2 LEU A 159     130.022 129.134 143.286  1.00 29.70           C  
ATOM    764  N   LEU A 160     134.858 126.734 143.114  1.00 29.54           N  
ATOM    765  CA  LEU A 160     136.311 126.687 142.987  1.00 29.54           C  
ATOM    766  C   LEU A 160     136.734 126.647 141.524  1.00 29.54           C  
ATOM    767  O   LEU A 160     137.687 127.326 141.125  1.00 29.54           O  
ATOM    768  CB  LEU A 160     136.862 125.476 143.740  1.00 29.54           C  
ATOM    769  CG  LEU A 160     138.354 125.490 144.072  1.00 29.54           C  
ATOM    770  CD1 LEU A 160     138.710 126.728 144.874  1.00 29.54           C  
ATOM    771  CD2 LEU A 160     138.746 124.230 144.825  1.00 29.54           C  
ATOM    772  N   VAL A 161     136.037 125.852 140.710  1.00 29.86           N  
ATOM    773  CA  VAL A 161     136.329 125.804 139.281  1.00 29.86           C  
ATOM    774  C   VAL A 161     135.975 127.130 138.620  1.00 29.86           C  
ATOM    775  O   VAL A 161     136.681 127.600 137.720  1.00 29.86           O  
ATOM    776  CB  VAL A 161     135.586 124.620 138.633  1.00 29.86           C  
ATOM    777  CG1 VAL A 161     135.680 124.684 137.118  1.00 29.86           C  
ATOM    778  CG2 VAL A 161     136.143 123.301 139.149  1.00 29.86           C  
ATOM    779  N   ILE A 162     134.880 127.758 139.057  1.00 28.39           N  
ATOM    780  CA  ILE A 162     134.485 129.051 138.502  1.00 28.39           C  
ATOM    781  C   ILE A 162     135.535 130.110 138.811  1.00 28.39           C  
ATOM    782  O   ILE A 162     135.898 130.918 137.948  1.00 28.39           O  
ATOM    783  CB  ILE A 162     133.095 129.455 139.030  1.00 28.39           C  
ATOM    784  CG1 ILE A 162     131.996 128.747 138.238  1.00 28.39           C  
ATOM    785  CG2 ILE A 162     132.906 130.963 138.965  1.00 28.39           C  
ATOM    786  CD1 ILE A 162     130.641 128.789 138.905  1.00 28.39           C  
ATOM    787  N   SER A 163     136.042 130.123 140.046  1.00 28.50           N  
ATOM    788  CA  SER A 163     137.059 131.101 140.421  1.00 28.50           C  
ATOM    789  C   SER A 163     138.336 130.910 139.613  1.00 28.50           C  
ATOM    790  O   SER A 163     138.975 131.888 139.208  1.00 28.50           O  
ATOM    791  CB  SER A 163     137.349 131.009 141.918  1.00 28.50           C  
ATOM    792  OG  SER A 163     138.167 129.891 142.211  1.00 28.50           O  
ATOM    793  N   PHE A 164     138.733 129.657 139.379  1.00 28.79           N  
ATOM    794  CA  PHE A 164     139.902 129.396 138.544  1.00 28.79           C  
ATOM    795  C   PHE A 164     139.665 129.833 137.105  1.00 28.79           C  
ATOM    796  O   PHE A 164     140.550 130.424 136.477  1.00 28.79           O  
ATOM    797  CB  PHE A 164     140.271 127.915 138.602  1.00 28.79           C  
ATOM    798  CG  PHE A 164     141.299 127.590 139.644  1.00 28.79           C  
ATOM    799  CD1 PHE A 164     142.621 127.961 139.471  1.00 28.79           C  
ATOM    800  CD2 PHE A 164     140.942 126.920 140.800  1.00 28.79           C  
ATOM    801  CE1 PHE A 164     143.568 127.667 140.431  1.00 28.79           C  
ATOM    802  CE2 PHE A 164     141.884 126.624 141.762  1.00 28.79           C  
ATOM    803  CZ  PHE A 164     143.198 126.996 141.578  1.00 28.79           C  
ATOM    804  N   ASP A 165     138.478 129.551 136.564  1.00 30.84           N  
ATOM    805  CA  ASP A 165     138.166 129.977 135.204  1.00 30.84           C  
ATOM    806  C   ASP A 165     138.168 131.495 135.088  1.00 30.84           C  
ATOM    807  O   ASP A 165     138.658 132.050 134.098  1.00 30.84           O  
ATOM    808  CB  ASP A 165     136.817 129.405 134.771  1.00 30.84           C  
ATOM    809  CG  ASP A 165     136.658 129.366 133.267  1.00 30.84           C  
ATOM    810  OD1 ASP A 165     137.276 128.492 132.625  1.00 30.84           O  
ATOM    811  OD2 ASP A 165     135.916 130.211 132.724  1.00 30.84           O  
ATOM    812  N   ARG A 166     137.615 132.184 136.089  1.00 29.18           N  
ATOM    813  CA  ARG A 166     137.655 133.642 136.097  1.00 29.18           C  
ATOM    814  C   ARG A 166     139.083 134.155 136.228  1.00 29.18           C  
ATOM    815  O   ARG A 166     139.454 135.142 135.584  1.00 29.18           O  
ATOM    816  CB  ARG A 166     136.788 134.186 137.231  1.00 29.18           C  
ATOM    817  CG  ARG A 166     135.353 134.475 136.837  1.00 29.18           C  
ATOM    818  CD  ARG A 166     134.472 134.640 138.062  1.00 29.18           C  
ATOM    819  NE  ARG A 166     133.062 134.745 137.709  1.00 29.18           N  
ATOM    820  CZ  ARG A 166     132.187 135.513 138.343  1.00 29.18           C  
ATOM    821  NH1 ARG A 166     132.545 136.263 139.372  1.00 29.18           N  
ATOM    822  NH2 ARG A 166     130.922 135.529 137.935  1.00 29.18           N  
ATOM    823  N   TYR A 167     139.894 133.501 137.062  1.00 27.41           N  
ATOM    824  CA  TYR A 167     141.253 133.972 137.306  1.00 27.41           C  
ATOM    825  C   TYR A 167     142.097 133.916 136.039  1.00 27.41           C  
ATOM    826  O   TYR A 167     142.776 134.888 135.688  1.00 27.41           O  
ATOM    827  CB  TYR A 167     141.899 133.147 138.418  1.00 27.41           C  
ATOM    828  CG  TYR A 167     143.368 133.438 138.617  1.00 27.41           C  
ATOM    829  CD1 TYR A 167     143.787 134.634 139.182  1.00 27.41           C  
ATOM    830  CD2 TYR A 167     144.335 132.521 138.233  1.00 27.41           C  
ATOM    831  CE1 TYR A 167     145.127 134.906 139.364  1.00 27.41           C  
ATOM    832  CE2 TYR A 167     145.678 132.785 138.411  1.00 27.41           C  
ATOM    833  CZ  TYR A 167     146.068 133.978 138.976  1.00 27.41           C  
ATOM    834  OH  TYR A 167     147.405 134.245 139.155  1.00 27.41           O  
ATOM    835  N   PHE A 168     142.068 132.782 135.338  1.00 27.05           N  
ATOM    836  CA  PHE A 168     142.868 132.637 134.128  1.00 27.05           C  
ATOM    837  C   PHE A 168     142.354 133.501 132.983  1.00 27.05           C  
ATOM    838  O   PHE A 168     143.115 133.793 132.055  1.00 27.05           O  
ATOM    839  CB  PHE A 168     142.909 131.171 133.698  1.00 27.05           C  
ATOM    840  CG  PHE A 168     143.734 130.296 134.599  1.00 27.05           C  
ATOM    841  CD1 PHE A 168     145.099 130.484 134.706  1.00 27.05           C  
ATOM    842  CD2 PHE A 168     143.144 129.281 135.330  1.00 27.05           C  
ATOM    843  CE1 PHE A 168     145.860 129.680 135.531  1.00 27.05           C  
ATOM    844  CE2 PHE A 168     143.900 128.475 136.157  1.00 27.05           C  
ATOM    845  CZ  PHE A 168     145.259 128.675 136.257  1.00 27.05           C  
ATOM    846  N   SER A 169     141.087 133.911 133.023  1.00 27.58           N  
ATOM    847  CA  SER A 169     140.539 134.800 132.009  1.00 27.58           C  
ATOM    848  C   SER A 169     140.940 136.254 132.218  1.00 27.58           C  
ATOM    849  O   SER A 169     140.776 137.063 131.299  1.00 27.58           O  
ATOM    850  CB  SER A 169     139.013 134.691 131.983  1.00 27.58           C  
ATOM    851  OG  SER A 169     138.598 133.491 131.356  1.00 27.58           O  
ATOM    852  N   ILE A 170     141.453 136.603 133.394  1.00 27.62           N  
ATOM    853  CA  ILE A 170     141.903 137.957 133.682  1.00 27.62           C  
ATOM    854  C   ILE A 170     143.412 138.090 133.520  1.00 27.62           C  
ATOM    855  O   ILE A 170     143.897 139.099 133.007  1.00 27.62           O  
ATOM    856  CB  ILE A 170     141.454 138.376 135.099  1.00 27.62           C  
ATOM    857  CG1 ILE A 170     139.933 138.300 135.224  1.00 27.62           C  
ATOM    858  CG2 ILE A 170     141.940 139.779 135.430  1.00 27.62           C  
ATOM    859  CD1 ILE A 170     139.199 139.246 134.311  1.00 27.62           C  
ATOM    860  N   THR A 171     144.167 137.079 133.953  1.00 28.00           N  
ATOM    861  CA  THR A 171     145.617 137.117 133.817  1.00 28.00           C  
ATOM    862  C   THR A 171     146.074 136.729 132.417  1.00 28.00           C  
ATOM    863  O   THR A 171     147.152 137.150 131.984  1.00 28.00           O  
ATOM    864  CB  THR A 171     146.269 136.194 134.847  1.00 28.00           C  
ATOM    865  OG1 THR A 171     146.071 134.829 134.462  1.00 28.00           O  
ATOM    866  CG2 THR A 171     145.659 136.417 136.217  1.00 28.00           C  
ATOM    867  N   ARG A 172     145.281 135.934 131.700  1.00 29.40           N  
ATOM    868  CA  ARG A 172     145.617 135.476 130.353  1.00 29.40           C  
ATOM    869  C   ARG A 172     144.430 135.715 129.428  1.00 29.40           C  
ATOM    870  O   ARG A 172     143.781 134.767 128.971  1.00 29.40           O  
ATOM    871  CB  ARG A 172     146.011 133.999 130.362  1.00 29.40           C  
ATOM    872  CG  ARG A 172     147.317 133.698 131.077  1.00 29.40           C  
ATOM    873  CD  ARG A 172     147.626 132.211 131.038  1.00 29.40           C  
ATOM    874  NE  ARG A 172     148.887 131.891 131.694  1.00 29.40           N  
ATOM    875  CZ  ARG A 172     149.007 131.580 132.977  1.00 29.40           C  
ATOM    876  NH1 ARG A 172     147.957 131.547 133.781  1.00 29.40           N  
ATOM    877  NH2 ARG A 172     150.211 131.298 133.467  1.00 29.40           N  
ATOM    878  N   PRO A 173     144.113 136.980 129.136  1.00 24.81           N  
ATOM    879  CA  PRO A 173     142.978 137.254 128.239  1.00 24.81           C  
ATOM    880  C   PRO A 173     143.178 136.718 126.834  1.00 24.81           C  
ATOM    881  O   PRO A 173     142.196 136.373 126.165  1.00 24.81           O  
ATOM    882  CB  PRO A 173     142.881 138.788 128.250  1.00 24.81           C  
ATOM    883  CG  PRO A 173     143.733 139.240 129.397  1.00 24.81           C  
ATOM    884  CD  PRO A 173     144.806 138.217 129.527  1.00 24.81           C  
ATOM    885  N   LEU A 174     144.421 136.640 126.364  1.00 23.74           N  
ATOM    886  CA  LEU A 174     144.727 136.211 125.008  1.00 23.74           C  
ATOM    887  C   LEU A 174     145.284 134.794 124.948  1.00 23.74           C  
ATOM    888  O   LEU A 174     145.744 134.367 123.885  1.00 23.74           O  
ATOM    889  CB  LEU A 174     145.715 137.186 124.362  1.00 23.74           C  
ATOM    890  CG  LEU A 174     145.149 138.463 123.733  1.00 23.74           C  
ATOM    891  CD1 LEU A 174     144.884 139.523 124.789  1.00 23.74           C  
ATOM    892  CD2 LEU A 174     146.092 138.998 122.668  1.00 23.74           C  
ATOM    893  N   THR A 175     145.263 134.062 126.050  1.00 30.27           N  
ATOM    894  CA  THR A 175     145.878 132.739 126.060  1.00 30.27           C  
ATOM    895  C   THR A 175     144.962 131.640 126.581  1.00 30.27           C  
ATOM    896  O   THR A 175     144.982 130.530 126.046  1.00 30.27           O  
ATOM    897  CB  THR A 175     147.170 132.785 126.902  1.00 30.27           C  
ATOM    898  OG1 THR A 175     148.072 133.748 126.344  1.00 30.27           O  
ATOM    899  CG2 THR A 175     147.849 131.426 126.933  1.00 30.27           C  
ATOM    900  N   TYR A 176     144.143 131.924 127.594  1.00 30.72           N  
ATOM    901  CA  TYR A 176     143.454 130.858 128.316  1.00 30.72           C  
ATOM    902  C   TYR A 176     142.202 130.383 127.587  1.00 30.72           C  
ATOM    903  O   TYR A 176     142.049 129.189 127.311  1.00 30.72           O  
ATOM    904  CB  TYR A 176     143.099 131.327 129.728  1.00 30.72           C  
ATOM    905  CG  TYR A 176     142.183 130.381 130.470  1.00 30.72           C  
ATOM    906  CD1 TYR A 176     142.636 129.143 130.904  1.00 30.72           C  
ATOM    907  CD2 TYR A 176     140.867 130.729 130.741  1.00 30.72           C  
ATOM    908  CE1 TYR A 176     141.804 128.280 131.586  1.00 30.72           C  
ATOM    909  CE2 TYR A 176     140.028 129.871 131.421  1.00 30.72           C  
ATOM    910  CZ  TYR A 176     140.501 128.648 131.841  1.00 30.72           C  
ATOM    911  OH  TYR A 176     139.669 127.790 132.520  1.00 30.72           O  
ATOM    912  N   ARG A 177     141.289 131.304 127.276  1.00 32.88           N  
ATOM    913  CA  ARG A 177     139.998 130.912 126.723  1.00 32.88           C  
ATOM    914  C   ARG A 177     140.116 130.286 125.340  1.00 32.88           C  
ATOM    915  O   ARG A 177     139.180 129.611 124.898  1.00 32.88           O  
ATOM    916  CB  ARG A 177     139.059 132.118 126.675  1.00 32.88           C  
ATOM    917  CG  ARG A 177     138.491 132.506 128.031  1.00 32.88           C  
ATOM    918  CD  ARG A 177     137.208 133.307 127.893  1.00 32.88           C  
ATOM    919  NE  ARG A 177     136.658 133.682 129.191  1.00 32.88           N  
ATOM    920  CZ  ARG A 177     135.710 134.592 129.369  1.00 32.88           C  
ATOM    921  NH1 ARG A 177     135.180 135.246 128.349  1.00 32.88           N  
ATOM    922  NH2 ARG A 177     135.284 134.853 130.601  1.00 32.88           N  
ATOM    923  N   ALA A 178     141.235 130.497 124.644  1.00 34.49           N  
ATOM    924  CA  ALA A 178     141.429 129.844 123.355  1.00 34.49           C  
ATOM    925  C   ALA A 178     141.709 128.356 123.524  1.00 34.49           C  
ATOM    926  O   ALA A 178     141.127 127.524 122.819  1.00 34.49           O  
ATOM    927  CB  ALA A 178     142.566 130.521 122.590  1.00 34.49           C  
ATOM    928  N   LYS A 179     142.594 128.001 124.458  1.00 37.07           N  
ATOM    929  CA  LYS A 179     142.948 126.601 124.657  1.00 37.07           C  
ATOM    930  C   LYS A 179     141.868 125.843 125.420  1.00 37.07           C  
ATOM    931  O   LYS A 179     141.638 124.657 125.160  1.00 37.07           O  
ATOM    932  CB  LYS A 179     144.288 126.500 125.385  1.00 37.07           C  
ATOM    933  CG  LYS A 179     145.465 127.020 124.576  1.00 37.07           C  
ATOM    934  CD  LYS A 179     146.768 126.882 125.341  1.00 37.07           C  
ATOM    935  CE  LYS A 179     147.947 127.321 124.491  1.00 37.07           C  
ATOM    936  NZ  LYS A 179     147.907 128.781 124.202  1.00 37.07           N  
ATOM    937  N   ARG A 180     141.201 126.503 126.363  1.00 37.53           N  
ATOM    938  CA  ARG A 180     140.152 125.869 127.159  1.00 37.53           C  
ATOM    939  C   ARG A 180     138.916 125.724 126.279  1.00 37.53           C  
ATOM    940  O   ARG A 180     138.186 126.689 126.042  1.00 37.53           O  
ATOM    941  CB  ARG A 180     139.873 126.685 128.418  1.00 37.53           C  
ATOM    942  CG  ARG A 180     138.930 126.027 129.422  1.00 37.53           C  
ATOM    943  CD  ARG A 180     137.489 126.412 129.133  1.00 37.53           C  
ATOM    944  NE  ARG A 180     137.294 127.848 129.246  1.00 37.53           N  
ATOM    945  CZ  ARG A 180     136.251 128.505 128.763  1.00 37.53           C  
ATOM    946  NH1 ARG A 180     135.288 127.889 128.118  1.00 37.53           N  
ATOM    947  NH2 ARG A 180     136.181 129.822 128.931  1.00 37.53           N  
ATOM    948  N   THR A 181     138.685 124.512 125.783  1.00 38.51           N  
ATOM    949  CA  THR A 181     137.607 124.212 124.857  1.00 38.51           C  
ATOM    950  C   THR A 181     136.500 123.441 125.575  1.00 38.51           C  
ATOM    951  O   THR A 181     136.527 123.267 126.799  1.00 38.51           O  
ATOM    952  CB  THR A 181     138.149 123.436 123.654  1.00 38.51           C  
ATOM    953  OG1 THR A 181     138.951 122.341 124.112  1.00 38.51           O  
ATOM    954  CG2 THR A 181     138.997 124.343 122.780  1.00 38.51           C  
ATOM    955  N   THR A 182     135.512 122.985 124.800  1.00 39.74           N  
ATOM    956  CA  THR A 182     134.389 122.253 125.378  1.00 39.74           C  
ATOM    957  C   THR A 182     134.852 120.958 126.035  1.00 39.74           C  
ATOM    958  O   THR A 182     134.389 120.606 127.126  1.00 39.74           O  
ATOM    959  CB  THR A 182     133.343 121.964 124.300  1.00 39.74           C  
ATOM    960  OG1 THR A 182     132.843 123.199 123.773  1.00 39.74           O  
