HEADER    MEMBRANE PROTEIN                        14-AUG-23   8KEX              
TITLE     CRYOEM STRUCTURE OF GQ COUPLED MRGPRX4 WITH AGONIST DCA-3P, LOCAL     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOLUBLE CYTOCHROME B562,MAS-RELATED G-PROTEIN COUPLED      
COMPND   3 RECEPTOR MEMBER X4,GREEN FLUORESCENT PROTEIN;                        
COMPND   4 CHAIN: E;                                                            
COMPND   5 SYNONYM: CYTOCHROME B-562,SENSORY NEURON-SPECIFIC G-PROTEIN COUPLED  
COMPND   6 RECEPTOR 5/6;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS, AEQUOREA        
SOURCE   3 VICTORIA;                                                            
SOURCE   4 ORGANISM_COMMON: HUMAN, WATER JELLYFISH, MESONEMA VICTORIA;          
SOURCE   5 ORGANISM_TAXID: 562, 9606, 6100;                                     
SOURCE   6 GENE: CYBC, MRGPRX4, MRGX4, SNSR5, SNSR6, GFP;                       
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    MRGPRX4, BILE ACID, CHOLESTATIC ITCH, GPCR, AGONIST, MEMBRANE PROTEIN 
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.YANG,J.P.FAN,X.G.LEI                                                
REVDAT   4   25-DEC-24 8KEX    1       JRNL                                     
REVDAT   3   27-NOV-24 8KEX    1       REMARK                                   
REVDAT   2   13-NOV-24 8KEX    1       JRNL                                     
REVDAT   1   06-NOV-24 8KEX    0                                                
JRNL        AUTH   J.YANG,T.ZHAO,J.FAN,H.ZOU,G.LAN,F.GUO,Y.SHI,H.KE,H.YU,Z.YUE, 
JRNL        AUTH 2 X.WANG,Y.BAI,S.LI,Y.LIU,X.WANG,Y.CHEN,Y.LI,X.LEI             
JRNL        TITL   STRUCTURE-GUIDED DISCOVERY OF BILE ACID DERIVATIVES FOR      
JRNL        TITL 2 TREATING LIVER DISEASES WITHOUT CAUSING ITCH.                
JRNL        REF    CELL                          V. 187  7164 2024              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   39476841                                                     
JRNL        DOI    10.1016/J.CELL.2024.10.001                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 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)  : 3.200                          
REMARK   3   NUMBER OF PARTICLES               : 451859                         
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 8KEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 23-AUG-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300040267.                                   
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                 : CRYO-EM STRUCTURE OF MRGPRX4      
REMARK 245                                    COMPLEX WITH AGONIST DCA-3P       
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      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1100.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2200.00                        
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)  : 6000.00                        
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)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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     ASP E  -115                                                      
REMARK 465     TYR E  -114                                                      
REMARK 465     LYS E  -113                                                      
REMARK 465     ASP E  -112                                                      
REMARK 465     ASP E  -111                                                      
REMARK 465     ASP E  -110                                                      
REMARK 465     ASP E  -109                                                      
REMARK 465     LYS E  -108                                                      
REMARK 465     GLU E  -107                                                      
REMARK 465     PHE E  -106                                                      
REMARK 465     ALA E  -105                                                      
REMARK 465     ASP E  -104                                                      
REMARK 465     LEU E  -103                                                      
REMARK 465     GLU E  -102                                                      
REMARK 465     ASP E  -101                                                      
REMARK 465     ASN E  -100                                                      
REMARK 465     TRP E   -99                                                      
REMARK 465     GLU E   -98                                                      
REMARK 465     THR E   -97                                                      
REMARK 465     LEU E   -96                                                      
REMARK 465     ASN E   -95                                                      
REMARK 465     ASP E   -94                                                      
REMARK 465     ASN E   -93                                                      
REMARK 465     LEU E   -92                                                      
REMARK 465     LYS E   -91                                                      
REMARK 465     VAL E   -90                                                      
REMARK 465     ILE E   -89                                                      
REMARK 465     GLU E   -88                                                      
REMARK 465     LYS E   -87                                                      
REMARK 465     ALA E   -86                                                      
REMARK 465     ASP E   -85                                                      
REMARK 465     ASN E   -84                                                      
REMARK 465     ALA E   -83                                                      
REMARK 465     ALA E   -82                                                      
REMARK 465     GLN E   -81                                                      
REMARK 465     VAL E   -80                                                      
REMARK 465     LYS E   -79                                                      
REMARK 465     ASP E   -78                                                      
REMARK 465     ALA E   -77                                                      
REMARK 465     LEU E   -76                                                      
REMARK 465     THR E   -75                                                      
REMARK 465     LYS E   -74                                                      
REMARK 465     MET E   -73                                                      
REMARK 465     ARG E   -72                                                      
REMARK 465     ALA E   -71                                                      
REMARK 465     ALA E   -70                                                      
REMARK 465     ALA E   -69                                                      
REMARK 465     LEU E   -68                                                      
REMARK 465     ASP E   -67                                                      
REMARK 465     ALA E   -66                                                      
REMARK 465     GLN E   -65                                                      
REMARK 465     LYS E   -64                                                      
REMARK 465     ALA E   -63                                                      
REMARK 465     THR E   -62                                                      
REMARK 465     PRO E   -61                                                      