ATOM    961  CG2 THR A 182     132.187 121.163 124.874  1.00 39.74           C  
ATOM    962  N   LYS A 183     135.770 120.237 125.388  1.00 40.68           N  
ATOM    963  CA  LYS A 183     136.301 119.013 125.973  1.00 40.68           C  
ATOM    964  C   LYS A 183     137.172 119.284 127.192  1.00 40.68           C  
ATOM    965  O   LYS A 183     137.410 118.366 127.984  1.00 40.68           O  
ATOM    966  CB  LYS A 183     137.095 118.230 124.928  1.00 40.68           C  
ATOM    967  N   ARG A 184     137.654 120.514 127.360  1.00 38.85           N  
ATOM    968  CA  ARG A 184     138.446 120.864 128.532  1.00 38.85           C  
ATOM    969  C   ARG A 184     137.587 121.299 129.710  1.00 38.85           C  
ATOM    970  O   ARG A 184     137.996 121.123 130.863  1.00 38.85           O  
ATOM    971  CB  ARG A 184     139.442 121.974 128.190  1.00 38.85           C  
ATOM    972  CG  ARG A 184     140.762 121.860 128.928  1.00 38.85           C  
ATOM    973  CD  ARG A 184     141.596 120.712 128.387  1.00 38.85           C  
ATOM    974  NE  ARG A 184     141.709 120.761 126.934  1.00 38.85           N  
ATOM    975  CZ  ARG A 184     142.640 121.438 126.278  1.00 38.85           C  
ATOM    976  NH1 ARG A 184     143.564 122.139 126.915  1.00 38.85           N  
ATOM    977  NH2 ARG A 184     142.645 121.412 124.948  1.00 38.85           N  
ATOM    978  N   ALA A 185     136.412 121.872 129.452  1.00 37.58           N  
ATOM    979  CA  ALA A 185     135.489 122.192 130.530  1.00 37.58           C  
ATOM    980  C   ALA A 185     134.770 120.961 131.061  1.00 37.58           C  
ATOM    981  O   ALA A 185     134.240 121.003 132.176  1.00 37.58           O  
ATOM    982  CB  ALA A 185     134.466 123.228 130.063  1.00 37.58           C  
ATOM    983  N   GLY A 186     134.730 119.876 130.285  1.00 34.09           N  
ATOM    984  CA  GLY A 186     134.114 118.653 130.772  1.00 34.09           C  
ATOM    985  C   GLY A 186     134.876 118.030 131.925  1.00 34.09           C  
ATOM    986  O   GLY A 186     134.278 117.608 132.918  1.00 34.09           O  
ATOM    987  N   VAL A 187     136.204 117.960 131.812  1.00 35.51           N  
ATOM    988  CA  VAL A 187     137.002 117.423 132.908  1.00 35.51           C  
ATOM    989  C   VAL A 187     136.984 118.371 134.100  1.00 35.51           C  
ATOM    990  O   VAL A 187     137.098 117.932 135.251  1.00 35.51           O  
ATOM    991  CB  VAL A 187     138.439 117.118 132.441  1.00 35.51           C  
ATOM    992  CG1 VAL A 187     138.427 116.079 131.332  1.00 35.51           C  
ATOM    993  CG2 VAL A 187     139.141 118.382 131.980  1.00 35.51           C  
ATOM    994  N   MET A 188     136.849 119.676 133.855  1.00 34.85           N  
ATOM    995  CA  MET A 188     136.702 120.626 134.953  1.00 34.85           C  
ATOM    996  C   MET A 188     135.398 120.391 135.704  1.00 34.85           C  
ATOM    997  O   MET A 188     135.380 120.337 136.938  1.00 34.85           O  
ATOM    998  CB  MET A 188     136.763 122.056 134.419  1.00 34.85           C  
ATOM    999  CG  MET A 188     138.161 122.634 134.344  1.00 34.85           C  
ATOM   1000  SD  MET A 188     138.252 124.105 133.307  1.00 34.85           S  
ATOM   1001  CE  MET A 188     138.231 125.399 134.544  1.00 34.85           C  
ATOM   1002  N   ILE A 189     134.293 120.252 134.969  1.00 34.03           N  
ATOM   1003  CA  ILE A 189     133.012 119.948 135.597  1.00 34.03           C  
ATOM   1004  C   ILE A 189     133.000 118.519 136.123  1.00 34.03           C  
ATOM   1005  O   ILE A 189     132.478 118.247 137.211  1.00 34.03           O  
ATOM   1006  CB  ILE A 189     131.862 120.199 134.604  1.00 34.03           C  
ATOM   1007  CG1 ILE A 189     131.734 121.693 134.306  1.00 34.03           C  
ATOM   1008  CG2 ILE A 189     130.552 119.653 135.148  1.00 34.03           C  
ATOM   1009  CD1 ILE A 189     130.878 122.000 133.100  1.00 34.03           C  
ATOM   1010  N   GLY A 190     133.576 117.585 135.364  1.00 33.02           N  
ATOM   1011  CA  GLY A 190     133.575 116.196 135.792  1.00 33.02           C  
ATOM   1012  C   GLY A 190     134.318 115.982 137.096  1.00 33.02           C  
ATOM   1013  O   GLY A 190     133.839 115.276 137.984  1.00 33.02           O  
ATOM   1014  N   LEU A 191     135.487 116.609 137.241  1.00 32.87           N  
ATOM   1015  CA  LEU A 191     136.262 116.442 138.465  1.00 32.87           C  
ATOM   1016  C   LEU A 191     135.542 117.027 139.673  1.00 32.87           C  
ATOM   1017  O   LEU A 191     135.677 116.505 140.784  1.00 32.87           O  
ATOM   1018  CB  LEU A 191     137.642 117.081 138.309  1.00 32.87           C  
ATOM   1019  CG  LEU A 191     138.686 116.252 137.559  1.00 32.87           C  
ATOM   1020  CD1 LEU A 191     139.924 117.085 137.280  1.00 32.87           C  
ATOM   1021  CD2 LEU A 191     139.044 114.998 138.339  1.00 32.87           C  
ATOM   1022  N   ALA A 192     134.781 118.105 139.479  1.00 32.26           N  
ATOM   1023  CA  ALA A 192     134.050 118.703 140.591  1.00 32.26           C  
ATOM   1024  C   ALA A 192     133.005 117.745 141.149  1.00 32.26           C  
ATOM   1025  O   ALA A 192     132.834 117.645 142.368  1.00 32.26           O  
ATOM   1026  CB  ALA A 192     133.397 120.011 140.148  1.00 32.26           C  
ATOM   1027  N   TRP A 193     132.294 117.033 140.272  1.00 31.55           N  
ATOM   1028  CA  TRP A 193     131.251 116.118 140.726  1.00 31.55           C  
ATOM   1029  C   TRP A 193     131.823 114.779 141.178  1.00 31.55           C  
ATOM   1030  O   TRP A 193     131.349 114.205 142.164  1.00 31.55           O  
ATOM   1031  CB  TRP A 193     130.221 115.907 139.617  1.00 31.55           C  
ATOM   1032  CG  TRP A 193     129.215 117.011 139.512  1.00 31.55           C  
ATOM   1033  CD1 TRP A 193     129.297 118.120 138.723  1.00 31.55           C  
ATOM   1034  CD2 TRP A 193     127.974 117.112 140.219  1.00 31.55           C  
ATOM   1035  NE1 TRP A 193     128.185 118.906 138.895  1.00 31.55           N  
ATOM   1036  CE2 TRP A 193     127.357 118.310 139.809  1.00 31.55           C  
ATOM   1037  CE3 TRP A 193     127.325 116.307 141.160  1.00 31.55           C  
ATOM   1038  CZ2 TRP A 193     126.123 118.722 140.305  1.00 31.55           C  
ATOM   1039  CZ3 TRP A 193     126.100 116.719 141.652  1.00 31.55           C  
ATOM   1040  CH2 TRP A 193     125.512 117.914 141.223  1.00 31.55           C  
ATOM   1041  N   VAL A 194     132.829 114.259 140.469  1.00 30.85           N  
ATOM   1042  CA  VAL A 194     133.395 112.963 140.832  1.00 30.85           C  
ATOM   1043  C   VAL A 194     134.082 113.032 142.191  1.00 30.85           C  
ATOM   1044  O   VAL A 194     133.901 112.149 143.037  1.00 30.85           O  
ATOM   1045  CB  VAL A 194     134.354 112.466 139.735  1.00 30.85           C  
ATOM   1046  CG1 VAL A 194     135.021 111.169 140.167  1.00 30.85           C  
ATOM   1047  CG2 VAL A 194     133.599 112.254 138.433  1.00 30.85           C  
ATOM   1048  N   ILE A 195     134.886 114.073 142.422  1.00 32.54           N  
ATOM   1049  CA  ILE A 195     135.550 114.220 143.714  1.00 32.54           C  
ATOM   1050  C   ILE A 195     134.525 114.453 144.817  1.00 32.54           C  
ATOM   1051  O   ILE A 195     134.641 113.902 145.918  1.00 32.54           O  
ATOM   1052  CB  ILE A 195     136.596 115.348 143.653  1.00 32.54           C  
ATOM   1053  CG1 ILE A 195     137.747 114.945 142.731  1.00 32.54           C  
ATOM   1054  CG2 ILE A 195     137.120 115.676 145.043  1.00 32.54           C  
ATOM   1055  CD1 ILE A 195     138.663 116.083 142.367  1.00 32.54           C  
ATOM   1056  N   SER A 196     133.506 115.271 144.541  1.00 32.41           N  
ATOM   1057  CA  SER A 196     132.426 115.447 145.505  1.00 32.41           C  
ATOM   1058  C   SER A 196     131.675 114.145 145.743  1.00 32.41           C  
ATOM   1059  O   SER A 196     131.129 113.936 146.832  1.00 32.41           O  
ATOM   1060  CB  SER A 196     131.462 116.533 145.029  1.00 32.41           C  
ATOM   1061  OG  SER A 196     132.162 117.702 144.646  1.00 32.41           O  
ATOM   1062  N   PHE A 197     131.634 113.260 144.745  1.00 33.79           N  
ATOM   1063  CA  PHE A 197     130.981 111.970 144.934  1.00 33.79           C  
ATOM   1064  C   PHE A 197     131.772 111.099 145.901  1.00 33.79           C  
ATOM   1065  O   PHE A 197     131.264 110.710 146.959  1.00 33.79           O  
ATOM   1066  CB  PHE A 197     130.794 111.258 143.596  1.00 33.79           C  
ATOM   1067  CG  PHE A 197     130.078 109.941 143.712  1.00 33.79           C  
ATOM   1068  CD1 PHE A 197     128.700 109.896 143.831  1.00 33.79           C  
ATOM   1069  CD2 PHE A 197     130.783 108.750 143.711  1.00 33.79           C  
ATOM   1070  CE1 PHE A 197     128.038 108.687 143.942  1.00 33.79           C  
ATOM   1071  CE2 PHE A 197     130.128 107.538 143.823  1.00 33.79           C  
ATOM   1072  CZ  PHE A 197     128.754 107.507 143.938  1.00 33.79           C  
ATOM   1073  N   VAL A 198     133.020 110.774 145.562  1.00 35.10           N  
ATOM   1074  CA  VAL A 198     133.810 109.996 146.508  1.00 35.10           C  
ATOM   1075  C   VAL A 198     134.571 110.936 147.438  1.00 35.10           C  
ATOM   1076  O   VAL A 198     135.801 111.052 147.383  1.00 35.10           O  
ATOM   1077  CB  VAL A 198     134.756 109.026 145.770  1.00 35.10           C  
ATOM   1078  CG1 VAL A 198     133.946 108.037 144.954  1.00 35.10           C  
ATOM   1079  CG2 VAL A 198     135.703 109.781 144.840  1.00 35.10           C  
ATOM   1080  N   LEU A 199     133.829 111.584 148.331  1.00 35.21           N  
ATOM   1081  CA  LEU A 199     134.347 112.147 149.572  1.00 35.21           C  
ATOM   1082  C   LEU A 199     133.393 111.954 150.737  1.00 35.21           C  
ATOM   1083  O   LEU A 199     133.847 111.909 151.886  1.00 35.21           O  
ATOM   1084  CB  LEU A 199     134.647 113.643 149.407  1.00 35.21           C  
ATOM   1085  CG  LEU A 199     135.265 114.395 150.590  1.00 35.21           C  
ATOM   1086  CD1 LEU A 199     136.551 113.724 151.044  1.00 35.21           C  
ATOM   1087  CD2 LEU A 199     135.515 115.849 150.230  1.00 35.21           C  
ATOM   1088  N   TRP A 200     132.095 111.811 150.477  1.00 36.16           N  
ATOM   1089  CA  TRP A 200     131.065 111.614 151.485  1.00 36.16           C  
ATOM   1090  C   TRP A 200     130.290 110.325 151.272  1.00 36.16           C  
ATOM   1091  O   TRP A 200     130.098 109.558 152.223  1.00 36.16           O  
ATOM   1092  CB  TRP A 200     130.096 112.807 151.480  1.00 36.16           C  
ATOM   1093  CG  TRP A 200     130.750 114.136 151.685  1.00 36.16           C  
ATOM   1094  CD1 TRP A 200     131.118 115.027 150.720  1.00 36.16           C  
ATOM   1095  CD2 TRP A 200     131.101 114.733 152.937  1.00 36.16           C  
ATOM   1096  NE1 TRP A 200     131.682 116.140 151.293  1.00 36.16           N  
ATOM   1097  CE2 TRP A 200     131.683 115.984 152.654  1.00 36.16           C  
ATOM   1098  CE3 TRP A 200     130.984 114.330 154.270  1.00 36.16           C  
ATOM   1099  CZ2 TRP A 200     132.146 116.835 153.654  1.00 36.16           C  
ATOM   1100  CZ3 TRP A 200     131.443 115.176 155.260  1.00 36.16           C  
ATOM   1101  CH2 TRP A 200     132.016 116.414 154.948  1.00 36.16           C  
ATOM   1102  N   ALA A 201     129.845 110.064 150.041  1.00 37.09           N  
ATOM   1103  CA  ALA A 201     128.917 108.961 149.796  1.00 37.09           C  
ATOM   1104  C   ALA A 201     129.481 107.598 150.178  1.00 37.09           C  
ATOM   1105  O   ALA A 201     128.780 106.844 150.876  1.00 37.09           O  
ATOM   1106  CB  ALA A 201     128.456 108.992 148.334  1.00 37.09           C  
ATOM   1107  N   PRO A 202     130.696 107.203 149.770  1.00 37.73           N  
ATOM   1108  CA  PRO A 202     131.225 105.923 150.272  1.00 37.73           C  
ATOM   1109  C   PRO A 202     131.377 105.894 151.783  1.00 37.73           C  
ATOM   1110  O   PRO A 202     131.165 104.848 152.406  1.00 37.73           O  
ATOM   1111  CB  PRO A 202     132.578 105.797 149.557  1.00 37.73           C  
ATOM   1112  CG  PRO A 202     132.453 106.661 148.354  1.00 37.73           C  
ATOM   1113  CD  PRO A 202     131.618 107.818 148.798  1.00 37.73           C  
ATOM   1114  N   ALA A 203     131.740 107.025 152.391  1.00 37.98           N  
ATOM   1115  CA  ALA A 203     131.902 107.074 153.839  1.00 37.98           C  
ATOM   1116  C   ALA A 203     130.560 107.138 154.560  1.00 37.98           C  
ATOM   1117  O   ALA A 203     130.389 106.512 155.611  1.00 37.98           O  
ATOM   1118  CB  ALA A 203     132.775 108.266 154.227  1.00 37.98           C  
ATOM   1119  N   ILE A 204     129.599 107.892 154.020  1.00 38.70           N  
ATOM   1120  CA  ILE A 204     128.303 108.022 154.680  1.00 38.70           C  
ATOM   1121  C   ILE A 204     127.515 106.722 154.586  1.00 38.70           C  
ATOM   1122  O   ILE A 204     126.933 106.260 155.575  1.00 38.70           O  
ATOM   1123  CB  ILE A 204     127.515 109.204 154.083  1.00 38.70           C  
ATOM   1124  CG1 ILE A 204     128.100 110.534 154.557  1.00 38.70           C  
ATOM   1125  CG2 ILE A 204     126.044 109.116 154.455  1.00 38.70           C  
ATOM   1126  CD1 ILE A 204     127.593 111.726 153.784  1.00 38.70           C  
ATOM   1127  N   LEU A 205     127.489 106.106 153.402  1.00 40.46           N  
ATOM   1128  CA  LEU A 205     126.631 104.945 153.188  1.00 40.46           C  
ATOM   1129  C   LEU A 205     127.172 103.704 153.889  1.00 40.46           C  
ATOM   1130  O   LEU A 205     126.401 102.925 154.460  1.00 40.46           O  
ATOM   1131  CB  LEU A 205     126.472 104.680 151.691  1.00 40.46           C  
ATOM   1132  CG  LEU A 205     125.719 105.726 150.867  1.00 40.46           C  
ATOM   1133  CD1 LEU A 205     125.743 105.359 149.392  1.00 40.46           C  
ATOM   1134  CD2 LEU A 205     124.291 105.877 151.359  1.00 40.46           C  
ATOM   1135  N   PHE A 206     128.488 103.500 153.858  1.00 43.38           N  
ATOM   1136  CA  PHE A 206     129.085 102.237 154.273  1.00 43.38           C  
ATOM   1137  C   PHE A 206     129.789 102.309 155.623  1.00 43.38           C  
ATOM   1138  O   PHE A 206     130.495 101.364 155.985  1.00 43.38           O  
ATOM   1139  CB  PHE A 206     130.063 101.746 153.203  1.00 43.38           C  
ATOM   1140  CG  PHE A 206     129.471 101.683 151.823  1.00 43.38           C  
ATOM   1141  CD1 PHE A 206     128.187 101.203 151.626  1.00 43.38           C  
ATOM   1142  CD2 PHE A 206     130.200 102.105 150.724  1.00 43.38           C  
ATOM   1143  CE1 PHE A 206     127.640 101.146 150.358  1.00 43.38           C  
ATOM   1144  CE2 PHE A 206     129.659 102.050 149.454  1.00 43.38           C  
ATOM   1145  CZ  PHE A 206     128.377 101.570 149.270  1.00 43.38           C  
ATOM   1146  N   TRP A 207     129.625 103.399 156.376  1.00 45.15           N  
ATOM   1147  CA  TRP A 207     130.254 103.465 157.692  1.00 45.15           C  
ATOM   1148  C   TRP A 207     129.642 102.452 158.652  1.00 45.15           C  
ATOM   1149  O   TRP A 207     130.361 101.811 159.428  1.00 45.15           O  
ATOM   1150  CB  TRP A 207     130.146 104.876 158.269  1.00 45.15           C  
ATOM   1151  CG  TRP A 207     131.069 105.101 159.425  1.00 45.15           C  
ATOM   1152  CD1 TRP A 207     130.753 105.040 160.749  1.00 45.15           C  
ATOM   1153  CD2 TRP A 207     132.467 105.407 159.360  1.00 45.15           C  
ATOM   1154  NE1 TRP A 207     131.864 105.297 161.514  1.00 45.15           N  
ATOM   1155  CE2 TRP A 207     132.930 105.524 160.684  1.00 45.15           C  
ATOM   1156  CE3 TRP A 207     133.371 105.596 158.310  1.00 45.15           C  
ATOM   1157  CZ2 TRP A 207     134.256 105.822 160.987  1.00 45.15           C  
ATOM   1158  CZ3 TRP A 207     134.685 105.891 158.613  1.00 45.15           C  
ATOM   1159  CH2 TRP A 207     135.115 106.002 159.940  1.00 45.15           C  
ATOM   1160  N   GLN A 208     128.317 102.297 158.620  1.00 51.10           N  
ATOM   1161  CA  GLN A 208     127.667 101.313 159.478  1.00 51.10           C  
ATOM   1162  C   GLN A 208     127.998  99.890 159.048  1.00 51.10           C  
ATOM   1163  O   GLN A 208     128.010  98.977 159.881  1.00 51.10           O  
ATOM   1164  CB  GLN A 208     126.155 101.531 159.475  1.00 51.10           C  
ATOM   1165  CG  GLN A 208     125.523 101.452 158.095  1.00 51.10           C  
ATOM   1166  CD  GLN A 208     124.091 101.942 158.078  1.00 51.10           C  
ATOM   1167  OE1 GLN A 208     123.555 102.363 159.102  1.00 51.10           O  
ATOM   1168  NE2 GLN A 208     123.461 101.888 156.911  1.00 51.10           N  
ATOM   1169  N   TYR A 209     128.267  99.684 157.761  1.00 54.37           N  
ATOM   1170  CA  TYR A 209     128.560  98.366 157.219  1.00 54.37           C  
ATOM   1171  C   TYR A 209     130.036  97.998 157.309  1.00 54.37           C  
ATOM   1172  O   TYR A 209     130.392  96.854 157.007  1.00 54.37           O  
ATOM   1173  CB  TYR A 209     128.096  98.296 155.758  1.00 54.37           C  
ATOM   1174  CG  TYR A 209     128.130  96.913 155.150  1.00 54.37           C  
ATOM   1175  CD1 TYR A 209     127.346  95.888 155.660  1.00 54.37           C  
ATOM   1176  CD2 TYR A 209     128.947  96.634 154.062  1.00 54.37           C  
ATOM   1177  CE1 TYR A 209     127.376  94.622 155.104  1.00 54.37           C  
ATOM   1178  CE2 TYR A 209     128.984  95.373 153.500  1.00 54.37           C  
ATOM   1179  CZ  TYR A 209     128.197  94.371 154.025  1.00 54.37           C  
ATOM   1180  OH  TYR A 209     128.230  93.113 153.468  1.00 54.37           O  
ATOM   1181  N   PHE A 210     130.898  98.922 157.731  1.00 56.03           N  
ATOM   1182  CA  PHE A 210     132.338  98.700 157.751  1.00 56.03           C  
ATOM   1183  C   PHE A 210     132.896  98.535 159.156  1.00 56.03           C  
ATOM   1184  O   PHE A 210     133.564  97.537 159.442  1.00 56.03           O  
ATOM   1185  CB  PHE A 210     133.055  99.857 157.042  1.00 56.03           C  
ATOM   1186  CG  PHE A 210     134.512  99.604 156.787  1.00 56.03           C  
ATOM   1187  CD1 PHE A 210     134.913  98.669 155.846  1.00 56.03           C  
ATOM   1188  CD2 PHE A 210     135.483 100.304 157.485  1.00 56.03           C  
ATOM   1189  CE1 PHE A 210     136.256  98.435 155.609  1.00 56.03           C  
ATOM   1190  CE2 PHE A 210     136.826 100.075 157.254  1.00 56.03           C  
ATOM   1191  CZ  PHE A 210     137.214  99.140 156.314  1.00 56.03           C  
ATOM   1192  N   VAL A 211     132.643  99.490 160.045  1.00 57.08           N  
ATOM   1193  CA  VAL A 211     133.138  99.449 161.417  1.00 57.08           C  
ATOM   1194  C   VAL A 211     131.941  99.238 162.332  1.00 57.08           C  
ATOM   1195  O   VAL A 211     131.060 100.102 162.424  1.00 57.08           O  
ATOM   1196  CB  VAL A 211     133.903 100.727 161.788  1.00 57.08           C  
ATOM   1197  CG1 VAL A 211     134.210 100.747 163.278  1.00 57.08           C  
ATOM   1198  CG2 VAL A 211     135.182 100.837 160.973  1.00 57.08           C  
ATOM   1199  N   GLY A 212     131.915  98.099 163.017  1.00 56.08           N  
ATOM   1200  CA  GLY A 212     130.804  97.801 163.905  1.00 56.08           C  
ATOM   1201  C   GLY A 212     129.496  97.703 163.144  1.00 56.08           C  
ATOM   1202  O   GLY A 212     129.399  97.034 162.110  1.00 56.08           O  
ATOM   1203  N   LYS A 213     128.472  98.376 163.662  1.00 54.33           N  
ATOM   1204  CA  LYS A 213     127.150  98.392 163.050  1.00 54.33           C  
ATOM   1205  C   LYS A 213     126.576  99.798 163.188  1.00 54.33           C  
ATOM   1206  O   LYS A 213     127.293 100.756 163.493  1.00 54.33           O  
ATOM   1207  CB  LYS A 213     126.242  97.328 163.682  1.00 54.33           C  
ATOM   1208  N   ARG A 214     125.272  99.922 162.947  1.00 52.54           N  
ATOM   1209  CA  ARG A 214     124.598 101.207 163.073  1.00 52.54           C  
ATOM   1210  C   ARG A 214     124.666 101.705 164.512  1.00 52.54           C  
ATOM   1211  O   ARG A 214     124.406 100.952 165.455  1.00 52.54           O  
ATOM   1212  CB  ARG A 214     123.144 101.077 162.618  1.00 52.54           C  
ATOM   1213  CG  ARG A 214     122.300 102.315 162.847  1.00 52.54           C  
ATOM   1214  CD  ARG A 214     122.875 103.514 162.116  1.00 52.54           C  
ATOM   1215  NE  ARG A 214     122.414 103.601 160.736  1.00 52.54           N  
ATOM   1216  CZ  ARG A 214     121.228 104.065 160.367  1.00 52.54           C  
ATOM   1217  NH1 ARG A 214     120.336 104.468 161.257  1.00 52.54           N  
ATOM   1218  NH2 ARG A 214     120.929 104.125 159.073  1.00 52.54           N  
ATOM   1219  N   THR A 215     125.017 102.982 164.679  1.00 54.09           N  
ATOM   1220  CA  THR A 215     125.227 103.557 166.000  1.00 54.09           C  
ATOM   1221  C   THR A 215     124.333 104.746 166.325  1.00 54.09           C  
ATOM   1222  O   THR A 215     124.193 105.074 167.508  1.00 54.09           O  
ATOM   1223  CB  THR A 215     126.691 103.993 166.173  1.00 54.09           C  
ATOM   1224  OG1 THR A 215     127.013 104.998 165.204  1.00 54.09           O  
ATOM   1225  CG2 THR A 215     127.625 102.808 165.998  1.00 54.09           C  
ATOM   1226  N   VAL A 216     123.741 105.403 165.333  1.00 51.92           N  
ATOM   1227  CA  VAL A 216     122.864 106.542 165.594  1.00 51.92           C  
ATOM   1228  C   VAL A 216     121.571 106.033 166.218  1.00 51.92           C  
ATOM   1229  O   VAL A 216     121.194 104.873 165.998  1.00 51.92           O  
ATOM   1230  CB  VAL A 216     122.584 107.349 164.315  1.00 51.92           C  
ATOM   1231  CG1 VAL A 216     123.874 107.667 163.594  1.00 51.92           C  
ATOM   1232  CG2 VAL A 216     121.626 106.604 163.403  1.00 51.92           C  
ATOM   1233  N   PRO A 217     120.880 106.842 167.019  1.00 54.22           N  
ATOM   1234  CA  PRO A 217     119.586 106.413 167.537  1.00 54.22           C  
ATOM   1235  C   PRO A 217     118.600 106.216 166.408  1.00 54.22           C  
ATOM   1236  O   PRO A 217     118.658 106.913 165.377  1.00 54.22           O  
ATOM   1237  CB  PRO A 217     119.172 107.573 168.455  1.00 54.22           C  
ATOM   1238  CG  PRO A 217     120.448 108.251 168.813  1.00 54.22           C  
ATOM   1239  CD  PRO A 217     121.318 108.119 167.604  1.00 54.22           C  
ATOM   1240  N   PRO A 218     117.676 105.260 166.546  1.00 55.08           N  
ATOM   1241  CA  PRO A 218     116.702 105.021 165.468  1.00 55.08           C  
ATOM   1242  C   PRO A 218     115.829 106.223 165.152  1.00 55.08           C  
ATOM   1243  O   PRO A 218     115.442 106.407 163.991  1.00 55.08           O  
ATOM   1244  CB  PRO A 218     115.871 103.845 166.003  1.00 55.08           C  
ATOM   1245  CG  PRO A 218     116.750 103.186 167.018  1.00 55.08           C  
ATOM   1246  CD  PRO A 218     117.532 104.295 167.649  1.00 55.08           C  
ATOM   1247  N   GLY A 219     115.504 107.048 166.147  1.00 54.63           N  
ATOM   1248  CA  GLY A 219     114.632 108.185 165.920  1.00 54.63           C  
ATOM   1249  C   GLY A 219     115.301 109.417 165.354  1.00 54.63           C  
ATOM   1250  O   GLY A 219     114.604 110.372 165.000  1.00 54.63           O  
ATOM   1251  N   GLU A 220     116.625 109.423 165.256  1.00 54.82           N  
ATOM   1252  CA  GLU A 220     117.379 110.550 164.726  1.00 54.82           C  
ATOM   1253  C   GLU A 220     118.170 110.106 163.501  1.00 54.82           C  
ATOM   1254  O   GLU A 220     118.109 108.949 163.079  1.00 54.82           O  
ATOM   1255  CB  GLU A 220     118.305 111.137 165.795  1.00 54.82           C  
ATOM   1256  CG  GLU A 220     117.574 111.797 166.950  1.00 54.82           C  
ATOM   1257  CD  GLU A 220     118.519 112.349 167.998  1.00 54.82           C  
ATOM   1258  OE1 GLU A 220     119.738 112.106 167.886  1.00 54.82           O  
ATOM   1259  OE2 GLU A 220     118.042 113.027 168.932  1.00 54.82           O  
ATOM   1260  N   CYS A 221     118.922 111.043 162.926  1.00 48.17           N  
ATOM   1261  CA  CYS A 221     119.733 110.739 161.754  1.00 48.17           C  
ATOM   1262  C   CYS A 221     120.848 111.763 161.622  1.00 48.17           C  
ATOM   1263  O   CYS A 221     120.591 112.970 161.653  1.00 48.17           O  
ATOM   1264  CB  CYS A 221     118.887 110.725 160.480  1.00 48.17           C  
ATOM   1265  SG  CYS A 221     119.856 110.393 158.996  1.00 48.17           S  
ATOM   1266  N   PHE A 222     122.076 111.277 161.466  1.00 43.75           N  
ATOM   1267  CA  PHE A 222     123.219 112.128 161.164  1.00 43.75           C  
ATOM   1268  C   PHE A 222     124.299 111.264 160.521  1.00 43.75           C  
ATOM   1269  O   PHE A 222     124.099 110.074 160.263  1.00 43.75           O  
ATOM   1270  CB  PHE A 222     123.723 112.863 162.412  1.00 43.75           C  
ATOM   1271  CG  PHE A 222     124.048 111.964 163.569  1.00 43.75           C  
ATOM   1272  CD1 PHE A 222     123.083 111.648 164.511  1.00 43.75           C  
ATOM   1273  CD2 PHE A 222     125.326 111.456 163.732  1.00 43.75           C  
ATOM   1274  CE1 PHE A 222     123.380 110.829 165.580  1.00 43.75           C  
ATOM   1275  CE2 PHE A 222     125.630 110.638 164.799  1.00 43.75           C  
ATOM   1276  CZ  PHE A 222     124.657 110.324 165.726  1.00 43.75           C  
ATOM   1277  N   ILE A 223     125.454 111.881 160.269  1.00 41.29           N  
ATOM   1278  CA  ILE A 223     126.466 111.280 159.404  1.00 41.29           C  
ATOM   1279  C   ILE A 223     127.052 110.017 160.029  1.00 41.29           C  
ATOM   1280  O   ILE A 223     127.386 109.059 159.322  1.00 41.29           O  
ATOM   1281  CB  ILE A 223     127.548 112.321 159.074  1.00 41.29           C  
ATOM   1282  CG1 ILE A 223     126.937 113.457 158.258  1.00 41.29           C  
ATOM   1283  CG2 ILE A 223     128.672 111.698 158.299  1.00 41.29           C  
ATOM   1284  CD1 ILE A 223     126.319 112.988 156.966  1.00 41.29           C  
ATOM   1285  N   GLN A 224     127.193 109.998 161.353  1.00 42.43           N  
ATOM   1286  CA  GLN A 224     127.614 108.883 162.196  1.00 42.43           C  
ATOM   1287  C   GLN A 224     129.124 108.641 162.187  1.00 42.43           C  
ATOM   1288  O   GLN A 224     129.589 107.793 162.949  1.00 42.43           O  
ATOM   1289  CB  GLN A 224     126.911 107.556 161.848  1.00 42.43           C  
ATOM   1290  N   PHE A 225     129.912 109.338 161.368  1.00 43.02           N  
ATOM   1291  CA  PHE A 225     131.359 109.319 161.541  1.00 43.02           C  
ATOM   1292  C   PHE A 225     131.905 110.674 161.967  1.00 43.02           C  
ATOM   1293  O   PHE A 225     133.126 110.846 162.045  1.00 43.02           O  
ATOM   1294  CB  PHE A 225     132.074 108.800 160.280  1.00 43.02           C  
ATOM   1295  CG  PHE A 225     131.944 109.675 159.054  1.00 43.02           C  
ATOM   1296  CD1 PHE A 225     132.576 110.908 158.973  1.00 43.02           C  
ATOM   1297  CD2 PHE A 225     131.248 109.221 157.947  1.00 43.02           C  
ATOM   1298  CE1 PHE A 225     132.472 111.687 157.838  1.00 43.02           C  
ATOM   1299  CE2 PHE A 225     131.147 109.993 156.805  1.00 43.02           C  
ATOM   1300  CZ  PHE A 225     131.758 111.229 156.753  1.00 43.02           C  
ATOM   1301  N   LEU A 226     131.029 111.638 162.255  1.00 44.98           N  
ATOM   1302  CA  LEU A 226     131.465 112.913 162.805  1.00 44.98           C  
ATOM   1303  C   LEU A 226     131.907 112.802 164.258  1.00 44.98           C  
ATOM   1304  O   LEU A 226     132.537 113.734 164.766  1.00 44.98           O  
ATOM   1305  CB  LEU A 226     130.347 113.950 162.685  1.00 44.98           C  
ATOM   1306  CG  LEU A 226     129.789 114.207 161.284  1.00 44.98           C  
ATOM   1307  CD1 LEU A 226     128.537 115.067 161.358  1.00 44.98           C  
ATOM   1308  CD2 LEU A 226     130.837 114.854 160.393  1.00 44.98           C  
ATOM   1309  N   SER A 227     131.584 111.699 164.937  1.00 47.76           N  
ATOM   1310  CA  SER A 227     132.013 111.530 166.321  1.00 47.76           C  
ATOM   1311  C   SER A 227     133.530 111.429 166.425  1.00 47.76           C  
ATOM   1312  O   SER A 227     134.135 112.013 167.331  1.00 47.76           O  
ATOM   1313  CB  SER A 227     131.349 110.294 166.927  1.00 47.76           C  
ATOM   1314  OG  SER A 227     131.774 110.090 168.263  1.00 47.76           O  
ATOM   1315  N   GLU A 228     134.158 110.696 165.514  1.00 52.56           N  
ATOM   1316  CA  GLU A 228     135.607 110.538 165.538  1.00 52.56           C  
ATOM   1317  C   GLU A 228     136.274 111.812 165.033  1.00 52.56           C  
ATOM   1318  O   GLU A 228     135.984 112.246 163.913  1.00 52.56           O  
ATOM   1319  CB  GLU A 228     136.029 109.352 164.682  1.00 52.56           C  
ATOM   1320  CG  GLU A 228     135.783 107.998 165.329  1.00 52.56           C  
ATOM   1321  CD  GLU A 228     136.331 106.851 164.503  1.00 52.56           C  
ATOM   1322  OE1 GLU A 228     136.638 107.067 163.312  1.00 52.56           O  
ATOM   1323  OE2 GLU A 228     136.454 105.733 165.046  1.00 52.56           O  
ATOM   1324  N   PRO A 229     137.161 112.438 165.811  1.00 51.55           N  
ATOM   1325  CA  PRO A 229     137.797 113.674 165.344  1.00 51.55           C  
ATOM   1326  C   PRO A 229     139.017 113.420 164.473  1.00 51.55           C  
ATOM   1327  O   PRO A 229     140.044 114.088 164.625  1.00 51.55           O  
ATOM   1328  CB  PRO A 229     138.182 114.375 166.650  1.00 51.55           C  
ATOM   1329  CG  PRO A 229     138.444 113.247 167.602  1.00 51.55           C  
ATOM   1330  CD  PRO A 229     137.598 112.069 167.169  1.00 51.55           C  
ATOM   1331  N   THR A 230     138.918 112.455 163.561  1.00 48.99           N  
ATOM   1332  CA  THR A 230     139.965 112.201 162.579  1.00 48.99           C  
ATOM   1333  C   THR A 230     139.466 112.345 161.151  1.00 48.99           C  
ATOM   1334  O   THR A 230     140.055 113.095 160.364  1.00 48.99           O  
ATOM   1335  CB  THR A 230     140.559 110.798 162.785  1.00 48.99           C  
ATOM   1336  OG1 THR A 230     140.881 110.612 164.168  1.00 48.99           O  
ATOM   1337  CG2 THR A 230     141.815 110.627 161.949  1.00 48.99           C  
ATOM   1338  N   ILE A 231     138.388 111.646 160.795  1.00 45.17           N  
ATOM   1339  CA  ILE A 231     137.853 111.741 159.442  1.00 45.17           C  
ATOM   1340  C   ILE A 231     137.075 113.037 159.256  1.00 45.17           C  
ATOM   1341  O   ILE A 231     137.014 113.575 158.145  1.00 45.17           O  
ATOM   1342  CB  ILE A 231     136.992 110.504 159.127  1.00 45.17           C  
ATOM   1343  CG1 ILE A 231     136.462 110.558 157.692  1.00 45.17           C  
ATOM   1344  CG2 ILE A 231     135.855 110.371 160.126  1.00 45.17           C  
ATOM   1345  CD1 ILE A 231     135.918 109.241 157.193  1.00 45.17           C  
ATOM   1346  N   THR A 232     136.481 113.568 160.328  1.00 46.19           N  
ATOM   1347  CA  THR A 232     135.747 114.824 160.218  1.00 46.19           C  
ATOM   1348  C   THR A 232     136.677 115.983 159.872  1.00 46.19           C  
ATOM   1349  O   THR A 232     136.306 116.865 159.090  1.00 46.19           O  
ATOM   1350  CB  THR A 232     134.974 115.099 161.509  1.00 46.19           C  
ATOM   1351  OG1 THR A 232     134.126 116.241 161.331  1.00 46.19           O  
ATOM   1352  CG2 THR A 232     135.918 115.340 162.674  1.00 46.19           C  
ATOM   1353  N   PHE A 233     137.885 116.002 160.441  1.00 46.46           N  
ATOM   1354  CA  PHE A 233     138.858 117.025 160.073  1.00 46.46           C  