REMARK 465     PRO E   -60                                                      
REMARK 465     LYS E   -59                                                      
REMARK 465     LEU E   -58                                                      
REMARK 465     GLU E   -57                                                      
REMARK 465     ASP E   -56                                                      
REMARK 465     LYS E   -55                                                      
REMARK 465     SER E   -54                                                      
REMARK 465     PRO E   -53                                                      
REMARK 465     ASP E   -52                                                      
REMARK 465     SER E   -51                                                      
REMARK 465     PRO E   -50                                                      
REMARK 465     GLU E   -49                                                      
REMARK 465     MET E   -48                                                      
REMARK 465     LYS E   -47                                                      
REMARK 465     ASP E   -46                                                      
REMARK 465     PHE E   -45                                                      
REMARK 465     ARG E   -44                                                      
REMARK 465     HIS E   -43                                                      
REMARK 465     GLY E   -42                                                      
REMARK 465     PHE E   -41                                                      
REMARK 465     ASP E   -40                                                      
REMARK 465     ILE E   -39                                                      
REMARK 465     LEU E   -38                                                      
REMARK 465     VAL E   -37                                                      
REMARK 465     GLY E   -36                                                      
REMARK 465     GLN E   -35                                                      
REMARK 465     ILE E   -34                                                      
REMARK 465     ASP E   -33                                                      
REMARK 465     ASP E   -32                                                      
REMARK 465     ALA E   -31                                                      
REMARK 465     LEU E   -30                                                      
REMARK 465     LYS E   -29                                                      
REMARK 465     LEU E   -28                                                      
REMARK 465     ALA E   -27                                                      
REMARK 465     ASN E   -26                                                      
REMARK 465     GLU E   -25                                                      
REMARK 465     GLY E   -24                                                      
REMARK 465     LYS E   -23                                                      
REMARK 465     VAL E   -22                                                      
REMARK 465     LYS E   -21                                                      
REMARK 465     GLU E   -20                                                      
REMARK 465     ALA E   -19                                                      
REMARK 465     GLN E   -18                                                      
REMARK 465     ALA E   -17                                                      
REMARK 465     ALA E   -16                                                      
REMARK 465     ALA E   -15                                                      
REMARK 465     GLU E   -14                                                      
REMARK 465     GLN E   -13                                                      
REMARK 465     LEU E   -12                                                      
REMARK 465     LYS E   -11                                                      
REMARK 465     THR E   -10                                                      
REMARK 465     THR E    -9                                                      
REMARK 465     ARG E    -8                                                      
REMARK 465     ASN E    -7                                                      
REMARK 465     ALA E    -6                                                      
REMARK 465     TYR E    -5                                                      
REMARK 465     ILE E    -4                                                      
REMARK 465     GLN E    -3                                                      
REMARK 465     LYS E    -2                                                      
REMARK 465     TYR E    -1                                                      
REMARK 465     LEU E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ASP E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     VAL E     5                                                      
REMARK 465     PRO E     6                                                      
REMARK 465     VAL E     7                                                      
REMARK 465     PHE E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     THR E    10                                                      
REMARK 465     LYS E    11                                                      
REMARK 465     LEU E    12                                                      
REMARK 465     THR E    13                                                      
REMARK 465     PRO E    14                                                      
REMARK 465     ILE E    15                                                      
REMARK 465     ASN E    16                                                      
REMARK 465     GLY E    17                                                      
REMARK 465     ARG E    18                                                      
REMARK 465     GLU E    19                                                      
REMARK 465     GLU E    20                                                      
REMARK 465     THR E    21                                                      
REMARK 465     SER E   166                                                      
REMARK 465     GLY E   167                                                      
REMARK 465     ALA E   168                                                      
REMARK 465     ASP E   169                                                      
REMARK 465     ARG E   281                                                      
REMARK 465     GLN E   282                                                      
REMARK 465     ASN E   283                                                      
REMARK 465     ARG E   284                                                      
REMARK 465     GLN E   285                                                      
REMARK 465     ASN E   286                                                      
REMARK 465     LEU E   287                                                      
REMARK 465     LYS E   288                                                      
REMARK 465     LEU E   289                                                      
REMARK 465     VAL E   290                                                      
REMARK 465     LEU E   291                                                      
REMARK 465     GLN E   292                                                      
REMARK 465     ARG E   293                                                      