ATOM   1355  C   PHE A 233     139.304 116.862 158.627  1.00 46.46           C  
ATOM   1356  O   PHE A 233     139.443 117.851 157.899  1.00 46.46           O  
ATOM   1357  CB  PHE A 233     140.061 116.974 161.014  1.00 46.46           C  
ATOM   1358  CG  PHE A 233     139.802 117.579 162.363  1.00 46.46           C  
ATOM   1359  CD1 PHE A 233     138.724 118.421 162.564  1.00 46.46           C  
ATOM   1360  CD2 PHE A 233     140.641 117.307 163.430  1.00 46.46           C  
ATOM   1361  CE1 PHE A 233     138.484 118.979 163.804  1.00 46.46           C  
ATOM   1362  CE2 PHE A 233     140.406 117.863 164.672  1.00 46.46           C  
ATOM   1363  CZ  PHE A 233     139.325 118.701 164.858  1.00 46.46           C  
ATOM   1364  N   GLY A 234     139.534 115.621 158.193  1.00 43.23           N  
ATOM   1365  CA  GLY A 234     139.918 115.391 156.811  1.00 43.23           C  
ATOM   1366  C   GLY A 234     138.834 115.791 155.830  1.00 43.23           C  
ATOM   1367  O   GLY A 234     139.118 116.360 154.774  1.00 43.23           O  
ATOM   1368  N   THR A 235     137.576 115.497 156.162  1.00 41.71           N  
ATOM   1369  CA  THR A 235     136.474 115.863 155.282  1.00 41.71           C  
ATOM   1370  C   THR A 235     136.146 117.349 155.356  1.00 41.71           C  
ATOM   1371  O   THR A 235     135.673 117.920 154.369  1.00 41.71           O  
ATOM   1372  CB  THR A 235     135.228 115.039 155.614  1.00 41.71           C  
ATOM   1373  OG1 THR A 235     134.920 115.169 157.007  1.00 41.71           O  
ATOM   1374  CG2 THR A 235     135.454 113.572 155.280  1.00 41.71           C  
ATOM   1375  N   ALA A 236     136.381 117.989 156.504  1.00 41.56           N  
ATOM   1376  CA  ALA A 236     136.069 119.410 156.631  1.00 41.56           C  
ATOM   1377  C   ALA A 236     137.057 120.267 155.849  1.00 41.56           C  
ATOM   1378  O   ALA A 236     136.660 121.201 155.144  1.00 41.56           O  
ATOM   1379  CB  ALA A 236     136.051 119.820 158.103  1.00 41.56           C  
ATOM   1380  N   ILE A 237     138.354 119.971 155.966  1.00 42.18           N  
ATOM   1381  CA  ILE A 237     139.353 120.774 155.268  1.00 42.18           C  
ATOM   1382  C   ILE A 237     139.270 120.546 153.764  1.00 42.18           C  
ATOM   1383  O   ILE A 237     139.424 121.483 152.973  1.00 42.18           O  
ATOM   1384  CB  ILE A 237     140.764 120.489 155.819  1.00 42.18           C  
ATOM   1385  CG1 ILE A 237     141.183 119.041 155.559  1.00 42.18           C  
ATOM   1386  CG2 ILE A 237     140.828 120.802 157.306  1.00 42.18           C  
ATOM   1387  CD1 ILE A 237     142.633 118.758 155.882  1.00 42.18           C  
ATOM   1388  N   ALA A 238     139.011 119.307 153.342  1.00 41.19           N  
ATOM   1389  CA  ALA A 238     138.918 119.000 151.922  1.00 41.19           C  
ATOM   1390  C   ALA A 238     137.638 119.521 151.286  1.00 41.19           C  
ATOM   1391  O   ALA A 238     137.522 119.491 150.057  1.00 41.19           O  
ATOM   1392  CB  ALA A 238     139.024 117.491 151.701  1.00 41.19           C  
ATOM   1393  N   ALA A 239     136.680 119.989 152.081  1.00 37.51           N  
ATOM   1394  CA  ALA A 239     135.412 120.488 151.569  1.00 37.51           C  
ATOM   1395  C   ALA A 239     135.246 121.991 151.713  1.00 37.51           C  
ATOM   1396  O   ALA A 239     134.708 122.634 150.809  1.00 37.51           O  
ATOM   1397  CB  ALA A 239     134.246 119.788 152.274  1.00 37.51           C  
ATOM   1398  N   PHE A 240     135.687 122.571 152.826  1.00 37.60           N  
ATOM   1399  CA  PHE A 240     135.479 123.988 153.094  1.00 37.60           C  
ATOM   1400  C   PHE A 240     136.776 124.770 153.217  1.00 37.60           C  
ATOM   1401  O   PHE A 240     136.954 125.774 152.520  1.00 37.60           O  
ATOM   1402  CB  PHE A 240     134.645 124.156 154.373  1.00 37.60           C  
ATOM   1403  CG  PHE A 240     134.483 125.583 154.811  1.00 37.60           C  
ATOM   1404  CD1 PHE A 240     133.604 126.427 154.155  1.00 37.60           C  
ATOM   1405  CD2 PHE A 240     135.206 126.079 155.883  1.00 37.60           C  
ATOM   1406  CE1 PHE A 240     133.451 127.738 154.558  1.00 37.60           C  
ATOM   1407  CE2 PHE A 240     135.058 127.390 156.289  1.00 37.60           C  
ATOM   1408  CZ  PHE A 240     134.180 128.220 155.626  1.00 37.60           C  
ATOM   1409  N   TYR A 241     137.694 124.334 154.081  1.00 38.77           N  
ATOM   1410  CA  TYR A 241     138.850 125.162 154.412  1.00 38.77           C  
ATOM   1411  C   TYR A 241     139.788 125.334 153.222  1.00 38.77           C  
ATOM   1412  O   TYR A 241     140.275 126.441 152.970  1.00 38.77           O  
ATOM   1413  CB  TYR A 241     139.586 124.569 155.612  1.00 38.77           C  
ATOM   1414  CG  TYR A 241     138.788 124.663 156.891  1.00 38.77           C  
ATOM   1415  CD1 TYR A 241     138.517 125.895 157.471  1.00 38.77           C  
ATOM   1416  CD2 TYR A 241     138.289 123.525 157.509  1.00 38.77           C  
ATOM   1417  CE1 TYR A 241     137.781 125.991 158.634  1.00 38.77           C  
ATOM   1418  CE2 TYR A 241     137.551 123.611 158.674  1.00 38.77           C  
ATOM   1419  CZ  TYR A 241     137.300 124.847 159.231  1.00 38.77           C  
ATOM   1420  OH  TYR A 241     136.567 124.941 160.390  1.00 38.77           O  
ATOM   1421  N   MET A 242     140.066 124.257 152.488  1.00 41.03           N  
ATOM   1422  CA  MET A 242     140.899 124.388 151.293  1.00 41.03           C  
ATOM   1423  C   MET A 242     140.246 125.240 150.210  1.00 41.03           C  
ATOM   1424  O   MET A 242     140.925 126.132 149.671  1.00 41.03           O  
ATOM   1425  CB  MET A 242     141.282 123.000 150.767  1.00 41.03           C  
ATOM   1426  CG  MET A 242     142.208 122.216 151.681  1.00 41.03           C  
ATOM   1427  SD  MET A 242     142.616 120.591 151.017  1.00 41.03           S  
ATOM   1428  CE  MET A 242     143.609 119.919 152.348  1.00 41.03           C  
ATOM   1429  N   PRO A 243     138.977 125.032 149.828  1.00 35.30           N  
ATOM   1430  CA  PRO A 243     138.381 125.926 148.819  1.00 35.30           C  
ATOM   1431  C   PRO A 243     138.325 127.384 149.244  1.00 35.30           C  
ATOM   1432  O   PRO A 243     138.484 128.271 148.397  1.00 35.30           O  
ATOM   1433  CB  PRO A 243     136.977 125.336 148.621  1.00 35.30           C  
ATOM   1434  CG  PRO A 243     137.122 123.909 148.985  1.00 35.30           C  
ATOM   1435  CD  PRO A 243     138.081 123.901 150.134  1.00 35.30           C  
ATOM   1436  N   VAL A 244     138.102 127.663 150.530  1.00 35.88           N  
ATOM   1437  CA  VAL A 244     138.034 129.050 150.987  1.00 35.88           C  
ATOM   1438  C   VAL A 244     139.376 129.743 150.791  1.00 35.88           C  
ATOM   1439  O   VAL A 244     139.438 130.892 150.337  1.00 35.88           O  
ATOM   1440  CB  VAL A 244     137.573 129.112 152.455  1.00 35.88           C  
ATOM   1441  CG1 VAL A 244     137.848 130.484 153.045  1.00 35.88           C  
ATOM   1442  CG2 VAL A 244     136.099 128.797 152.553  1.00 35.88           C  
ATOM   1443  N   THR A 245     140.470 129.058 151.128  1.00 33.00           N  
ATOM   1444  CA  THR A 245     141.794 129.650 150.971  1.00 33.00           C  
ATOM   1445  C   THR A 245     142.095 129.953 149.508  1.00 33.00           C  
ATOM   1446  O   THR A 245     142.634 131.017 149.184  1.00 33.00           O  
ATOM   1447  CB  THR A 245     142.856 128.719 151.556  1.00 33.00           C  
ATOM   1448  OG1 THR A 245     142.562 128.464 152.934  1.00 33.00           O  
ATOM   1449  CG2 THR A 245     144.236 129.347 151.448  1.00 33.00           C  
ATOM   1450  N   ILE A 246     141.747 129.031 148.609  1.00 33.13           N  
ATOM   1451  CA  ILE A 246     142.046 129.226 147.194  1.00 33.13           C  
ATOM   1452  C   ILE A 246     141.178 130.331 146.605  1.00 33.13           C  
ATOM   1453  O   ILE A 246     141.662 131.191 145.872  1.00 33.13           O  
ATOM   1454  CB  ILE A 246     141.879 127.902 146.428  1.00 33.13           C  
ATOM   1455  CG1 ILE A 246     142.802 126.832 147.012  1.00 33.13           C  
ATOM   1456  CG2 ILE A 246     142.164 128.101 144.953  1.00 33.13           C  
ATOM   1457  CD1 ILE A 246     142.369 125.417 146.707  1.00 33.13           C  
ATOM   1458  N   MET A 247     139.881 130.331 146.919  1.00 34.29           N  
ATOM   1459  CA  MET A 247     138.988 131.351 146.373  1.00 34.29           C  
ATOM   1460  C   MET A 247     139.372 132.745 146.853  1.00 34.29           C  
ATOM   1461  O   MET A 247     139.361 133.703 146.072  1.00 34.29           O  
ATOM   1462  CB  MET A 247     137.539 131.038 146.745  1.00 34.29           C  
ATOM   1463  CG  MET A 247     136.987 129.779 146.100  1.00 34.29           C  
ATOM   1464  SD  MET A 247     135.307 129.407 146.633  1.00 34.29           S  
ATOM   1465  CE  MET A 247     134.395 130.717 145.823  1.00 34.29           C  
ATOM   1466  N   THR A 248     139.707 132.882 148.138  1.00 33.44           N  
ATOM   1467  CA  THR A 248     140.110 134.182 148.662  1.00 33.44           C  
ATOM   1468  C   THR A 248     141.405 134.662 148.018  1.00 33.44           C  
ATOM   1469  O   THR A 248     141.543 135.846 147.690  1.00 33.44           O  
ATOM   1470  CB  THR A 248     140.263 134.111 150.182  1.00 33.44           C  
ATOM   1471  OG1 THR A 248     139.053 133.611 150.762  1.00 33.44           O  
ATOM   1472  CG2 THR A 248     140.560 135.489 150.754  1.00 33.44           C  
ATOM   1473  N   ILE A 249     142.368 133.757 147.834  1.00 31.77           N  
ATOM   1474  CA  ILE A 249     143.631 134.126 147.203  1.00 31.77           C  
ATOM   1475  C   ILE A 249     143.408 134.527 145.750  1.00 31.77           C  
ATOM   1476  O   ILE A 249     143.962 135.526 145.275  1.00 31.77           O  
ATOM   1477  CB  ILE A 249     144.641 132.970 147.326  1.00 31.77           C  
ATOM   1478  CG1 ILE A 249     145.217 132.911 148.741  1.00 31.77           C  
ATOM   1479  CG2 ILE A 249     145.757 133.114 146.304  1.00 31.77           C  
ATOM   1480  CD1 ILE A 249     145.956 131.627 149.041  1.00 31.77           C  
ATOM   1481  N   LEU A 250     142.594 133.761 145.022  1.00 31.59           N  
ATOM   1482  CA  LEU A 250     142.390 134.028 143.602  1.00 31.59           C  
ATOM   1483  C   LEU A 250     141.656 135.345 143.378  1.00 31.59           C  
ATOM   1484  O   LEU A 250     141.985 136.093 142.450  1.00 31.59           O  
ATOM   1485  CB  LEU A 250     141.631 132.871 142.957  1.00 31.59           C  
ATOM   1486  CG  LEU A 250     142.455 131.619 142.658  1.00 31.59           C  
ATOM   1487  CD1 LEU A 250     142.826 130.893 143.927  1.00 31.59           C  
ATOM   1488  CD2 LEU A 250     141.704 130.700 141.714  1.00 31.59           C  
ATOM   1489  N   TYR A 251     140.656 135.644 144.208  1.00 31.81           N  
ATOM   1490  CA  TYR A 251     139.909 136.886 144.038  1.00 31.81           C  
ATOM   1491  C   TYR A 251     140.707 138.099 144.494  1.00 31.81           C  
ATOM   1492  O   TYR A 251     140.526 139.193 143.950  1.00 31.81           O  
ATOM   1493  CB  TYR A 251     138.578 136.808 144.784  1.00 31.81           C  
ATOM   1494  CG  TYR A 251     137.515 136.044 144.029  1.00 31.81           C  
ATOM   1495  CD1 TYR A 251     137.278 136.296 142.685  1.00 31.81           C  
ATOM   1496  CD2 TYR A 251     136.756 135.065 144.654  1.00 31.81           C  
ATOM   1497  CE1 TYR A 251     136.313 135.600 141.987  1.00 31.81           C  
ATOM   1498  CE2 TYR A 251     135.788 134.364 143.963  1.00 31.81           C  
ATOM   1499  CZ  TYR A 251     135.571 134.636 142.630  1.00 31.81           C  
ATOM   1500  OH  TYR A 251     134.607 133.940 141.938  1.00 31.81           O  
ATOM   1501  N   TRP A 252     141.578 137.934 145.491  1.00 33.86           N  
ATOM   1502  CA  TRP A 252     142.516 138.998 145.831  1.00 33.86           C  
ATOM   1503  C   TRP A 252     143.499 139.238 144.693  1.00 33.86           C  
ATOM   1504  O   TRP A 252     143.842 140.387 144.393  1.00 33.86           O  
ATOM   1505  CB  TRP A 252     143.253 138.653 147.125  1.00 33.86           C  
ATOM   1506  CG  TRP A 252     144.379 139.585 147.461  1.00 33.86           C  
ATOM   1507  CD1 TRP A 252     145.694 139.258 147.605  1.00 33.86           C  
ATOM   1508  CD2 TRP A 252     144.287 140.994 147.704  1.00 33.86           C  
ATOM   1509  NE1 TRP A 252     146.429 140.374 147.918  1.00 33.86           N  
ATOM   1510  CE2 TRP A 252     145.588 141.454 147.985  1.00 33.86           C  
ATOM   1511  CE3 TRP A 252     143.232 141.912 147.709  1.00 33.86           C  
ATOM   1512  CZ2 TRP A 252     145.863 142.789 148.269  1.00 33.86           C  
ATOM   1513  CZ3 TRP A 252     143.507 143.237 147.991  1.00 33.86           C  
ATOM   1514  CH2 TRP A 252     144.812 143.663 148.267  1.00 33.86           C  
ATOM   1515  N   ARG A 253     143.963 138.164 144.048  1.00 34.48           N  
ATOM   1516  CA  ARG A 253     144.809 138.312 142.869  1.00 34.48           C  
ATOM   1517  C   ARG A 253     144.046 138.968 141.725  1.00 34.48           C  
ATOM   1518  O   ARG A 253     144.609 139.775 140.975  1.00 34.48           O  
ATOM   1519  CB  ARG A 253     145.352 136.951 142.438  1.00 34.48           C  
ATOM   1520  CG  ARG A 253     146.508 136.436 143.277  1.00 34.48           C  
ATOM   1521  CD  ARG A 253     146.880 135.020 142.867  1.00 34.48           C  
ATOM   1522  NE  ARG A 253     147.926 134.451 143.707  1.00 34.48           N  
ATOM   1523  CZ  ARG A 253     149.212 134.417 143.383  1.00 34.48           C  
ATOM   1524  NH1 ARG A 253     149.651 134.919 142.241  1.00 34.48           N  
ATOM   1525  NH2 ARG A 253     150.079 133.863 144.227  1.00 34.48           N  
ATOM   1526  N   ILE A 254     142.767 138.622 141.566  1.00 32.99           N  
ATOM   1527  CA  ILE A 254     141.948 139.230 140.521  1.00 32.99           C  
ATOM   1528  C   ILE A 254     141.802 140.727 140.761  1.00 32.99           C  
ATOM   1529  O   ILE A 254     141.897 141.534 139.828  1.00 32.99           O  
ATOM   1530  CB  ILE A 254     140.579 138.529 140.442  1.00 32.99           C  
ATOM   1531  CG1 ILE A 254     140.680 137.250 139.611  1.00 32.99           C  
ATOM   1532  CG2 ILE A 254     139.525 139.456 139.857  1.00 32.99           C  
ATOM   1533  CD1 ILE A 254     139.389 136.469 139.539  1.00 32.99           C  
ATOM   1534  N   TYR A 255     141.576 141.123 142.016  1.00 37.82           N  
ATOM   1535  CA  TYR A 255     141.405 142.539 142.326  1.00 37.82           C  
ATOM   1536  C   TYR A 255     142.678 143.327 142.047  1.00 37.82           C  
ATOM   1537  O   TYR A 255     142.618 144.477 141.599  1.00 37.82           O  
ATOM   1538  CB  TYR A 255     140.978 142.715 143.783  1.00 37.82           C  
ATOM   1539  CG  TYR A 255     140.806 144.162 144.187  1.00 37.82           C  
ATOM   1540  CD1 TYR A 255     139.658 144.864 143.849  1.00 37.82           C  
ATOM   1541  CD2 TYR A 255     141.795 144.828 144.898  1.00 37.82           C  
ATOM   1542  CE1 TYR A 255     139.497 146.187 144.212  1.00 37.82           C  
ATOM   1543  CE2 TYR A 255     141.644 146.149 145.264  1.00 37.82           C  
ATOM   1544  CZ  TYR A 255     140.493 146.824 144.919  1.00 37.82           C  
ATOM   1545  OH  TYR A 255     140.337 148.141 145.282  1.00 37.82           O  
ATOM   1546  N   LYS A 256     143.842 142.730 142.315  1.00 39.75           N  
ATOM   1547  CA  LYS A 256     145.101 143.436 142.107  1.00 39.75           C  
ATOM   1548  C   LYS A 256     145.351 143.763 140.641  1.00 39.75           C  
ATOM   1549  O   LYS A 256     146.135 144.672 140.347  1.00 39.75           O  
ATOM   1550  CB  LYS A 256     146.266 142.614 142.660  1.00 39.75           C  
ATOM   1551  CG  LYS A 256     146.322 142.562 144.178  1.00 39.75           C  
ATOM   1552  CD  LYS A 256     147.629 141.954 144.662  1.00 39.75           C  
ATOM   1553  CE  LYS A 256     148.110 140.858 143.725  1.00 39.75           C  
ATOM   1554  NZ  LYS A 256     149.204 140.047 144.325  1.00 39.75           N  
ATOM   1555  N   GLU A 257     144.706 143.051 139.717  1.00 43.38           N  
ATOM   1556  CA  GLU A 257     144.861 143.324 138.296  1.00 43.38           C  
ATOM   1557  C   GLU A 257     143.767 144.216 137.729  1.00 43.38           C  
ATOM   1558  O   GLU A 257     144.001 144.883 136.715  1.00 43.38           O  
ATOM   1559  CB  GLU A 257     144.900 142.012 137.504  1.00 43.38           C  
ATOM   1560  CG  GLU A 257     146.132 141.170 137.782  1.00 43.38           C  
ATOM   1561  CD  GLU A 257     146.136 139.875 137.003  1.00 43.38           C  
ATOM   1562  OE1 GLU A 257     145.119 139.578 136.344  1.00 43.38           O  
ATOM   1563  OE2 GLU A 257     147.157 139.157 137.046  1.00 43.38           O  
ATOM   1564  N   THR A 258     142.584 144.239 138.344  1.00 44.78           N  
ATOM   1565  CA  THR A 258     141.549 145.172 137.910  1.00 44.78           C  
ATOM   1566  C   THR A 258     141.938 146.609 138.235  1.00 44.78           C  
ATOM   1567  O   THR A 258     141.701 147.520 137.434  1.00 44.78           O  
ATOM   1568  CB  THR A 258     140.212 144.813 138.556  1.00 44.78           C  
ATOM   1569  OG1 THR A 258     139.842 143.481 138.178  1.00 44.78           O  
ATOM   1570  CG2 THR A 258     139.124 145.774 138.104  1.00 44.78           C  
ATOM   1571  N   GLU A 259     142.540 146.831 139.406  1.00 48.86           N  
ATOM   1572  CA  GLU A 259     143.050 148.158 139.733  1.00 48.86           C  
ATOM   1573  C   GLU A 259     144.286 148.497 138.910  1.00 48.86           C  
ATOM   1574  O   GLU A 259     144.519 149.670 138.598  1.00 48.86           O  
ATOM   1575  CB  GLU A 259     143.362 148.251 141.227  1.00 48.86           C  
ATOM   1576  CG  GLU A 259     144.322 147.187 141.733  1.00 48.86           C  
ATOM   1577  CD  GLU A 259     144.915 147.528 143.087  1.00 48.86           C  
ATOM   1578  OE1 GLU A 259     144.330 148.372 143.799  1.00 48.86           O  
ATOM   1579  OE2 GLU A 259     145.966 146.952 143.439  1.00 48.86           O  
ATOM   1580  N   LYS A 260     145.087 147.491 138.557  1.00 52.72           N  
ATOM   1581  CA  LYS A 260     146.266 147.731 137.732  1.00 52.72           C  
ATOM   1582  C   LYS A 260     145.876 148.139 136.318  1.00 52.72           C  
ATOM   1583  O   LYS A 260     146.539 148.983 135.704  1.00 52.72           O  
ATOM   1584  CB  LYS A 260     147.148 146.483 137.710  1.00 52.72           C  
ATOM   1585  CG  LYS A 260     148.543 146.706 137.156  1.00 52.72           C  
ATOM   1586  CD  LYS A 260     149.298 145.391 137.053  1.00 52.72           C  
ATOM   1587  CE  LYS A 260     149.513 144.775 138.426  1.00 52.72           C  
ATOM   1588  NZ  LYS A 260     150.183 143.448 138.349  1.00 52.72           N  
ATOM   1589  N   ARG A 261     144.807 147.545 135.781  1.00 56.02           N  
ATOM   1590  CA  ARG A 261     144.360 147.891 134.436  1.00 56.02           C  
ATOM   1591  C   ARG A 261     143.890 149.339 134.368  1.00 56.02           C  
ATOM   1592  O   ARG A 261     144.276 150.088 133.464  1.00 56.02           O  
ATOM   1593  CB  ARG A 261     143.246 146.940 133.997  1.00 56.02           C  
ATOM   1594  CG  ARG A 261     142.464 147.414 132.785  1.00 56.02           C  
ATOM   1595  CD  ARG A 261     141.033 147.772 133.154  1.00 56.02           C  
ATOM   1596  NE  ARG A 261     140.169 147.837 131.981  1.00 56.02           N  
ATOM   1597  CZ  ARG A 261     138.902 148.227 132.003  1.00 56.02           C  
ATOM   1598  NH1 ARG A 261     138.315 148.607 133.126  1.00 56.02           N  
ATOM   1599  NH2 ARG A 261     138.206 148.235 130.870  1.00 56.02           N  
ATOM   1600  N   THR A 262     143.059 149.754 135.326  1.00 58.51           N  
ATOM   1601  CA  THR A 262     142.570 151.128 135.340  1.00 58.51           C  
ATOM   1602  C   THR A 262     143.646 152.119 135.759  1.00 58.51           C  
ATOM   1603  O   THR A 262     143.491 153.321 135.515  1.00 58.51           O  
ATOM   1604  CB  THR A 262     141.361 151.252 136.269  1.00 58.51           C  
ATOM   1605  OG1 THR A 262     141.746 150.918 137.609  1.00 58.51           O  
ATOM   1606  CG2 THR A 262     140.246 150.320 135.819  1.00 58.51           C  
ATOM   1607  N   LYS A 263     144.724 151.648 136.390  1.00 63.55           N  
ATOM   1608  CA  LYS A 263     145.832 152.537 136.721  1.00 63.55           C  
ATOM   1609  C   LYS A 263     146.641 152.886 135.479  1.00 63.55           C  
ATOM   1610  O   LYS A 263     147.051 154.039 135.301  1.00 63.55           O  
ATOM   1611  CB  LYS A 263     146.721 151.892 137.786  1.00 63.55           C  
ATOM   1612  CG  LYS A 263     147.900 152.743 138.234  1.00 63.55           C  
ATOM   1613  CD  LYS A 263     149.197 152.288 137.581  1.00 63.55           C  
ATOM   1614  CE  LYS A 263     149.637 150.935 138.112  1.00 63.55           C  
ATOM   1615  NZ  LYS A 263     150.897 150.473 137.472  1.00 63.55           N  
ATOM   1616  N   GLU A 264     146.883 151.901 134.611  1.00 66.82           N  
ATOM   1617  CA  GLU A 264     147.604 152.164 133.370  1.00 66.82           C  
ATOM   1618  C   GLU A 264     146.809 153.087 132.455  1.00 66.82           C  
ATOM   1619  O   GLU A 264     147.381 153.973 131.808  1.00 66.82           O  
ATOM   1620  CB  GLU A 264     147.925 150.848 132.661  1.00 66.82           C  
ATOM   1621  CG  GLU A 264     149.152 150.134 133.204  1.00 66.82           C  
ATOM   1622  CD  GLU A 264     149.069 148.628 133.046  1.00 66.82           C  
ATOM   1623  OE1 GLU A 264     148.267 148.160 132.210  1.00 66.82           O  
ATOM   1624  OE2 GLU A 264     149.804 147.912 133.757  1.00 66.82           O  
ATOM   1625  N   LEU A 265     145.496 152.897 132.387  1.00 67.80           N  
ATOM   1626  CA  LEU A 265     144.641 153.728 131.549  1.00 67.80           C  
ATOM   1627  C   LEU A 265     144.257 155.017 132.269  1.00 67.80           C  
ATOM   1628  O   LEU A 265     144.811 156.082 131.995  1.00 67.80           O  
ATOM   1629  CB  LEU A 265     143.384 152.960 131.137  1.00 67.80           C  
ATOM   1630  CG  LEU A 265     143.606 151.560 130.562  1.00 67.80           C  
ATOM   1631  CD1 LEU A 265     142.279 150.847 130.356  1.00 67.80           C  
ATOM   1632  CD2 LEU A 265     144.390 151.631 129.260  1.00 67.80           C  
ATOM   1633  N   GLU A 486     138.091 149.463 140.039  1.00 48.44           N  
ATOM   1634  CA  GLU A 486     138.088 149.305 141.488  1.00 48.44           C  
ATOM   1635  C   GLU A 486     136.765 149.767 142.090  1.00 48.44           C  
ATOM   1636  O   GLU A 486     136.405 149.370 143.199  1.00 48.44           O  
ATOM   1637  CB  GLU A 486     139.252 150.078 142.114  1.00 48.44           C  
ATOM   1638  CG  GLU A 486     139.300 151.549 141.736  1.00 48.44           C  
ATOM   1639  CD  GLU A 486     138.645 152.440 142.772  1.00 48.44           C  
ATOM   1640  OE1 GLU A 486     138.432 151.973 143.911  1.00 48.44           O  
ATOM   1641  OE2 GLU A 486     138.345 153.609 142.450  1.00 48.44           O  
ATOM   1642  N   LYS A 487     136.047 150.618 141.352  1.00 46.27           N  
ATOM   1643  CA  LYS A 487     134.754 151.099 141.828  1.00 46.27           C  
ATOM   1644  C   LYS A 487     133.749 149.960 141.944  1.00 46.27           C  
ATOM   1645  O   LYS A 487     133.007 149.874 142.928  1.00 46.27           O  
ATOM   1646  CB  LYS A 487     134.227 152.190 140.896  1.00 46.27           C  
ATOM   1647  N   LYS A 488     133.712 149.073 140.949  1.00 39.00           N  
ATOM   1648  CA  LYS A 488     132.818 147.924 140.976  1.00 39.00           C  
ATOM   1649  C   LYS A 488     133.521 146.627 141.346  1.00 39.00           C  
ATOM   1650  O   LYS A 488     132.854 145.686 141.790  1.00 39.00           O  
ATOM   1651  CB  LYS A 488     132.132 147.750 139.615  1.00 39.00           C  
ATOM   1652  CG  LYS A 488     130.950 148.674 139.390  1.00 39.00           C  
ATOM   1653  CD  LYS A 488     130.363 148.491 137.999  1.00 39.00           C  
ATOM   1654  CE  LYS A 488     129.767 147.104 137.826  1.00 39.00           C  
ATOM   1655  NZ  LYS A 488     128.605 146.883 138.728  1.00 39.00           N  
ATOM   1656  N   ALA A 489     134.841 146.551 141.168  1.00 38.12           N  
ATOM   1657  CA  ALA A 489     135.572 145.352 141.561  1.00 38.12           C  
ATOM   1658  C   ALA A 489     135.524 145.145 143.068  1.00 38.12           C  
ATOM   1659  O   ALA A 489     135.355 144.016 143.540  1.00 38.12           O  
ATOM   1660  CB  ALA A 489     137.019 145.435 141.077  1.00 38.12           C  
ATOM   1661  N   ALA A 490     135.676 146.222 143.841  1.00 37.90           N  
ATOM   1662  CA  ALA A 490     135.619 146.102 145.294  1.00 37.90           C  
ATOM   1663  C   ALA A 490     134.226 145.699 145.762  1.00 37.90           C  
ATOM   1664  O   ALA A 490     134.087 144.890 146.687  1.00 37.90           O  
ATOM   1665  CB  ALA A 490     136.048 147.415 145.947  1.00 37.90           C  
ATOM   1666  N   GLN A 491     133.185 146.253 145.140  1.00 38.45           N  
ATOM   1667  CA  GLN A 491     131.821 145.930 145.544  1.00 38.45           C  
ATOM   1668  C   GLN A 491     131.457 144.495 145.179  1.00 38.45           C  
ATOM   1669  O   GLN A 491     130.879 143.765 145.991  1.00 38.45           O  
ATOM   1670  CB  GLN A 491     130.839 146.913 144.903  1.00 38.45           C  
ATOM   1671  CG  GLN A 491     129.407 146.775 145.398  1.00 38.45           C  
ATOM   1672  CD  GLN A 491     128.485 146.160 144.361  1.00 38.45           C  
ATOM   1673  OE1 GLN A 491     128.442 146.600 143.212  1.00 38.45           O  
ATOM   1674  NE2 GLN A 491     127.741 145.137 144.763  1.00 38.45           N  
ATOM   1675  N   THR A 492     131.786 144.073 143.956  1.00 35.45           N  
ATOM   1676  CA  THR A 492     131.360 142.757 143.489  1.00 35.45           C  
ATOM   1677  C   THR A 492     132.140 141.638 144.170  1.00 35.45           C  
ATOM   1678  O   THR A 492     131.552 140.640 144.603  1.00 35.45           O  
ATOM   1679  CB  THR A 492     131.509 142.666 141.970  1.00 35.45           C  
ATOM   1680  OG1 THR A 492     130.612 143.592 141.345  1.00 35.45           O  
ATOM   1681  CG2 THR A 492     131.191 141.261 141.483  1.00 35.45           C  
ATOM   1682  N   LEU A 493     133.463 141.783 144.275  1.00 34.81           N  
ATOM   1683  CA  LEU A 493     134.278 140.717 144.850  1.00 34.81           C  
ATOM   1684  C   LEU A 493     133.992 140.535 146.335  1.00 34.81           C  
ATOM   1685  O   LEU A 493     134.002 139.407 146.840  1.00 34.81           O  
ATOM   1686  CB  LEU A 493     135.760 141.003 144.616  1.00 34.81           C  
ATOM   1687  CG  LEU A 493     136.227 140.932 143.161  1.00 34.81           C  
ATOM   1688  CD1 LEU A 493     137.718 141.191 143.061  1.00 34.81           C  
ATOM   1689  CD2 LEU A 493     135.870 139.590 142.546  1.00 34.81           C  
ATOM   1690  N   SER A 494     133.743 141.631 147.054  1.00 36.83           N  
ATOM   1691  CA  SER A 494     133.415 141.526 148.471  1.00 36.83           C  
ATOM   1692  C   SER A 494     132.015 140.972 148.701  1.00 36.83           C  
ATOM   1693  O   SER A 494     131.764 140.374 149.751  1.00 36.83           O  
ATOM   1694  CB  SER A 494     133.552 142.890 149.147  1.00 36.83           C  
ATOM   1695  OG  SER A 494     134.894 143.342 149.119  1.00 36.83           O  
ATOM   1696  N   ALA A 495     131.101 141.159 147.748  1.00 34.88           N  
ATOM   1697  CA  ALA A 495     129.744 140.649 147.902  1.00 34.88           C  
ATOM   1698  C   ALA A 495     129.660 139.149 147.653  1.00 34.88           C  
ATOM   1699  O   ALA A 495     128.830 138.471 148.267  1.00 34.88           O  
ATOM   1700  CB  ALA A 495     128.793 141.389 146.962  1.00 34.88           C  
ATOM   1701  N   ILE A 496     130.497 138.616 146.761  1.00 35.47           N  
ATOM   1702  CA  ILE A 496     130.424 137.192 146.450  1.00 35.47           C  
ATOM   1703  C   ILE A 496     131.176 136.361 147.484  1.00 35.47           C  
ATOM   1704  O   ILE A 496     130.766 135.237 147.796  1.00 35.47           O  
ATOM   1705  CB  ILE A 496     130.945 136.923 145.027  1.00 35.47           C  
ATOM   1706  CG1 ILE A 496     132.408 137.346 144.890  1.00 35.47           C  
ATOM   1707  CG2 ILE A 496     130.093 137.652 144.003  1.00 35.47           C  
ATOM   1708  CD1 ILE A 496     133.045 136.917 143.589  1.00 35.47           C  
ATOM   1709  N   LEU A 497     132.277 136.883 148.029  1.00 35.18           N  
ATOM   1710  CA  LEU A 497     133.038 136.128 149.018  1.00 35.18           C  
ATOM   1711  C   LEU A 497     132.327 136.102 150.365  1.00 35.18           C  
ATOM   1712  O   LEU A 497     132.307 135.069 151.043  1.00 35.18           O  
ATOM   1713  CB  LEU A 497     134.442 136.714 149.161  1.00 35.18           C  
ATOM   1714  CG  LEU A 497     135.527 136.077 148.291  1.00 35.18           C  
ATOM   1715  CD1 LEU A 497     136.859 136.783 148.491  1.00 35.18           C  
ATOM   1716  CD2 LEU A 497     135.654 134.591 148.589  1.00 35.18           C  
ATOM   1717  N   LEU A 498     131.738 137.230 150.771  1.00 36.69           N  
ATOM   1718  CA  LEU A 498     131.030 137.273 152.045  1.00 36.69           C  
ATOM   1719  C   LEU A 498     129.790 136.390 152.031  1.00 36.69           C  
ATOM   1720  O   LEU A 498     129.428 135.820 153.065  1.00 36.69           O  
ATOM   1721  CB  LEU A 498     130.654 138.712 152.393  1.00 36.69           C  
ATOM   1722  CG  LEU A 498     131.788 139.593 152.921  1.00 36.69           C  
ATOM   1723  CD1 LEU A 498     131.308 141.021 153.122  1.00 36.69           C  
ATOM   1724  CD2 LEU A 498     132.350 139.025 154.212  1.00 36.69           C  
ATOM   1725  N   ALA A 499     129.128 136.266 150.878  1.00 35.16           N  
ATOM   1726  CA  ALA A 499     127.980 135.372 150.782  1.00 35.16           C  
ATOM   1727  C   ALA A 499     128.388 133.926 151.031  1.00 35.16           C  
ATOM   1728  O   ALA A 499     127.679 133.181 151.717  1.00 35.16           O  
ATOM   1729  CB  ALA A 499     127.315 135.516 149.414  1.00 35.16           C  
ATOM   1730  N   PHE A 500     129.530 133.510 150.479  1.00 36.62           N  
ATOM   1731  CA  PHE A 500     130.019 132.157 150.720  1.00 36.62           C  
ATOM   1732  C   PHE A 500     130.512 131.991 152.151  1.00 36.62           C  
ATOM   1733  O   PHE A 500     130.282 130.950 152.776  1.00 36.62           O  
ATOM   1734  CB  PHE A 500     131.131 131.820 149.728  1.00 36.62           C  
ATOM   1735  CG  PHE A 500     131.609 130.401 149.814  1.00 36.62           C  
ATOM   1736  CD1 PHE A 500     130.842 129.366 149.309  1.00 36.62           C  
ATOM   1737  CD2 PHE A 500     132.826 130.100 150.400  1.00 36.62           C  
ATOM   1738  CE1 PHE A 500     131.278 128.059 149.387  1.00 36.62           C  
ATOM   1739  CE2 PHE A 500     133.268 128.795 150.481  1.00 36.62           C  
ATOM   1740  CZ  PHE A 500     132.493 127.774 149.974  1.00 36.62           C  
ATOM   1741  N   ILE A 501     131.197 133.005 152.684  1.00 36.54           N  
ATOM   1742  CA  ILE A 501     131.772 132.896 154.021  1.00 36.54           C  
ATOM   1743  C   ILE A 501     130.678 132.849 155.081  1.00 36.54           C  
ATOM   1744  O   ILE A 501     130.721 132.022 155.999  1.00 36.54           O  
ATOM   1745  CB  ILE A 501     132.756 134.053 154.271  1.00 36.54           C  
ATOM   1746  CG1 ILE A 501     134.050 133.832 153.485  1.00 36.54           C  
ATOM   1747  CG2 ILE A 501     133.050 134.202 155.756  1.00 36.54           C  
ATOM   1748  CD1 ILE A 501     134.957 135.041 153.451  1.00 36.54           C  
ATOM   1749  N   ILE A 502     129.678 133.726 154.972  1.00 36.47           N  