REMARK 465     ALA E   294                                                      
REMARK 465     LEU E   295                                                      
REMARK 465     GLN E   296                                                      
REMARK 465     ASP E   297                                                      
REMARK 465     LYS E   298                                                      
REMARK 465     PRO E   299                                                      
REMARK 465     GLU E   300                                                      
REMARK 465     VAL E   301                                                      
REMARK 465     ASP E   302                                                      
REMARK 465     LYS E   303                                                      
REMARK 465     GLY E   304                                                      
REMARK 465     GLU E   305                                                      
REMARK 465     GLY E   306                                                      
REMARK 465     GLN E   307                                                      
REMARK 465     LEU E   308                                                      
REMARK 465     PRO E   309                                                      
REMARK 465     GLU E   310                                                      
REMARK 465     GLU E   311                                                      
REMARK 465     SER E   312                                                      
REMARK 465     LEU E   313                                                      
REMARK 465     GLU E   314                                                      
REMARK 465     LEU E   315                                                      
REMARK 465     SER E   316                                                      
REMARK 465     GLY E   317                                                      
REMARK 465     SER E   318                                                      
REMARK 465     ARG E   319                                                      
REMARK 465     LEU E   320                                                      
REMARK 465     GLY E   321                                                      
REMARK 465     PRO E   322                                                      
REMARK 465     LEU E   323                                                      
REMARK 465     GLU E   324                                                      
REMARK 465     LEU E   325                                                      
REMARK 465     GLU E   326                                                      
REMARK 465     VAL E   327                                                      
REMARK 465     LEU E   328                                                      
REMARK 465     PHE E   329                                                      
REMARK 465     GLN E   330                                                      
REMARK 465     GLY E   331                                                      
REMARK 465     PRO E   332                                                      
REMARK 465     SER E   333                                                      
REMARK 465     LYS E   334                                                      
REMARK 465     GLY E   335                                                      
REMARK 465     GLU E   336                                                      
REMARK 465     GLU E   337                                                      
REMARK 465     LEU E   338                                                      
REMARK 465     PHE E   339                                                      
REMARK 465     THR E   340                                                      
REMARK 465     GLY E   341                                                      
REMARK 465     VAL E   342                                                      
REMARK 465     VAL E   343                                                      
REMARK 465     PRO E   344                                                      
REMARK 465     ILE E   345                                                      
REMARK 465     LEU E   346                                                      
REMARK 465     VAL E   347                                                      
REMARK 465     GLU E   348                                                      
REMARK 465     LEU E   349                                                      
REMARK 465     ASP E   350                                                      
REMARK 465     GLY E   351                                                      
REMARK 465     ASP E   352                                                      
REMARK 465     VAL E   353                                                      
REMARK 465     ASN E   354                                                      
REMARK 465     GLY E   355                                                      
REMARK 465     HIS E   356                                                      
REMARK 465     LYS E   357                                                      
REMARK 465     PHE E   358                                                      
REMARK 465     SER E   359                                                      
REMARK 465     VAL E   360                                                      
REMARK 465     ARG E   361                                                      
REMARK 465     GLY E   362                                                      
REMARK 465     GLU E   363                                                      
REMARK 465     GLY E   364                                                      
REMARK 465     GLU E   365                                                      
REMARK 465     GLY E   366                                                      
REMARK 465     ASP E   367                                                      
REMARK 465     ALA E   368                                                      
REMARK 465     THR E   369                                                      
REMARK 465     ASN E   370                                                      
REMARK 465     GLY E   371                                                      
REMARK 465     LYS E   372                                                      
REMARK 465     LEU E   373                                                      
REMARK 465     THR E   374                                                      
REMARK 465     LEU E   375                                                      
REMARK 465     LYS E   376                                                      
REMARK 465     PHE E   377                                                      
REMARK 465     ILE E   378                                                      
REMARK 465     CYS E   379                                                      
REMARK 465     THR E   380                                                      
REMARK 465     THR E   381                                                      
REMARK 465     GLY E   382                                                      
REMARK 465     LYS E   383                                                      
REMARK 465     LEU E   384                                                      
REMARK 465     PRO E   385                                                      
REMARK 465     VAL E   386                                                      
REMARK 465     PRO E   387                                                      