ATOM   1750  CA  ILE A 502     128.669 133.840 156.022  1.00 36.47           C  
ATOM   1751  C   ILE A 502     127.808 132.583 156.090  1.00 36.47           C  
ATOM   1752  O   ILE A 502     127.469 132.107 157.180  1.00 36.47           O  
ATOM   1753  CB  ILE A 502     127.818 135.105 155.806  1.00 36.47           C  
ATOM   1754  CG1 ILE A 502     128.639 136.357 156.122  1.00 36.47           C  
ATOM   1755  CG2 ILE A 502     126.563 135.070 156.664  1.00 36.47           C  
ATOM   1756  CD1 ILE A 502     127.948 137.649 155.751  1.00 36.47           C  
ATOM   1757  N   THR A 503     127.450 132.018 154.941  1.00 35.99           N  
ATOM   1758  CA  THR A 503     126.507 130.908 154.891  1.00 35.99           C  
ATOM   1759  C   THR A 503     127.162 129.540 155.041  1.00 35.99           C  
ATOM   1760  O   THR A 503     126.456 128.529 154.988  1.00 35.99           O  
ATOM   1761  CB  THR A 503     125.713 130.945 153.579  1.00 35.99           C  
ATOM   1762  OG1 THR A 503     126.601 130.748 152.473  1.00 35.99           O  
ATOM   1763  CG2 THR A 503     124.998 132.279 153.424  1.00 35.99           C  
ATOM   1764  N   TRP A 504     128.479 129.472 155.226  1.00 37.22           N  
ATOM   1765  CA  TRP A 504     129.146 128.179 155.311  1.00 37.22           C  
ATOM   1766  C   TRP A 504     130.008 128.057 156.562  1.00 37.22           C  
ATOM   1767  O   TRP A 504     130.222 126.950 157.065  1.00 37.22           O  
ATOM   1768  CB  TRP A 504     129.996 127.940 154.062  1.00 37.22           C  
ATOM   1769  CG  TRP A 504     129.234 127.335 152.923  1.00 37.22           C  
ATOM   1770  CD1 TRP A 504     128.837 127.962 151.780  1.00 37.22           C  
ATOM   1771  CD2 TRP A 504     128.775 125.982 152.819  1.00 37.22           C  
ATOM   1772  NE1 TRP A 504     128.160 127.084 150.972  1.00 37.22           N  
ATOM   1773  CE2 TRP A 504     128.107 125.863 151.584  1.00 37.22           C  
ATOM   1774  CE3 TRP A 504     128.864 124.861 153.649  1.00 37.22           C  
ATOM   1775  CZ2 TRP A 504     127.532 124.668 151.159  1.00 37.22           C  
ATOM   1776  CZ3 TRP A 504     128.291 123.675 153.225  1.00 37.22           C  
ATOM   1777  CH2 TRP A 504     127.635 123.588 151.992  1.00 37.22           C  
ATOM   1778  N   THR A 505     130.515 129.183 157.063  1.00 37.77           N  
ATOM   1779  CA  THR A 505     131.402 129.146 158.226  1.00 37.77           C  
ATOM   1780  C   THR A 505     130.737 128.601 159.486  1.00 37.77           C  
ATOM   1781  O   THR A 505     131.354 127.757 160.158  1.00 37.77           O  
ATOM   1782  CB  THR A 505     131.988 130.540 158.475  1.00 37.77           C  
ATOM   1783  OG1 THR A 505     132.411 131.110 157.231  1.00 37.77           O  
ATOM   1784  CG2 THR A 505     133.175 130.457 159.418  1.00 37.77           C  
ATOM   1785  N   PRO A 506     129.526 129.029 159.880  1.00 38.24           N  
ATOM   1786  CA  PRO A 506     128.978 128.545 161.161  1.00 38.24           C  
ATOM   1787  C   PRO A 506     128.864 127.034 161.256  1.00 38.24           C  
ATOM   1788  O   PRO A 506     129.132 126.467 162.322  1.00 38.24           O  
ATOM   1789  CB  PRO A 506     127.603 129.223 161.224  1.00 38.24           C  
ATOM   1790  CG  PRO A 506     127.773 130.454 160.426  1.00 38.24           C  
ATOM   1791  CD  PRO A 506     128.634 130.035 159.275  1.00 38.24           C  
ATOM   1792  N   TYR A 507     128.477 126.358 160.172  1.00 38.31           N  
ATOM   1793  CA  TYR A 507     128.386 124.903 160.221  1.00 38.31           C  
ATOM   1794  C   TYR A 507     129.765 124.267 160.337  1.00 38.31           C  
ATOM   1795  O   TYR A 507     129.951 123.313 161.099  1.00 38.31           O  
ATOM   1796  CB  TYR A 507     127.657 124.369 158.989  1.00 38.31           C  
ATOM   1797  CG  TYR A 507     127.765 122.869 158.833  1.00 38.31           C  
ATOM   1798  CD1 TYR A 507     126.984 122.014 159.600  1.00 38.31           C  
ATOM   1799  CD2 TYR A 507     128.654 122.306 157.927  1.00 38.31           C  
ATOM   1800  CE1 TYR A 507     127.083 120.643 159.466  1.00 38.31           C  
ATOM   1801  CE2 TYR A 507     128.761 120.937 157.787  1.00 38.31           C  
ATOM   1802  CZ  TYR A 507     127.973 120.110 158.559  1.00 38.31           C  
ATOM   1803  OH  TYR A 507     128.074 118.746 158.420  1.00 38.31           O  
ATOM   1804  N   ASN A 508     130.743 124.782 159.592  1.00 38.44           N  
ATOM   1805  CA  ASN A 508     132.084 124.214 159.617  1.00 38.44           C  
ATOM   1806  C   ASN A 508     132.839 124.535 160.898  1.00 38.44           C  
ATOM   1807  O   ASN A 508     133.874 123.913 161.157  1.00 38.44           O  
ATOM   1808  CB  ASN A 508     132.880 124.698 158.406  1.00 38.44           C  
ATOM   1809  CG  ASN A 508     132.561 123.914 157.153  1.00 38.44           C  
ATOM   1810  OD1 ASN A 508     131.830 124.384 156.282  1.00 38.44           O  
ATOM   1811  ND2 ASN A 508     133.103 122.707 157.058  1.00 38.44           N  
ATOM   1812  N   ILE A 509     132.357 125.482 161.696  1.00 40.83           N  
ATOM   1813  CA  ILE A 509     132.952 125.749 163.001  1.00 40.83           C  
ATOM   1814  C   ILE A 509     132.309 124.891 164.082  1.00 40.83           C  
ATOM   1815  O   ILE A 509     133.002 124.347 164.945  1.00 40.83           O  
ATOM   1816  CB  ILE A 509     132.843 127.251 163.333  1.00 40.83           C  
ATOM   1817  CG1 ILE A 509     133.715 128.072 162.382  1.00 40.83           C  
ATOM   1818  CG2 ILE A 509     133.238 127.515 164.777  1.00 40.83           C  
ATOM   1819  CD1 ILE A 509     135.176 127.691 162.412  1.00 40.83           C  
ATOM   1820  N   MET A 510     130.982 124.749 164.043  1.00 42.51           N  
ATOM   1821  CA  MET A 510     130.293 123.948 165.048  1.00 42.51           C  
ATOM   1822  C   MET A 510     130.561 122.459 164.871  1.00 42.51           C  
ATOM   1823  O   MET A 510     130.573 121.715 165.858  1.00 42.51           O  
ATOM   1824  CB  MET A 510     128.791 124.224 165.003  1.00 42.51           C  
ATOM   1825  CG  MET A 510     128.408 125.625 165.440  1.00 42.51           C  
ATOM   1826  SD  MET A 510     126.626 125.875 165.481  1.00 42.51           S  
ATOM   1827  CE  MET A 510     126.245 125.825 163.736  1.00 42.51           C  
ATOM   1828  N   VAL A 511     130.769 122.004 163.634  1.00 41.34           N  
ATOM   1829  CA  VAL A 511     131.018 120.583 163.409  1.00 41.34           C  
ATOM   1830  C   VAL A 511     132.356 120.172 164.011  1.00 41.34           C  
ATOM   1831  O   VAL A 511     132.498 119.061 164.532  1.00 41.34           O  
ATOM   1832  CB  VAL A 511     130.928 120.245 161.908  1.00 41.34           C  
ATOM   1833  CG1 VAL A 511     132.069 120.879 161.125  1.00 41.34           C  
ATOM   1834  CG2 VAL A 511     130.911 118.738 161.703  1.00 41.34           C  
ATOM   1835  N   LEU A 512     133.356 121.056 163.959  1.00 43.49           N  
ATOM   1836  CA  LEU A 512     134.649 120.739 164.557  1.00 43.49           C  
ATOM   1837  C   LEU A 512     134.570 120.752 166.077  1.00 43.49           C  
ATOM   1838  O   LEU A 512     135.186 119.912 166.744  1.00 43.49           O  
ATOM   1839  CB  LEU A 512     135.713 121.722 164.067  1.00 43.49           C  
ATOM   1840  CG  LEU A 512     135.982 121.784 162.561  1.00 43.49           C  
ATOM   1841  CD1 LEU A 512     137.357 122.373 162.295  1.00 43.49           C  
ATOM   1842  CD2 LEU A 512     135.849 120.413 161.914  1.00 43.49           C  
ATOM   1843  N   VAL A 513     133.822 121.701 166.642  1.00 44.88           N  
ATOM   1844  CA  VAL A 513     133.651 121.757 168.089  1.00 44.88           C  
ATOM   1845  C   VAL A 513     132.862 120.549 168.579  1.00 44.88           C  
ATOM   1846  O   VAL A 513     133.137 120.004 169.654  1.00 44.88           O  
ATOM   1847  CB  VAL A 513     132.977 123.082 168.491  1.00 44.88           C  
ATOM   1848  CG1 VAL A 513     132.607 123.076 169.966  1.00 44.88           C  
ATOM   1849  CG2 VAL A 513     133.888 124.255 168.172  1.00 44.88           C  
ATOM   1850  N   ASN A 514     131.880 120.104 167.791  1.00 48.60           N  
ATOM   1851  CA  ASN A 514     131.028 118.995 168.207  1.00 48.60           C  
ATOM   1852  C   ASN A 514     131.820 117.709 168.405  1.00 48.60           C  
ATOM   1853  O   ASN A 514     131.446 116.874 169.236  1.00 48.60           O  
ATOM   1854  CB  ASN A 514     129.918 118.781 167.178  1.00 48.60           C  
ATOM   1855  CG  ASN A 514     128.739 118.017 167.742  1.00 48.60           C  
ATOM   1856  OD1 ASN A 514     128.421 116.919 167.286  1.00 48.60           O  
ATOM   1857  ND2 ASN A 514     128.083 118.595 168.740  1.00 48.60           N  
ATOM   1858  N   THR A 515     132.905 117.523 167.651  1.00 49.03           N  
ATOM   1859  CA  THR A 515     133.708 116.314 167.798  1.00 49.03           C  
ATOM   1860  C   THR A 515     134.472 116.313 169.116  1.00 49.03           C  
ATOM   1861  O   THR A 515     134.467 115.316 169.848  1.00 49.03           O  
ATOM   1862  CB  THR A 515     134.674 116.182 166.622  1.00 49.03           C  
ATOM   1863  OG1 THR A 515     135.741 117.128 166.771  1.00 49.03           O  
ATOM   1864  CG2 THR A 515     133.952 116.461 165.330  1.00 49.03           C  
ATOM   1865  N   PHE A 516     135.138 117.423 169.436  1.00 54.75           N  
ATOM   1866  CA  PHE A 516     135.905 117.489 170.675  1.00 54.75           C  
ATOM   1867  C   PHE A 516     134.990 117.605 171.886  1.00 54.75           C  
ATOM   1868  O   PHE A 516     135.219 116.950 172.910  1.00 54.75           O  
ATOM   1869  CB  PHE A 516     136.883 118.662 170.622  1.00 54.75           C  
ATOM   1870  CG  PHE A 516     138.224 118.305 170.050  1.00 54.75           C  
ATOM   1871  CD1 PHE A 516     139.207 117.748 170.850  1.00 54.75           C  
ATOM   1872  CD2 PHE A 516     138.499 118.522 168.712  1.00 54.75           C  
ATOM   1873  CE1 PHE A 516     140.442 117.417 170.326  1.00 54.75           C  
ATOM   1874  CE2 PHE A 516     139.731 118.193 168.182  1.00 54.75           C  
ATOM   1875  CZ  PHE A 516     140.704 117.640 168.990  1.00 54.75           C  
ATOM   1876  N   CYS A 517     133.952 118.430 171.790  1.00 59.10           N  
ATOM   1877  CA  CYS A 517     133.002 118.596 172.876  1.00 59.10           C  
ATOM   1878  C   CYS A 517     131.991 117.451 172.866  1.00 59.10           C  
ATOM   1879  O   CYS A 517     131.999 116.586 171.987  1.00 59.10           O  
ATOM   1880  CB  CYS A 517     132.309 119.950 172.765  1.00 59.10           C  
ATOM   1881  SG  CYS A 517     131.152 120.310 174.095  1.00 59.10           S  
ATOM   1882  N   ASP A 518     131.107 117.440 173.863  1.00 65.56           N  
ATOM   1883  CA  ASP A 518     130.102 116.392 173.988  1.00 65.56           C  
ATOM   1884  C   ASP A 518     128.685 116.922 173.807  1.00 65.56           C  
ATOM   1885  O   ASP A 518     127.963 116.458 172.920  1.00 65.56           O  
ATOM   1886  CB  ASP A 518     130.242 115.697 175.350  1.00 65.56           C  
ATOM   1887  N   SER A 519     128.263 117.890 174.626  1.00 67.50           N  
ATOM   1888  CA  SER A 519     126.900 118.403 174.542  1.00 67.50           C  
ATOM   1889  C   SER A 519     126.838 119.909 174.774  1.00 67.50           C  
ATOM   1890  O   SER A 519     125.805 120.427 175.210  1.00 67.50           O  
ATOM   1891  CB  SER A 519     125.984 117.688 175.538  1.00 67.50           C  
ATOM   1892  OG  SER A 519     126.493 117.783 176.856  1.00 67.50           O  
ATOM   1893  N   CYS A 520     127.924 120.629 174.492  1.00 65.80           N  
ATOM   1894  CA  CYS A 520     127.934 122.069 174.720  1.00 65.80           C  
ATOM   1895  C   CYS A 520     127.350 122.862 173.560  1.00 65.80           C  
ATOM   1896  O   CYS A 520     127.148 124.073 173.702  1.00 65.80           O  
ATOM   1897  CB  CYS A 520     129.357 122.553 175.005  1.00 65.80           C  
ATOM   1898  SG  CYS A 520     130.533 122.200 173.691  1.00 65.80           S  
ATOM   1899  N   ILE A 521     127.076 122.223 172.428  1.00 57.84           N  
ATOM   1900  CA  ILE A 521     126.461 122.884 171.282  1.00 57.84           C  
ATOM   1901  C   ILE A 521     124.955 122.650 171.361  1.00 57.84           C  
ATOM   1902  O   ILE A 521     124.519 121.491 171.282  1.00 57.84           O  
ATOM   1903  CB  ILE A 521     127.030 122.365 169.957  1.00 57.84           C  
ATOM   1904  CG1 ILE A 521     128.444 122.905 169.737  1.00 57.84           C  
ATOM   1905  CG2 ILE A 521     126.129 122.763 168.796  1.00 57.84           C  
ATOM   1906  CD1 ILE A 521     128.497 124.399 169.506  1.00 57.84           C  
ATOM   1907  N   PRO A 522     124.143 123.693 171.531  1.00 52.45           N  
ATOM   1908  CA  PRO A 522     122.692 123.492 171.604  1.00 52.45           C  
ATOM   1909  C   PRO A 522     122.135 122.940 170.301  1.00 52.45           C  
ATOM   1910  O   PRO A 522     122.664 123.190 169.216  1.00 52.45           O  
ATOM   1911  CB  PRO A 522     122.152 124.897 171.894  1.00 52.45           C  
ATOM   1912  CG  PRO A 522     123.313 125.645 172.466  1.00 52.45           C  
ATOM   1913  CD  PRO A 522     124.522 125.092 171.780  1.00 52.45           C  
ATOM   1914  N   LYS A 523     121.051 122.171 170.425  1.00 50.03           N  
ATOM   1915  CA  LYS A 523     120.415 121.587 169.249  1.00 50.03           C  
ATOM   1916  C   LYS A 523     119.864 122.665 168.325  1.00 50.03           C  
ATOM   1917  O   LYS A 523     119.956 122.547 167.098  1.00 50.03           O  
ATOM   1918  CB  LYS A 523     119.305 120.627 169.679  1.00 50.03           C  
ATOM   1919  CG  LYS A 523     118.590 119.940 168.528  1.00 50.03           C  
ATOM   1920  CD  LYS A 523     119.497 118.943 167.827  1.00 50.03           C  
ATOM   1921  CE  LYS A 523     118.747 118.182 166.748  1.00 50.03           C  
ATOM   1922  NZ  LYS A 523     119.635 117.248 166.005  1.00 50.03           N  
ATOM   1923  N   THR A 524     119.280 123.720 168.897  1.00 46.90           N  
ATOM   1924  CA  THR A 524     118.754 124.811 168.081  1.00 46.90           C  
ATOM   1925  C   THR A 524     119.868 125.515 167.315  1.00 46.90           C  
ATOM   1926  O   THR A 524     119.707 125.849 166.136  1.00 46.90           O  
ATOM   1927  CB  THR A 524     117.996 125.805 168.962  1.00 46.90           C  
ATOM   1928  OG1 THR A 524     116.888 125.144 169.587  1.00 46.90           O  
ATOM   1929  CG2 THR A 524     117.478 126.971 168.134  1.00 46.90           C  
ATOM   1930  N   PHE A 525     121.008 125.746 167.969  1.00 48.40           N  
ATOM   1931  CA  PHE A 525     122.120 126.418 167.304  1.00 48.40           C  
ATOM   1932  C   PHE A 525     122.706 125.555 166.194  1.00 48.40           C  
ATOM   1933  O   PHE A 525     123.122 126.074 165.152  1.00 48.40           O  
ATOM   1934  CB  PHE A 525     123.197 126.788 168.324  1.00 48.40           C  
ATOM   1935  CG  PHE A 525     122.909 128.056 169.077  1.00 48.40           C  
ATOM   1936  CD1 PHE A 525     121.743 128.193 169.812  1.00 48.40           C  
ATOM   1937  CD2 PHE A 525     123.804 129.111 169.049  1.00 48.40           C  
ATOM   1938  CE1 PHE A 525     121.475 129.356 170.505  1.00 48.40           C  
ATOM   1939  CE2 PHE A 525     123.542 130.279 169.741  1.00 48.40           C  
ATOM   1940  CZ  PHE A 525     122.375 130.401 170.469  1.00 48.40           C  
ATOM   1941  N   TRP A 526     122.760 124.238 166.403  1.00 43.27           N  
ATOM   1942  CA  TRP A 526     123.267 123.346 165.366  1.00 43.27           C  
ATOM   1943  C   TRP A 526     122.363 123.351 164.139  1.00 43.27           C  
ATOM   1944  O   TRP A 526     122.851 123.340 163.002  1.00 43.27           O  
ATOM   1945  CB  TRP A 526     123.413 121.927 165.914  1.00 43.27           C  
ATOM   1946  CG  TRP A 526     123.762 120.921 164.864  1.00 43.27           C  
ATOM   1947  CD1 TRP A 526     122.899 120.113 164.186  1.00 43.27           C  
ATOM   1948  CD2 TRP A 526     125.070 120.620 164.366  1.00 43.27           C  
ATOM   1949  NE1 TRP A 526     123.587 119.326 163.297  1.00 43.27           N  
ATOM   1950  CE2 TRP A 526     124.923 119.617 163.388  1.00 43.27           C  
ATOM   1951  CE3 TRP A 526     126.352 121.099 164.653  1.00 43.27           C  
ATOM   1952  CZ2 TRP A 526     126.007 119.085 162.696  1.00 43.27           C  
ATOM   1953  CZ3 TRP A 526     127.426 120.570 163.965  1.00 43.27           C  
ATOM   1954  CH2 TRP A 526     127.248 119.574 162.998  1.00 43.27           C  
ATOM   1955  N   ASN A 527     121.045 123.358 164.348  1.00 42.54           N  
ATOM   1956  CA  ASN A 527     120.114 123.321 163.225  1.00 42.54           C  
ATOM   1957  C   ASN A 527     120.213 124.583 162.376  1.00 42.54           C  
ATOM   1958  O   ASN A 527     120.129 124.515 161.145  1.00 42.54           O  
ATOM   1959  CB  ASN A 527     118.686 123.127 163.733  1.00 42.54           C  
ATOM   1960  CG  ASN A 527     118.375 121.679 164.062  1.00 42.54           C  
ATOM   1961  OD1 ASN A 527     118.866 120.763 163.405  1.00 42.54           O  
ATOM   1962  ND2 ASN A 527     117.555 121.467 165.085  1.00 42.54           N  
ATOM   1963  N   LEU A 528     120.380 125.744 163.015  1.00 38.83           N  
ATOM   1964  CA  LEU A 528     120.462 126.993 162.265  1.00 38.83           C  
ATOM   1965  C   LEU A 528     121.678 127.003 161.346  1.00 38.83           C  
ATOM   1966  O   LEU A 528     121.583 127.417 160.185  1.00 38.83           O  
ATOM   1967  CB  LEU A 528     120.496 128.183 163.227  1.00 38.83           C  
ATOM   1968  CG  LEU A 528     120.406 129.604 162.657  1.00 38.83           C  
ATOM   1969  CD1 LEU A 528     119.812 130.539 163.693  1.00 38.83           C  
ATOM   1970  CD2 LEU A 528     121.764 130.133 162.201  1.00 38.83           C  
ATOM   1971  N   GLY A 529     122.829 126.555 161.848  1.00 37.38           N  
ATOM   1972  CA  GLY A 529     124.002 126.451 160.996  1.00 37.38           C  
ATOM   1973  C   GLY A 529     123.827 125.423 159.897  1.00 37.38           C  
ATOM   1974  O   GLY A 529     124.315 125.606 158.778  1.00 37.38           O  
ATOM   1975  N   TYR A 530     123.139 124.322 160.202  1.00 37.18           N  
ATOM   1976  CA  TYR A 530     122.801 123.344 159.174  1.00 37.18           C  
ATOM   1977  C   TYR A 530     121.894 123.957 158.115  1.00 37.18           C  
ATOM   1978  O   TYR A 530     122.086 123.732 156.914  1.00 37.18           O  
ATOM   1979  CB  TYR A 530     122.136 122.128 159.820  1.00 37.18           C  
ATOM   1980  CG  TYR A 530     122.222 120.854 159.013  1.00 37.18           C  
ATOM   1981  CD1 TYR A 530     121.373 120.632 157.937  1.00 37.18           C  
ATOM   1982  CD2 TYR A 530     123.141 119.866 159.336  1.00 37.18           C  
ATOM   1983  CE1 TYR A 530     121.443 119.467 157.201  1.00 37.18           C  
ATOM   1984  CE2 TYR A 530     123.219 118.697 158.605  1.00 37.18           C  
ATOM   1985  CZ  TYR A 530     122.368 118.502 157.538  1.00 37.18           C  
ATOM   1986  OH  TYR A 530     122.440 117.340 156.806  1.00 37.18           O  
ATOM   1987  N   TRP A 531     120.902 124.741 158.541  1.00 39.92           N  
ATOM   1988  CA  TRP A 531     119.999 125.379 157.590  1.00 39.92           C  
ATOM   1989  C   TRP A 531     120.681 126.512 156.833  1.00 39.92           C  
ATOM   1990  O   TRP A 531     120.330 126.781 155.678  1.00 39.92           O  
ATOM   1991  CB  TRP A 531     118.756 125.902 158.311  1.00 39.92           C  
ATOM   1992  CG  TRP A 531     117.874 126.720 157.428  1.00 39.92           C  
ATOM   1993  CD1 TRP A 531     117.707 128.073 157.462  1.00 39.92           C  
ATOM   1994  CD2 TRP A 531     117.050 126.240 156.361  1.00 39.92           C  
ATOM   1995  NE1 TRP A 531     116.823 128.465 156.486  1.00 39.92           N  
ATOM   1996  CE2 TRP A 531     116.405 127.357 155.796  1.00 39.92           C  
ATOM   1997  CE3 TRP A 531     116.791 124.973 155.831  1.00 39.92           C  
ATOM   1998  CZ2 TRP A 531     115.519 127.245 154.729  1.00 39.92           C  
ATOM   1999  CZ3 TRP A 531     115.912 124.864 154.772  1.00 39.92           C  
ATOM   2000  CH2 TRP A 531     115.292 125.995 154.228  1.00 39.92           C  
ATOM   2001  N   LEU A 532     121.647 127.186 157.460  1.00 36.67           N  
ATOM   2002  CA  LEU A 532     122.304 128.323 156.826  1.00 36.67           C  
ATOM   2003  C   LEU A 532     123.094 127.925 155.587  1.00 36.67           C  
ATOM   2004  O   LEU A 532     123.318 128.768 154.713  1.00 36.67           O  
ATOM   2005  CB  LEU A 532     123.225 129.020 157.828  1.00 36.67           C  
ATOM   2006  CG  LEU A 532     123.432 130.522 157.637  1.00 36.67           C  
ATOM   2007  CD1 LEU A 532     122.097 131.244 157.597  1.00 36.67           C  
ATOM   2008  CD2 LEU A 532     124.317 131.083 158.738  1.00 36.67           C  
ATOM   2009  N   CYS A 533     123.526 126.666 155.493  1.00 35.96           N  
ATOM   2010  CA  CYS A 533     124.269 126.226 154.317  1.00 35.96           C  
ATOM   2011  C   CYS A 533     123.401 126.264 153.066  1.00 35.96           C  
ATOM   2012  O   CYS A 533     123.886 126.594 151.978  1.00 35.96           O  
ATOM   2013  CB  CYS A 533     124.822 124.820 154.543  1.00 35.96           C  
ATOM   2014  SG  CYS A 533     126.050 124.710 155.857  1.00 35.96           S  
ATOM   2015  N   TYR A 534     122.117 125.928 153.203  1.00 36.05           N  
ATOM   2016  CA  TYR A 534     121.210 125.926 152.062  1.00 36.05           C  
ATOM   2017  C   TYR A 534     120.985 127.320 151.490  1.00 36.05           C  
ATOM   2018  O   TYR A 534     120.511 127.439 150.355  1.00 36.05           O  
ATOM   2019  CB  TYR A 534     119.871 125.309 152.464  1.00 36.05           C  
ATOM   2020  CG  TYR A 534     119.969 123.874 152.931  1.00 36.05           C  
ATOM   2021  CD1 TYR A 534     120.794 122.968 152.282  1.00 36.05           C  
ATOM   2022  CD2 TYR A 534     119.234 123.425 154.019  1.00 36.05           C  
ATOM   2023  CE1 TYR A 534     120.885 121.657 152.702  1.00 36.05           C  
ATOM   2024  CE2 TYR A 534     119.318 122.116 154.447  1.00 36.05           C  
ATOM   2025  CZ  TYR A 534     120.145 121.236 153.785  1.00 36.05           C  
ATOM   2026  OH  TYR A 534     120.233 119.930 154.207  1.00 36.05           O  
ATOM   2027  N   ILE A 535     121.308 128.372 152.247  1.00 36.17           N  
ATOM   2028  CA  ILE A 535     121.129 129.733 151.750  1.00 36.17           C  
ATOM   2029  C   ILE A 535     122.074 130.017 150.592  1.00 36.17           C  
ATOM   2030  O   ILE A 535     121.765 130.832 149.714  1.00 36.17           O  
ATOM   2031  CB  ILE A 535     121.317 130.748 152.893  1.00 36.17           C  
ATOM   2032  CG1 ILE A 535     120.521 130.314 154.123  1.00 36.17           C  
ATOM   2033  CG2 ILE A 535     120.885 132.137 152.456  1.00 36.17           C  
ATOM   2034  CD1 ILE A 535     119.039 130.201 153.875  1.00 36.17           C  
ATOM   2035  N   ASN A 536     123.236 129.360 150.566  1.00 36.12           N  
ATOM   2036  CA  ASN A 536     124.190 129.581 149.484  1.00 36.12           C  
ATOM   2037  C   ASN A 536     123.602 129.180 148.138  1.00 36.12           C  
ATOM   2038  O   ASN A 536     123.868 129.826 147.118  1.00 36.12           O  
ATOM   2039  CB  ASN A 536     125.480 128.809 149.761  1.00 36.12           C  
ATOM   2040  CG  ASN A 536     126.587 129.155 148.785  1.00 36.12           C  
ATOM   2041  OD1 ASN A 536     127.701 128.642 148.885  1.00 36.12           O  
ATOM   2042  ND2 ASN A 536     126.289 130.030 147.835  1.00 36.12           N  
ATOM   2043  N   SER A 537     122.804 128.110 148.112  1.00 35.69           N  
ATOM   2044  CA  SER A 537     122.142 127.709 146.875  1.00 35.69           C  
ATOM   2045  C   SER A 537     121.140 128.762 146.418  1.00 35.69           C  
ATOM   2046  O   SER A 537     120.993 129.005 145.215  1.00 35.69           O  
ATOM   2047  CB  SER A 537     121.455 126.358 147.063  1.00 35.69           C  
ATOM   2048  OG  SER A 537     122.405 125.310 147.118  1.00 35.69           O  
ATOM   2049  N   THR A 538     120.432 129.384 147.362  1.00 35.95           N  
ATOM   2050  CA  THR A 538     119.504 130.456 147.015  1.00 35.95           C  
ATOM   2051  C   THR A 538     120.239 131.663 146.444  1.00 35.95           C  
ATOM   2052  O   THR A 538     119.783 132.274 145.470  1.00 35.95           O  
ATOM   2053  CB  THR A 538     118.691 130.859 148.247  1.00 35.95           C  
ATOM   2054  OG1 THR A 538     117.900 129.749 148.686  1.00 35.95           O  
ATOM   2055  CG2 THR A 538     117.778 132.031 147.934  1.00 35.95           C  
ATOM   2056  N   VAL A 539     121.385 132.011 147.030  1.00 36.51           N  
ATOM   2057  CA  VAL A 539     122.098 133.229 146.662  1.00 36.51           C  
ATOM   2058  C   VAL A 539     123.013 133.041 145.452  1.00 36.51           C  
ATOM   2059  O   VAL A 539     123.297 134.019 144.745  1.00 36.51           O  
ATOM   2060  CB  VAL A 539     122.874 133.733 147.897  1.00 36.51           C  
ATOM   2061  CG1 VAL A 539     123.858 134.831 147.545  1.00 36.51           C  
ATOM   2062  CG2 VAL A 539     121.900 134.219 148.962  1.00 36.51           C  
ATOM   2063  N   ASN A 540     123.442 131.810 145.169  1.00 35.95           N  
ATOM   2064  CA  ASN A 540     124.381 131.576 144.072  1.00 35.95           C  
ATOM   2065  C   ASN A 540     123.918 132.113 142.719  1.00 35.95           C  
ATOM   2066  O   ASN A 540     124.754 132.699 142.009  1.00 35.95           O  
ATOM   2067  CB  ASN A 540     124.694 130.077 143.974  1.00 35.95           C  
ATOM   2068  CG  ASN A 540     125.923 129.686 144.768  1.00 35.95           C  
ATOM   2069  OD1 ASN A 540     126.696 130.542 145.198  1.00 35.95           O  
ATOM   2070  ND2 ASN A 540     126.108 128.387 144.969  1.00 35.95           N  
ATOM   2071  N   PRO A 541     122.660 131.952 142.290  1.00 37.51           N  
ATOM   2072  CA  PRO A 541     122.261 132.538 140.998  1.00 37.51           C  
ATOM   2073  C   PRO A 541     122.341 134.055 140.961  1.00 37.51           C  
ATOM   2074  O   PRO A 541     122.347 134.633 139.868  1.00 37.51           O  
ATOM   2075  CB  PRO A 541     120.816 132.051 140.814  1.00 37.51           C  
ATOM   2076  CG  PRO A 541     120.362 131.660 142.171  1.00 37.51           C  
ATOM   2077  CD  PRO A 541     121.575 131.136 142.862  1.00 37.51           C  
ATOM   2078  N   VAL A 542     122.395 134.719 142.115  1.00 38.14           N  
ATOM   2079  CA  VAL A 542     122.490 136.174 142.132  1.00 38.14           C  
ATOM   2080  C   VAL A 542     123.938 136.626 141.984  1.00 38.14           C  
ATOM   2081  O   VAL A 542     124.228 137.595 141.273  1.00 38.14           O  
ATOM   2082  CB  VAL A 542     121.849 136.729 143.417  1.00 38.14           C  
ATOM   2083  CG1 VAL A 542     122.061 138.233 143.516  1.00 38.14           C  
ATOM   2084  CG2 VAL A 542     120.367 136.389 143.460  1.00 38.14           C  
ATOM   2085  N   CYS A 543     124.868 135.935 142.642  1.00 39.34           N  
ATOM   2086  CA  CYS A 543     126.263 136.354 142.658  1.00 39.34           C  
ATOM   2087  C   CYS A 543     127.045 135.919 141.426  1.00 39.34           C  
ATOM   2088  O   CYS A 543     128.167 136.398 141.231  1.00 39.34           O  
ATOM   2089  CB  CYS A 543     126.955 135.814 143.911  1.00 39.34           C  
ATOM   2090  SG  CYS A 543     126.231 136.380 145.462  1.00 39.34           S  
ATOM   2091  N   TYR A 544     126.500 135.043 140.599  1.00 36.52           N  
ATOM   2092  CA  TYR A 544     127.269 134.548 139.463  1.00 36.52           C  
ATOM   2093  C   TYR A 544     126.547 134.697 138.134  1.00 36.52           C  
ATOM   2094  O   TYR A 544     127.195 134.965 137.119  1.00 36.52           O  
ATOM   2095  CB  TYR A 544     127.648 133.078 139.695  1.00 36.52           C  
ATOM   2096  CG  TYR A 544     128.653 132.892 140.806  1.00 36.52           C  
ATOM   2097  CD1 TYR A 544     130.016 132.911 140.545  1.00 36.52           C  
ATOM   2098  CD2 TYR A 544     128.241 132.713 142.119  1.00 36.52           C  
ATOM   2099  CE1 TYR A 544     130.939 132.749 141.557  1.00 36.52           C  
ATOM   2100  CE2 TYR A 544     129.156 132.550 143.138  1.00 36.52           C  
ATOM   2101  CZ  TYR A 544     130.504 132.569 142.852  1.00 36.52           C  
ATOM   2102  OH  TYR A 544     131.420 132.406 143.865  1.00 36.52           O  
ATOM   2103  N   ALA A 545     125.226 134.531 138.109  1.00 39.48           N  
ATOM   2104  CA  ALA A 545     124.474 134.682 136.870  1.00 39.48           C  
ATOM   2105  C   ALA A 545     124.027 136.123 136.649  1.00 39.48           C  
ATOM   2106  O   ALA A 545     124.176 136.658 135.547  1.00 39.48           O  
ATOM   2107  CB  ALA A 545     123.264 133.744 136.870  1.00 39.48           C  
ATOM   2108  N   LEU A 546     123.489 136.768 137.687  1.00 41.83           N  
ATOM   2109  CA  LEU A 546     123.025 138.145 137.561  1.00 41.83           C  
ATOM   2110  C   LEU A 546     124.159 139.137 137.338  1.00 41.83           C  
ATOM   2111  O   LEU A 546     123.887 140.283 136.968  1.00 41.83           O  
ATOM   2112  CB  LEU A 546     122.223 138.549 138.799  1.00 41.83           C  
ATOM   2113  CG  LEU A 546     120.902 137.808 139.008  1.00 41.83           C  
ATOM   2114  CD1 LEU A 546     120.263 138.190 140.333  1.00 41.83           C  
ATOM   2115  CD2 LEU A 546     119.963 138.108 137.862  1.00 41.83           C  
ATOM   2116  N   CYS A 547     125.411 138.735 137.563  1.00 41.49           N  
ATOM   2117  CA  CYS A 547     126.533 139.603 137.228  1.00 41.49           C  
ATOM   2118  C   CYS A 547     126.609 139.842 135.726  1.00 41.49           C  
ATOM   2119  O   CYS A 547     126.892 140.959 135.279  1.00 41.49           O  
ATOM   2120  CB  CYS A 547     127.838 138.999 137.745  1.00 41.49           C  
ATOM   2121  SG  CYS A 547     128.038 139.100 139.538  1.00 41.49           S  
ATOM   2122  N   ASN A 548     126.364 138.802 134.933  1.00 41.01           N  
ATOM   2123  CA  ASN A 548     126.328 138.947 133.485  1.00 41.01           C  
ATOM   2124  C   ASN A 548     125.082 139.716 133.068  1.00 41.01           C  
ATOM   2125  O   ASN A 548     123.977 139.433 133.540  1.00 41.01           O  
ATOM   2126  CB  ASN A 548     126.352 137.573 132.817  1.00 41.01           C  
ATOM   2127  CG  ASN A 548     126.849 137.625 131.389  1.00 41.01           C  
ATOM   2128  OD1 ASN A 548     126.359 138.407 130.575  1.00 41.01           O  
ATOM   2129  ND2 ASN A 548     127.828 136.787 131.074  1.00 41.01           N  
ATOM   2130  N   LYS A 549     125.260 140.696 132.179  1.00 41.55           N  
ATOM   2131  CA  LYS A 549     124.128 141.480 131.701  1.00 41.55           C  
ATOM   2132  C   LYS A 549     123.247 140.698 130.737  1.00 41.55           C  
ATOM   2133  O   LYS A 549     122.074 141.046 130.569  1.00 41.55           O  
ATOM   2134  CB  LYS A 549     124.620 142.764 131.032  1.00 41.55           C  
ATOM   2135  N   THR A 550     123.783 139.660 130.094  1.00 42.05           N  
ATOM   2136  CA  THR A 550     122.972 138.847 129.196  1.00 42.05           C  
ATOM   2137  C   THR A 550     122.026 137.936 129.971  1.00 42.05           C  
ATOM   2138  O   THR A 550     120.865 137.768 129.581  1.00 42.05           O  
ATOM   2139  CB  THR A 550     123.871 138.026 128.271  1.00 42.05           C  
ATOM   2140  OG1 THR A 550     124.803 138.894 127.618  1.00 42.05           O  
ATOM   2141  CG2 THR A 550     123.038 137.318 127.214  1.00 42.05           C  
ATOM   2142  N   PHE A 551     122.506 137.338 131.065  1.00 40.43           N  
ATOM   2143  CA  PHE A 551     121.627 136.555 131.928  1.00 40.43           C  
ATOM   2144  C   PHE A 551     120.553 137.434 132.556  1.00 40.43           C  