REMARK 465     TRP E   388                                                      
REMARK 465     PRO E   389                                                      
REMARK 465     THR E   390                                                      
REMARK 465     LEU E   391                                                      
REMARK 465     VAL E   392                                                      
REMARK 465     THR E   393                                                      
REMARK 465     THR E   394                                                      
REMARK 465     LEU E   395                                                      
REMARK 465     THR E   396                                                      
REMARK 465     TYR E   397                                                      
REMARK 465     GLY E   398                                                      
REMARK 465     VAL E   399                                                      
REMARK 465     GLN E   400                                                      
REMARK 465     CYS E   401                                                      
REMARK 465     PHE E   402                                                      
REMARK 465     SER E   403                                                      
REMARK 465     ARG E   404                                                      
REMARK 465     TYR E   405                                                      
REMARK 465     PRO E   406                                                      
REMARK 465     ASP E   407                                                      
REMARK 465     HIS E   408                                                      
REMARK 465     MET E   409                                                      
REMARK 465     LYS E   410                                                      
REMARK 465     ARG E   411                                                      
REMARK 465     HIS E   412                                                      
REMARK 465     ASP E   413                                                      
REMARK 465     PHE E   414                                                      
REMARK 465     PHE E   415                                                      
REMARK 465     LYS E   416                                                      
REMARK 465     SER E   417                                                      
REMARK 465     ALA E   418                                                      
REMARK 465     MET E   419                                                      
REMARK 465     PRO E   420                                                      
REMARK 465     GLU E   421                                                      
REMARK 465     GLY E   422                                                      
REMARK 465     TYR E   423                                                      
REMARK 465     VAL E   424                                                      
REMARK 465     GLN E   425                                                      
REMARK 465     GLU E   426                                                      
REMARK 465     ARG E   427                                                      
REMARK 465     THR E   428                                                      
REMARK 465     ILE E   429                                                      
REMARK 465     SER E   430                                                      
REMARK 465     PHE E   431                                                      
REMARK 465     LYS E   432                                                      
REMARK 465     ASP E   433                                                      
REMARK 465     ASP E   434                                                      
REMARK 465     GLY E   435                                                      
REMARK 465     THR E   436                                                      
REMARK 465     TYR E   437                                                      
REMARK 465     LYS E   438                                                      
REMARK 465     THR E   439                                                      
REMARK 465     ARG E   440                                                      
REMARK 465     ALA E   441                                                      
REMARK 465     GLU E   442                                                      
REMARK 465     VAL E   443                                                      
REMARK 465     LYS E   444                                                      
REMARK 465     PHE E   445                                                      
REMARK 465     GLU E   446                                                      
REMARK 465     GLY E   447                                                      
REMARK 465     ASP E   448                                                      
REMARK 465     THR E   449                                                      
REMARK 465     LEU E   450                                                      
REMARK 465     VAL E   451                                                      
REMARK 465     ASN E   452                                                      
REMARK 465     ARG E   453                                                      
REMARK 465     ILE E   454                                                      
REMARK 465     GLU E   455                                                      
REMARK 465     LEU E   456                                                      
REMARK 465     LYS E   457                                                      
REMARK 465     GLY E   458                                                      
REMARK 465     ILE E   459                                                      
REMARK 465     ASP E   460                                                      
REMARK 465     PHE E   461                                                      
REMARK 465     LYS E   462                                                      
REMARK 465     GLU E   463                                                      
REMARK 465     ASP E   464                                                      
REMARK 465     GLY E   465                                                      
REMARK 465     ASN E   466                                                      
REMARK 465     ILE E   467                                                      
REMARK 465     LEU E   468                                                      
REMARK 465     GLY E   469                                                      
REMARK 465     HIS E   470                                                      
REMARK 465     LYS E   471                                                      
REMARK 465     LEU E   472                                                      
REMARK 465     GLU E   473                                                      
REMARK 465     TYR E   474                                                      
REMARK 465     ASN E   475                                                      
REMARK 465     PHE E   476                                                      
REMARK 465     ASN E   477                                                      
REMARK 465     SER E   478                                                      
REMARK 465     HIS E   479                                                      
REMARK 465     ASN E   480                                                      
REMARK 465     VAL E   481                                                      
REMARK 465     TYR E   482                                                      
REMARK 465     ILE E   483                                                      
REMARK 465     THR E   484                                                      
REMARK 465     ALA E   485                                                      
REMARK 465     ASP E   486                                                      
REMARK 465     LYS E   487                                                      
REMARK 465     GLN E   488                                                      
REMARK 465     LYS E   489                                                      
REMARK 465     ASN E   490                                                      
REMARK 465     GLY E   491                                                      
REMARK 465     ILE E   492                                                      
REMARK 465     LYS E   493                                                      
REMARK 465     ALA E   494                                                      
REMARK 465     ASN E   495                                                      
REMARK 465     PHE E   496                                                      
REMARK 465     LYS E   497                                                      
REMARK 465     ILE E   498                                                      
REMARK 465     ARG E   499                                                      
REMARK 465     HIS E   500                                                      
REMARK 465     ASN E   501                                                      
REMARK 465     VAL E   502                                                      
REMARK 465     GLU E   503                                                      
REMARK 465     ASP E   504                                                      
REMARK 465     GLY E   505                                                      
REMARK 465     SER E   506                                                      
REMARK 465     VAL E   507                                                      
REMARK 465     GLN E   508                                                      
REMARK 465     LEU E   509                                                      
REMARK 465     ALA E   510                                                      
REMARK 465     ASP E   511                                                      
REMARK 465     HIS E   512                                                      
REMARK 465     TYR E   513                                                      
REMARK 465     GLN E   514                                                      
REMARK 465     GLN E   515                                                      
REMARK 465     ASN E   516                                                      
REMARK 465     THR E   517                                                      
REMARK 465     PRO E   518                                                      
REMARK 465     ILE E   519                                                      
REMARK 465     GLY E   520                                                      
REMARK 465     ASP E   521                                                      
REMARK 465     GLY E   522                                                      
REMARK 465     PRO E   523                                                      
REMARK 465     VAL E   524                                                      
REMARK 465     LEU E   525                                                      
REMARK 465     LEU E   526                                                      
REMARK 465     PRO E   527                                                      
REMARK 465     ASP E   528                                                      
REMARK 465     ASN E   529                                                      
REMARK 465     HIS E   530                                                      
REMARK 465     TYR E   531                                                      
REMARK 465     LEU E   532                                                      
REMARK 465     SER E   533                                                      
REMARK 465     THR E   534                                                      
REMARK 465     GLN E   535                                                      
REMARK 465     SER E   536                                                      
REMARK 465     VAL E   537                                                      
REMARK 465     LEU E   538                                                      
REMARK 465     SER E   539                                                      
REMARK 465     LYS E   540                                                      
REMARK 465     ASP E   541                                                      
REMARK 465     PRO E   542                                                      
REMARK 465     ASN E   543                                                      
REMARK 465     GLU E   544                                                      
REMARK 465     LYS E   545                                                      
REMARK 465     ARG E   546                                                      
REMARK 465     ASP E   547                                                      
REMARK 465     HIS E   548                                                      
REMARK 465     MET E   549                                                      
REMARK 465     VAL E   550                                                      
REMARK 465     LEU E   551                                                      
REMARK 465     LEU E   552                                                      
REMARK 465     GLU E   553                                                      
REMARK 465     PHE E   554                                                      
REMARK 465     VAL E   555                                                      
REMARK 465     THR E   556                                                      
REMARK 465     ALA E   557                                                      
REMARK 465     ALA E   558                                                      
REMARK 465     GLY E   559                                                      
REMARK 465     ILE E   560                                                      
REMARK 465     THR E   561                                                      
REMARK 465     HIS E   562                                                      
REMARK 465     GLY E   563                                                      
REMARK 465     MET E   564                                                      
REMARK 465     ASP E   565                                                      
REMARK 465     GLU E   566                                                      
REMARK 465     TRP E   567                                                      
REMARK 465     SER E   568                                                      
REMARK 465     HIS E   569                                                      
REMARK 465     PRO E   570                                                      
REMARK 465     GLN E   571                                                      
REMARK 465     PHE E   572                                                      
REMARK 465     GLU E   573                                                      
REMARK 465     LYS E   574                                                      
REMARK 465     GLY E   575                                                      
REMARK 465     GLY E   576                                                      