ATOM   2145  O   PHE A 551     119.392 137.025 132.669  1.00 40.43           O  
ATOM   2146  CB  PHE A 551     122.440 135.859 133.019  1.00 40.43           C  
ATOM   2147  CG  PHE A 551     122.817 134.442 132.694  1.00 40.43           C  
ATOM   2148  CD1 PHE A 551     121.883 133.424 132.781  1.00 40.43           C  
ATOM   2149  CD2 PHE A 551     124.111 134.125 132.318  1.00 40.43           C  
ATOM   2150  CE1 PHE A 551     122.230 132.119 132.488  1.00 40.43           C  
ATOM   2151  CE2 PHE A 551     124.464 132.823 132.024  1.00 40.43           C  
ATOM   2152  CZ  PHE A 551     123.522 131.819 132.109  1.00 40.43           C  
ATOM   2153  N   ARG A 552     120.928 138.646 132.974  1.00 43.86           N  
ATOM   2154  CA  ARG A 552     119.976 139.546 133.616  1.00 43.86           C  
ATOM   2155  C   ARG A 552     118.844 139.920 132.669  1.00 43.86           C  
ATOM   2156  O   ARG A 552     117.678 139.985 133.078  1.00 43.86           O  
ATOM   2157  CB  ARG A 552     120.699 140.798 134.109  1.00 43.86           C  
ATOM   2158  CG  ARG A 552     120.004 141.519 135.248  1.00 43.86           C  
ATOM   2159  CD  ARG A 552     120.865 142.653 135.782  1.00 43.86           C  
ATOM   2160  NE  ARG A 552     122.284 142.324 135.746  1.00 43.86           N  
ATOM   2161  CZ  ARG A 552     123.250 143.199 135.500  1.00 43.86           C  
ATOM   2162  NH1 ARG A 552     122.983 144.472 135.258  1.00 43.86           N  
ATOM   2163  NH2 ARG A 552     124.514 142.787 135.496  1.00 43.86           N  
ATOM   2164  N   THR A 553     119.168 140.178 131.401  1.00 44.25           N  
ATOM   2165  CA  THR A 553     118.133 140.484 130.418  1.00 44.25           C  
ATOM   2166  C   THR A 553     117.212 139.290 130.197  1.00 44.25           C  
ATOM   2167  O   THR A 553     115.987 139.447 130.126  1.00 44.25           O  
ATOM   2168  CB  THR A 553     118.777 140.918 129.100  1.00 44.25           C  
ATOM   2169  OG1 THR A 553     119.414 142.190 129.273  1.00 44.25           O  
ATOM   2170  CG2 THR A 553     117.733 141.030 128.000  1.00 44.25           C  
ATOM   2171  N   THR A 554     117.781 138.087 130.098  1.00 45.61           N  
ATOM   2172  CA  THR A 554     116.975 136.904 129.814  1.00 45.61           C  
ATOM   2173  C   THR A 554     116.060 136.547 130.980  1.00 45.61           C  
ATOM   2174  O   THR A 554     114.947 136.053 130.762  1.00 45.61           O  
ATOM   2175  CB  THR A 554     117.878 135.722 129.464  1.00 45.61           C  
ATOM   2176  OG1 THR A 554     118.778 136.104 128.416  1.00 45.61           O  
ATOM   2177  CG2 THR A 554     117.049 134.543 128.987  1.00 45.61           C  
ATOM   2178  N   PHE A 555     116.503 136.784 132.218  1.00 47.47           N  
ATOM   2179  CA  PHE A 555     115.649 136.508 133.369  1.00 47.47           C  
ATOM   2180  C   PHE A 555     114.394 137.370 133.343  1.00 47.47           C  
ATOM   2181  O   PHE A 555     113.290 136.881 133.609  1.00 47.47           O  
ATOM   2182  CB  PHE A 555     116.418 136.736 134.669  1.00 47.47           C  
ATOM   2183  CG  PHE A 555     117.373 135.633 135.012  1.00 47.47           C  
ATOM   2184  CD1 PHE A 555     117.298 134.406 134.381  1.00 47.47           C  
ATOM   2185  CD2 PHE A 555     118.346 135.825 135.973  1.00 47.47           C  
ATOM   2186  CE1 PHE A 555     118.183 133.393 134.703  1.00 47.47           C  
ATOM   2187  CE2 PHE A 555     119.231 134.818 136.298  1.00 47.47           C  
ATOM   2188  CZ  PHE A 555     119.149 133.602 135.662  1.00 47.47           C  
ATOM   2189  N   LYS A 556     114.543 138.657 133.026  1.00 49.78           N  
ATOM   2190  CA  LYS A 556     113.381 139.534 132.935  1.00 49.78           C  
ATOM   2191  C   LYS A 556     112.502 139.176 131.745  1.00 49.78           C  
ATOM   2192  O   LYS A 556     111.283 139.370 131.798  1.00 49.78           O  
ATOM   2193  CB  LYS A 556     113.828 140.994 132.849  1.00 49.78           C  
ATOM   2194  N   MET A 557     113.098 138.663 130.667  1.00 50.97           N  
ATOM   2195  CA  MET A 557     112.307 138.251 129.513  1.00 50.97           C  
ATOM   2196  C   MET A 557     111.383 137.092 129.862  1.00 50.97           C  
ATOM   2197  O   MET A 557     110.213 137.081 129.464  1.00 50.97           O  
ATOM   2198  CB  MET A 557     113.228 137.874 128.352  1.00 50.97           C  
ATOM   2199  N   LEU A 558     111.888 136.106 130.605  1.00 51.92           N  
ATOM   2200  CA  LEU A 558     111.069 134.957 130.975  1.00 51.92           C  
ATOM   2201  C   LEU A 558     110.102 135.287 132.106  1.00 51.92           C  
ATOM   2202  O   LEU A 558     108.970 134.792 132.121  1.00 51.92           O  
ATOM   2203  CB  LEU A 558     111.964 133.782 131.370  1.00 51.92           C  
ATOM   2204  CG  LEU A 558     112.868 133.215 130.275  1.00 51.92           C  
ATOM   2205  CD1 LEU A 558     113.601 131.984 130.774  1.00 51.92           C  
ATOM   2206  CD2 LEU A 558     112.065 132.891 129.026  1.00 51.92           C  
ATOM   2207  N   LEU A 559     110.530 136.115 133.062  1.00 55.96           N  
ATOM   2208  CA  LEU A 559     109.702 136.379 134.236  1.00 55.96           C  
ATOM   2209  C   LEU A 559     108.530 137.295 133.905  1.00 55.96           C  
ATOM   2210  O   LEU A 559     107.404 137.056 134.356  1.00 55.96           O  
ATOM   2211  CB  LEU A 559     110.554 136.981 135.352  1.00 55.96           C  
ATOM   2212  N   LEU A 560     108.768 138.345 133.119  1.00 59.32           N  
ATOM   2213  CA  LEU A 560     107.731 139.334 132.837  1.00 59.32           C  
ATOM   2214  C   LEU A 560     106.840 138.904 131.674  1.00 59.32           C  
ATOM   2215  O   LEU A 560     105.626 138.749 131.837  1.00 59.32           O  
ATOM   2216  CB  LEU A 560     108.370 140.697 132.552  1.00 59.32           C  
ATOM   2217  N   CYS A 561     107.430 138.712 130.497  1.00 63.13           N  
ATOM   2218  CA  CYS A 561     106.697 138.276 129.309  1.00 63.13           C  
ATOM   2219  C   CYS A 561     106.923 136.775 129.163  1.00 63.13           C  
ATOM   2220  O   CYS A 561     107.833 136.332 128.461  1.00 63.13           O  
ATOM   2221  CB  CYS A 561     107.155 139.043 128.074  1.00 63.13           C  
ATOM   2222  SG  CYS A 561     106.922 140.834 128.174  1.00 63.13           S  
ATOM   2223  N   GLN A 562     106.076 135.992 129.830  1.00 65.15           N  
ATOM   2224  CA  GLN A 562     106.271 134.549 129.897  1.00 65.15           C  
ATOM   2225  C   GLN A 562     106.328 133.939 128.502  1.00 65.15           C  
ATOM   2226  O   GLN A 562     105.458 134.188 127.663  1.00 65.15           O  
ATOM   2227  CB  GLN A 562     105.148 133.906 130.710  1.00 65.15           C  
ATOM   2228  CG  GLN A 562     105.324 134.026 132.216  1.00 65.15           C  
ATOM   2229  CD  GLN A 562     104.831 135.353 132.755  1.00 65.15           C  
ATOM   2230  OE1 GLN A 562     104.036 136.041 132.114  1.00 65.15           O  
ATOM   2231  NE2 GLN A 562     105.301 135.722 133.941  1.00 65.15           N  
ATOM   2232  N   CYS A 563     107.360 133.136 128.263  1.00 68.05           N  
ATOM   2233  CA  CYS A 563     107.567 132.505 126.967  1.00 68.05           C  
ATOM   2234  C   CYS A 563     108.102 131.089 127.142  1.00 68.05           C  
ATOM   2235  O   CYS A 563     108.832 130.806 128.092  1.00 68.05           O  
ATOM   2236  CB  CYS A 563     108.531 133.331 126.112  1.00 68.05           C  
ATOM   2237  SG  CYS A 563     107.857 134.901 125.520  1.00 68.05           S  
TER    2238      CYS A 563                                                      
HETATM 2239  C01 IXO A 801     124.851 119.454 153.889  1.00 36.60           C  
HETATM 2240  N02 IXO A 801     125.076 120.509 154.915  1.00 36.60           N  
HETATM 2241  C03 IXO A 801     123.860 121.362 155.009  1.00 36.60           C  
HETATM 2242  C04 IXO A 801     125.317 119.860 156.232  1.00 36.60           C  
HETATM 2243  C05 IXO A 801     126.268 121.349 154.550  1.00 36.60           C  
HETATM 2244  C06 IXO A 801     127.271 120.575 153.816  1.00 36.60           C  
HETATM 2245  C07 IXO A 801     128.088 119.966 153.216  1.00 36.60           C  
HETATM 2246  C08 IXO A 801     129.106 119.232 152.469  1.00 36.60           C  
HETATM 2247  O09 IXO A 801     130.401 119.587 152.957  1.00 36.60           O  
HETATM 2248  C10 IXO A 801     130.712 120.890 152.955  1.00 36.60           C  
HETATM 2249  N11 IXO A 801     130.837 121.671 153.995  1.00 36.60           N  
HETATM 2250  O12 IXO A 801     131.489 122.862 153.564  1.00 36.60           O  
HETATM 2251  C13 IXO A 801     131.465 122.933 152.116  1.00 36.60           C  
HETATM 2252  C14 IXO A 801     130.972 121.578 151.654  1.00 36.60           C  
HETATM 2253  CAA Y01 A 802     139.997 120.638 148.222  1.00 40.99           C  
HETATM 2254  CBA Y01 A 802     140.030 119.621 147.090  1.00 40.99           C  
HETATM 2255  CAB Y01 A 802     139.300 118.356 147.515  1.00 40.99           C  
HETATM 2256  CAN Y01 A 802     141.483 119.248 146.807  1.00 40.99           C  
HETATM 2257  CAJ Y01 A 802     141.721 119.135 145.316  1.00 40.99           C  
HETATM 2258  CAO Y01 A 802     141.489 120.484 144.650  1.00 40.99           C  
HETATM 2259  CBB Y01 A 802     141.246 120.247 143.169  1.00 40.99           C  
HETATM 2260  CAC Y01 A 802     140.049 119.328 142.995  1.00 40.99           C  
HETATM 2261  CBE Y01 A 802     141.022 121.566 142.417  1.00 40.99           C  
HETATM 2262  CAP Y01 A 802     141.825 122.740 143.025  1.00 40.99           C  
HETATM 2263  CAQ Y01 A 802     142.745 123.260 141.922  1.00 40.99           C  
HETATM 2264  CBG Y01 A 802     141.945 122.940 140.670  1.00 40.99           C  
HETATM 2265  CBI Y01 A 802     141.502 121.491 140.943  1.00 40.99           C  
HETATM 2266  CAE Y01 A 802     142.702 120.520 140.830  1.00 40.99           C  
HETATM 2267  CAU Y01 A 802     140.418 121.163 139.918  1.00 40.99           C  
HETATM 2268  CAS Y01 A 802     141.022 121.254 138.517  1.00 40.99           C  
HETATM 2269  CBF Y01 A 802     141.682 122.613 138.220  1.00 40.99           C  
HETATM 2270  CBD Y01 A 802     142.662 123.011 139.334  1.00 40.99           C  
HETATM 2271  CAK Y01 A 802     143.171 124.421 139.088  1.00 40.99           C  
HETATM 2272  CAI Y01 A 802     143.750 124.517 137.728  1.00 40.99           C  
HETATM 2273  CAZ Y01 A 802     143.428 123.699 136.742  1.00 40.99           C  
HETATM 2274  CAV Y01 A 802     144.071 123.877 135.402  1.00 40.99           C  
HETATM 2275  CBH Y01 A 802     142.442 122.571 136.870  1.00 40.99           C  
HETATM 2276  CAD Y01 A 802     143.215 121.253 136.739  1.00 40.99           C  
HETATM 2277  CAT Y01 A 802     141.422 122.683 135.732  1.00 40.99           C  
HETATM 2278  CAR Y01 A 802     142.120 122.729 134.375  1.00 40.99           C  
HETATM 2279  CBC Y01 A 802     142.990 123.985 134.327  1.00 40.99           C  
HETATM 2280  OAW Y01 A 802     143.606 124.040 133.052  1.00 40.99           O  
HETATM 2281  CAY Y01 A 802     144.044 125.278 132.640  1.00 40.99           C  
HETATM 2282  OAG Y01 A 802     143.747 126.244 133.322  1.00 40.99           O  
HETATM 2283  CAM Y01 A 802     144.851 125.308 131.374  1.00 40.99           C  
HETATM 2284  CAL Y01 A 802     143.936 125.749 130.240  1.00 40.99           C  
HETATM 2285  CAX Y01 A 802     142.951 124.649 129.805  1.00 40.99           C  
HETATM 2286  OAH Y01 A 802     143.270 123.961 128.819  1.00 40.99           O  
HETATM 2287  OAF Y01 A 802     141.889 124.523 130.482  1.00 40.99           O  
CONECT  624 1265                                                                
CONECT 1265  624                                                                
CONECT 1881 1898                                                                
CONECT 1898 1881                                                                
CONECT 2239 2240                                                                
CONECT 2240 2239 2241 2242 2243                                                 
CONECT 2241 2240                                                                
CONECT 2242 2240                                                                
CONECT 2243 2240 2244                                                           
CONECT 2244 2243 2245                                                           
CONECT 2245 2244 2246                                                           
CONECT 2246 2245 2247                                                           
CONECT 2247 2246 2248                                                           
CONECT 2248 2247 2249 2252                                                      
CONECT 2249 2248 2250                                                           
CONECT 2250 2249 2251                                                           
CONECT 2251 2250 2252                                                           
CONECT 2252 2248 2251                                                           
CONECT 2253 2254                                                                
CONECT 2254 2253 2255 2256                                                      
CONECT 2255 2254                                                                
CONECT 2256 2254 2257                                                           
CONECT 2257 2256 2258                                                           
CONECT 2258 2257 2259                                                           
CONECT 2259 2258 2260 2261                                                      
CONECT 2260 2259                                                                
CONECT 2261 2259 2262 2265                                                      
CONECT 2262 2261 2263                                                           
CONECT 2263 2262 2264                                                           
CONECT 2264 2263 2265 2270                                                      
CONECT 2265 2261 2264 2266 2267                                                 
CONECT 2266 2265                                                                
CONECT 2267 2265 2268                                                           
CONECT 2268 2267 2269                                                           
CONECT 2269 2268 2270 2275                                                      
CONECT 2270 2264 2269 2271                                                      
CONECT 2271 2270 2272                                                           
CONECT 2272 2271 2273                                                           
CONECT 2273 2272 2274 2275                                                      
CONECT 2274 2273 2279                                                           
CONECT 2275 2269 2273 2276 2277                                                 
CONECT 2276 2275                                                                
CONECT 2277 2275 2278                                                           
CONECT 2278 2277 2279                                                           
CONECT 2279 2274 2278 2280                                                      
CONECT 2280 2279 2281                                                           
CONECT 2281 2280 2282 2283                                                      
CONECT 2282 2281                                                                
CONECT 2283 2281 2284                                                           
CONECT 2284 2283 2285                                                           
CONECT 2285 2284 2286 2287                                                      
CONECT 2286 2285                                                                
CONECT 2287 2285                                                                
MASTER      432    0    2   14    0    0    0    6 2286    1   53   44          
END