REMARK 465     GLY E   577                                                      
REMARK 465     SER E   578                                                      
REMARK 465     GLY E   579                                                      
REMARK 465     GLY E   580                                                      
REMARK 465     GLY E   581                                                      
REMARK 465     SER E   582                                                      
REMARK 465     GLY E   583                                                      
REMARK 465     GLY E   584                                                      
REMARK 465     SER E   585                                                      
REMARK 465     ALA E   586                                                      
REMARK 465     TRP E   587                                                      
REMARK 465     SER E   588                                                      
REMARK 465     HIS E   589                                                      
REMARK 465     PRO E   590                                                      
REMARK 465     GLN E   591                                                      
REMARK 465     PHE E   592                                                      
REMARK 465     GLU E   593                                                      
REMARK 465     LYS E   594                                                      
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     GLN E  26    CG   CD   OE1  NE2                                  
REMARK 470     VAL E  32    CG1  CG2                                            
REMARK 470     LEU E  33    CG   CD1  CD2                                       
REMARK 470     ILE E  36    CG1  CG2  CD1                                       
REMARK 470     SER E  38    OG                                                  
REMARK 470     MET E  56    CG   SD   CE                                        
REMARK 470     ARG E  57    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE E  73    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER E 154    OG                                                  
REMARK 470     LEU E 156    CG   CD1  CD2                                       
REMARK 470     ARG E 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE E 163    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE E 178    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E 207    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 208    CG   CD   CE   NZ                                   
REMARK 470     MET E 209    CG   SD   CE                                        
REMARK 470     MET E 242    CG   SD   CE                                        
REMARK 470     HIS E 252    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET E 258    CG   SD   CE                                        
REMARK 470     SER E 277    OG                                                  
REMARK 470     PHE E 278    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E 280    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER E   100     NE1  TRP E   158              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU E  42   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    LEU E  98   CA  -  CB  -  CG  ANGL. DEV. =  19.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS E  23      -70.40    -63.42                                   
REMARK 500    TYR E  24      -40.84   -135.11                                   
REMARK 500    ASN E  59      -70.27    -73.45                                   
REMARK 500    ALA E  60      -25.10   -141.20                                   
REMARK 500    HIS E  92       -0.80     71.45                                   
REMARK 500    PHE E 153       12.75     58.07                                   
REMARK 500    PRO E 210       43.65    -87.68                                   
REMARK 500    LEU E 211       46.15    -92.41                                   
REMARK 500    LEU E 246       -9.88     72.03                                   
REMARK 500    GLU E 247     -136.69     37.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET E  209     PRO E  210                  143.71                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-37191   RELATED DB: EMDB                             
REMARK 900 CRYOEM STRUCTURE OF GQ COUPLED MRGPRX4 WITH AGONIST DCA-3P, LOCAL    
DBREF  8KEX E -105     0  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  8KEX E    1   322  UNP    Q96LA9   MRGX4_HUMAN      1    322             
DBREF  8KEX E  333   566  UNP    P42212   GFP_AEQVI        2    235             
SEQADV 8KEX ASP E -115  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX TYR E -114  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX LYS E -113  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX ASP E -112  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX ASP E -111  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX ASP E -110  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX ASP E -109  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX LYS E -108  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX GLU E -107  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX PHE E -106  UNP  P0ABE7              EXPRESSION TAG                 
SEQADV 8KEX TRP E  -99  UNP  P0ABE7    MET    29 CONFLICT                       
SEQADV 8KEX ILE E   -4  UNP  P0ABE7    HIS   124 CONFLICT                       
SEQADV 8KEX LEU E    0  UNP  P0ABE7    ARG   128 CONFLICT                       
SEQADV 8KEX LEU E  323  UNP  Q96LA9              LINKER                         
SEQADV 8KEX GLU E  324  UNP  Q96LA9              LINKER                         
SEQADV 8KEX LEU E  325  UNP  Q96LA9              LINKER                         
SEQADV 8KEX GLU E  326  UNP  Q96LA9              LINKER                         
SEQADV 8KEX VAL E  327  UNP  Q96LA9              LINKER                         
SEQADV 8KEX LEU E  328  UNP  Q96LA9              LINKER                         
SEQADV 8KEX PHE E  329  UNP  Q96LA9              LINKER                         
SEQADV 8KEX GLN E  330  UNP  Q96LA9              LINKER                         
SEQADV 8KEX GLY E  331  UNP  Q96LA9              LINKER                         
SEQADV 8KEX PRO E  332  UNP  Q96LA9              LINKER                         
SEQADV 8KEX ARG E  361  UNP  P42212    SER    30 CONFLICT                       
SEQADV 8KEX ASN E  370  UNP  P42212    TYR    39 CONFLICT                       
SEQADV 8KEX LEU E  395  UNP  P42212    PHE    64 CONFLICT                       
SEQADV 8KEX THR E  396  UNP  P42212    SER    65 CONFLICT                       
SEQADV 8KEX ARG E  411  UNP  P42212    GLN    80 CONFLICT                       
SEQADV 8KEX SER E  430  UNP  P42212    PHE    99 CONFLICT                       
SEQADV 8KEX THR E  436  UNP  P42212    ASN   105 CONFLICT                       
SEQADV 8KEX PHE E  476  UNP  P42212    TYR   145 CONFLICT                       
SEQADV 8KEX THR E  484  UNP  P42212    MET   153 CONFLICT                       
SEQADV 8KEX ALA E  494  UNP  P42212    VAL   163 CONFLICT                       
SEQADV 8KEX VAL E  502  UNP  P42212    ILE   171 CONFLICT                       
SEQADV 8KEX VAL E  537  UNP  P42212    ALA   206 CONFLICT                       
SEQADV 8KEX TRP E  567  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX SER E  568  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX HIS E  569  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX PRO E  570  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLN E  571  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX PHE E  572  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLU E  573  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX LYS E  574  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  575  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  576  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  577  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX SER E  578  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  579  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  580  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  581  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX SER E  582  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  583  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLY E  584  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX SER E  585  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX ALA E  586  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX TRP E  587  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX SER E  588  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX HIS E  589  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX PRO E  590  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLN E  591  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX PHE E  592  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX GLU E  593  UNP  P42212              EXPRESSION TAG                 
SEQADV 8KEX LYS E  594  UNP  P42212              EXPRESSION TAG                 
SEQRES   1 E  710  ASP TYR LYS ASP ASP ASP ASP LYS GLU PHE ALA ASP LEU          
SEQRES   2 E  710  GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL          
SEQRES   3 E  710  ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA          
SEQRES   4 E  710  LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS          
SEQRES   5 E  710  ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER          
SEQRES   6 E  710  PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU          
SEQRES   7 E  710  VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU          
SEQRES   8 E  710  GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU          
SEQRES   9 E  710  LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU MET          
SEQRES  10 E  710  ASP PRO THR VAL PRO VAL PHE GLY THR LYS LEU THR PRO          
SEQRES  11 E  710  ILE ASN GLY ARG GLU GLU THR PRO CYS TYR ASN GLN THR          
SEQRES  12 E  710  LEU SER PHE THR VAL LEU THR CYS ILE ILE SER LEU VAL          
SEQRES  13 E  710  GLY LEU THR GLY ASN ALA VAL VAL LEU TRP LEU LEU GLY          
SEQRES  14 E  710  TYR ARG MET ARG ARG ASN ALA VAL SER ILE TYR ILE LEU          
SEQRES  15 E  710  ASN LEU ALA ALA ALA ASP PHE LEU PHE LEU SER PHE GLN          
SEQRES  16 E  710  ILE ILE ARG LEU PRO LEU ARG LEU ILE ASN ILE SER HIS          
SEQRES  17 E  710  LEU ILE ARG LYS ILE LEU VAL SER VAL MET THR PHE PRO          
SEQRES  18 E  710  TYR PHE THR GLY LEU SER MET LEU SER ALA ILE SER THR          
SEQRES  19 E  710  GLU ARG CYS LEU SER VAL LEU TRP PRO ILE TRP TYR ARG          
SEQRES  20 E  710  CYS ARG ARG PRO THR HIS LEU SER ALA VAL VAL CYS VAL          
SEQRES  21 E  710  LEU LEU TRP GLY LEU SER LEU LEU PHE SER MET LEU GLU          
SEQRES  22 E  710  TRP ARG PHE CYS ASP PHE LEU PHE SER GLY ALA ASP SER          
SEQRES  23 E  710  SER TRP CYS GLU THR SER ASP PHE ILE PRO VAL ALA TRP          
SEQRES  24 E  710  LEU ILE PHE LEU CYS VAL VAL LEU CYS VAL SER SER LEU          
SEQRES  25 E  710  VAL LEU LEU VAL ARG ILE LEU CYS GLY SER ARG LYS MET          
SEQRES  26 E  710  PRO LEU THR ARG LEU TYR VAL THR ILE LEU LEU THR VAL          
SEQRES  27 E  710  LEU VAL PHE LEU LEU CYS GLY LEU PRO PHE GLY ILE LEU          
SEQRES  28 E  710  GLY ALA LEU ILE TYR ARG MET HIS LEU ASN LEU GLU VAL          
SEQRES  29 E  710  LEU TYR CYS HIS VAL TYR LEU VAL CYS MET SER LEU SER          
SEQRES  30 E  710  SER LEU ASN SER SER ALA ASN PRO ILE ILE TYR PHE PHE          
SEQRES  31 E  710  VAL GLY SER PHE ARG GLN ARG GLN ASN ARG GLN ASN LEU          
SEQRES  32 E  710  LYS LEU VAL LEU GLN ARG ALA LEU GLN ASP LYS PRO GLU          
SEQRES  33 E  710  VAL ASP LYS GLY GLU GLY GLN LEU PRO GLU GLU SER LEU          
SEQRES  34 E  710  GLU LEU SER GLY SER ARG LEU GLY PRO LEU GLU LEU GLU          
SEQRES  35 E  710  VAL LEU PHE GLN GLY PRO SER LYS GLY GLU GLU LEU PHE          
SEQRES  36 E  710  THR GLY VAL VAL PRO ILE LEU VAL GLU LEU ASP GLY ASP          
SEQRES  37 E  710  VAL ASN GLY HIS LYS PHE SER VAL ARG GLY GLU GLY GLU          
SEQRES  38 E  710  GLY ASP ALA THR ASN GLY LYS LEU THR LEU LYS PHE ILE          
SEQRES  39 E  710  CYS THR THR GLY LYS LEU PRO VAL PRO TRP PRO THR LEU          
SEQRES  40 E  710  VAL THR THR LEU THR TYR GLY VAL GLN CYS PHE SER ARG          
SEQRES  41 E  710  TYR PRO ASP HIS MET LYS ARG HIS ASP PHE PHE LYS SER          
SEQRES  42 E  710  ALA MET PRO GLU GLY TYR VAL GLN GLU ARG THR ILE SER          
SEQRES  43 E  710  PHE LYS ASP ASP GLY THR TYR LYS THR ARG ALA GLU VAL          
SEQRES  44 E  710  LYS PHE GLU GLY ASP THR LEU VAL ASN ARG ILE GLU LEU          
SEQRES  45 E  710  LYS GLY ILE ASP PHE LYS GLU ASP GLY ASN ILE LEU GLY          
SEQRES  46 E  710  HIS LYS LEU GLU TYR ASN PHE ASN SER HIS ASN VAL TYR          
SEQRES  47 E  710  ILE THR ALA ASP LYS GLN LYS ASN GLY ILE LYS ALA ASN          
SEQRES  48 E  710  PHE LYS ILE ARG HIS ASN VAL GLU ASP GLY SER VAL GLN          
SEQRES  49 E  710  LEU ALA ASP HIS TYR GLN GLN ASN THR PRO ILE GLY ASP          
SEQRES  50 E  710  GLY PRO VAL LEU LEU PRO ASP ASN HIS TYR LEU SER THR          
SEQRES  51 E  710  GLN SER VAL LEU SER LYS ASP PRO ASN GLU LYS ARG ASP          
SEQRES  52 E  710  HIS MET VAL LEU LEU GLU PHE VAL THR ALA ALA GLY ILE          
SEQRES  53 E  710  THR HIS GLY MET ASP GLU TRP SER HIS PRO GLN PHE GLU          
SEQRES  54 E  710  LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER ALA          
SEQRES  55 E  710  TRP SER HIS PRO GLN PHE GLU LYS                              
HET    JW0  E 601      32                                                       
HETNAM     JW0 (4~{R})-4-[(3~{R},5~{R},8~{R},9~{S},10~{S},12~{S},               
HETNAM   2 JW0  13~{R},14~{S},17~{R})-10,13-DIMETHYL-12-OXIDANYL-3-             
HETNAM   3 JW0  PHOSPHONOOXY-2,3,4,5,6,7,8,9,11,12,14,15,16,17-                 
HETNAM   4 JW0  TETRADECAHYDRO-1~{H}-CYCLOPENTA[A]PHENANTHREN-17-               
HETNAM   5 JW0  YL]PENTANOIC ACID                                               
FORMUL   2  JW0    C24 H41 O7 P                                                 
HELIX    1 AA1 THR E   27  ARG E   55  1                                  29    
HELIX    2 AA2 VAL E   61  LEU E   83  1                                  23    
HELIX    3 AA3 PRO E   84  ARG E   86  5                                   3    
HELIX    4 AA4 LEU E   93  TRP E  126  1                                  34    
HELIX    5 AA5 TRP E  126  CYS E  132  1                                   7    
HELIX    6 AA6 HIS E  137  LEU E  152  1                                  16    
HELIX    7 AA7 PHE E  178  CYS E  204  1                                  27    
HELIX    8 AA8 THR E  212  LEU E  227  1                                  16    
HELIX    9 AA9 GLY E  229  MET E  242  1                                  14    
HELIX   10 AB1 HIS E  252  ARG E  279  1                                  28    
SSBOND   1 CYS E   23    CYS E  251                          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 E  22      88.196 141.479 130.736  1.00101.59           N  
ATOM      2  CA  PRO E  22      87.936 141.792 129.328  1.00106.63           C  
ATOM      3  C   PRO E  22      86.837 142.837 129.183  1.00102.55           C  
ATOM      4  O   PRO E  22      85.853 142.772 129.919  1.00 94.34           O  
ATOM      5  CB  PRO E  22      87.492 140.447 128.741  1.00107.91           C  
ATOM      6  CG  PRO E  22      87.905 139.388 129.751  1.00101.36           C  
ATOM      7  CD  PRO E  22      88.548 140.063 130.928  1.00101.25           C  
ATOM      8  N   CYS E  23      87.007 143.793 128.266  1.00103.13           N  
ATOM      9  CA  CYS E  23      86.001 144.839 128.109  1.00103.26           C  
ATOM     10  C   CYS E  23      84.671 144.249 127.657  1.00100.53           C  
ATOM     11  O   CYS E  23      83.701 144.208 128.423  1.00 97.59           O  
ATOM     12  CB  CYS E  23      86.493 145.884 127.105  1.00100.45           C  
ATOM     13  SG  CYS E  23      88.243 146.316 127.256  1.00 96.33           S  
ATOM     14  N   TYR E  24      84.608 143.783 126.411  1.00110.62           N  
ATOM     15  CA  TYR E  24      83.519 142.924 125.965  1.00110.52           C  
ATOM     16  C   TYR E  24      84.067 141.753 125.158  1.00109.04           C  
ATOM     17  O   TYR E  24      83.650 140.607 125.346  1.00108.75           O  
ATOM     18  CB  TYR E  24      82.507 143.729 125.146  1.00109.27           C  
ATOM     19  CG  TYR E  24      81.082 143.545 125.607  1.00107.40           C  
ATOM     20  CD1 TYR E  24      80.640 144.113 126.792  1.00110.71           C  
ATOM     21  CD2 TYR E  24      80.185 142.780 124.872  1.00107.84           C  
ATOM     22  CE1 TYR E  24      79.341 143.940 127.227  1.00113.57           C  
ATOM     23  CE2 TYR E  24      78.881 142.604 125.297  1.00109.60           C  
ATOM     24  CZ  TYR E  24      78.465 143.185 126.478  1.00113.04           C  
ATOM     25  OH  TYR E  24      77.171 143.014 126.912  1.00112.69           O  
ATOM     26  N   ASN E  25      85.053 142.041 124.313  1.00 92.61           N  
ATOM     27  CA  ASN E  25      85.600 141.144 123.297  1.00 92.67           C  
ATOM     28  C   ASN E  25      87.037 141.580 123.020  1.00 92.65           C  
ATOM     29  O   ASN E  25      87.634 142.313 123.816  1.00 93.69           O  
ATOM     30  CB  ASN E  25      84.748 141.163 122.014  1.00 93.45           C  
ATOM     31  CG  ASN E  25      83.359 140.581 122.203  1.00 94.28           C  
ATOM     32  OD1 ASN E  25      83.158 139.651 122.982  1.00 93.73           O  
ATOM     33  ND2 ASN E  25      82.390 141.132 121.482  1.00 93.85           N  
ATOM     34  N   GLN E  26      87.594 141.112 121.899  1.00 68.26           N  
ATOM     35  CA  GLN E  26      88.915 141.527 121.422  1.00 65.03           C  
ATOM     36  C   GLN E  26      90.014 141.177 122.417  1.00 63.13           C  
ATOM     37  O   GLN E  26      91.066 141.820 122.454  1.00 54.74           O  
ATOM     38  CB  GLN E  26      88.946 143.024 121.097  1.00 62.01           C  
ATOM     39  N   THR E  27      89.775 140.149 123.227  1.00 74.67           N  
ATOM     40  CA  THR E  27      90.742 139.687 124.209  1.00 76.96           C  
ATOM     41  C   THR E  27      91.370 138.352 123.853  1.00 77.66           C  
ATOM     42  O   THR E  27      92.550 138.147 124.140  1.00 78.99           O  
ATOM     43  CB  THR E  27      90.083 139.566 125.589  1.00 73.09           C  
ATOM     44  OG1 THR E  27      89.198 140.674 125.796  1.00 69.22           O  
ATOM     45  CG2 THR E  27      91.137 139.555 126.685  1.00 70.37           C  
ATOM     46  N   LEU E  28      90.611 137.447 123.229  1.00 72.51           N  
ATOM     47  CA  LEU E  28      91.113 136.107 122.948  1.00 66.74           C  
ATOM     48  C   LEU E  28      92.296 136.145 121.987  1.00 70.91           C  
ATOM     49  O   LEU E  28      93.323 135.501 122.228  1.00 73.33           O  
ATOM     50  CB  LEU E  28      89.989 135.228 122.394  1.00 67.53           C  
ATOM     51  CG  LEU E  28      89.177 135.705 121.185  1.00 69.94           C  
ATOM     52  CD1 LEU E  28      88.658 134.511 120.403  1.00 73.58           C  
ATOM     53  CD2 LEU E  28      88.021 136.602 121.603  1.00 67.39           C  
ATOM     54  N   SER E  29      92.178 136.905 120.896  1.00 79.73           N  
ATOM     55  CA  SER E  29      93.295 137.024 119.965  1.00 81.40           C  
ATOM     56  C   SER E  29      94.487 137.710 120.615  1.00 79.93           C  
ATOM     57  O   SER E  29      95.639 137.349 120.342  1.00 77.39           O  
ATOM     58  CB  SER E  29      92.860 137.784 118.712  1.00 80.95           C  
ATOM     59  OG  SER E  29      92.366 136.899 117.721  1.00 83.36           O  
ATOM     60  N   PHE E  30      94.229 138.691 121.481  1.00 73.03           N  
ATOM     61  CA  PHE E  30      95.312 139.419 122.131  1.00 70.35           C  
ATOM     62  C   PHE E  30      96.103 138.502 123.057  1.00 70.19           C  
ATOM     63  O   PHE E  30      97.340 138.486 123.029  1.00 75.75           O  
ATOM     64  CB  PHE E  30      94.737 140.607 122.899  1.00 65.27           C  
ATOM     65  CG  PHE E  30      95.567 141.849 122.805  1.00 70.78           C  
ATOM     66  CD1 PHE E  30      96.808 141.924 123.406  1.00 70.66           C  
ATOM     67  CD2 PHE E  30      95.105 142.944 122.094  1.00 68.50           C  
ATOM     68  CE1 PHE E  30      97.565 143.075 123.306  1.00 69.53           C  
ATOM     69  CE2 PHE E  30      95.858 144.093 121.994  1.00 65.02           C  
ATOM     70  CZ  PHE E  30      97.090 144.158 122.601  1.00 66.22           C  
ATOM     71  N   THR E  31      95.403 137.701 123.867  1.00 65.16           N  
ATOM     72  CA  THR E  31      96.114 136.777 124.742  1.00 62.66           C  
ATOM     73  C   THR E  31      96.732 135.630 123.957  1.00 69.09           C  
ATOM     74  O   THR E  31      97.743 135.074 124.387  1.00 73.17           O  
ATOM     75  CB  THR E  31      95.200 136.223 125.837  1.00 68.68           C  
ATOM     76  OG1 THR E  31      95.871 135.150 126.509  1.00 70.49           O  
ATOM     77  CG2 THR E  31      93.925 135.672 125.252  1.00 68.72           C  
ATOM     78  N   VAL E  32      96.159 135.267 122.806  1.00 69.33           N  
ATOM     79  CA  VAL E  32      96.779 134.246 121.965  1.00 65.71           C  
ATOM     80  C   VAL E  32      98.116 134.740 121.426  1.00 61.68           C  
ATOM     81  O   VAL E  32      99.116 134.012 121.431  1.00 57.52           O  
ATOM     82  CB  VAL E  32      95.827 133.838 120.827  1.00 63.96           C  
ATOM     83  N   LEU E  33      98.149 135.986 120.946  1.00 61.88           N  
ATOM     84  CA  LEU E  33      99.408 136.569 120.492  1.00 66.00           C  
ATOM     85  C   LEU E  33     100.404 136.675 121.639  1.00 64.24           C  
ATOM     86  O   LEU E  33     101.595 136.378 121.471  1.00 66.96           O  
ATOM     87  CB  LEU E  33      99.158 137.942 119.869  1.00 64.51           C  
ATOM     88  N   THR E  34      99.929 137.089 122.816  1.00 76.37           N  
ATOM     89  CA  THR E  34     100.799 137.149 123.985  1.00 79.72           C  
ATOM     90  C   THR E  34     101.376 135.776 124.308  1.00 79.73           C  
ATOM     91  O   THR E  34     102.568 135.650 124.603  1.00 77.12           O  
ATOM     92  CB  THR E  34     100.027 137.701 125.184  1.00 76.83           C  
ATOM     93  OG1 THR E  34      99.600 139.039 124.905  1.00 78.90           O  
ATOM     94  CG2 THR E  34     100.904 137.707 126.426  1.00 75.56           C  
ATOM     95  N   CYS E  35     100.546 134.734 124.238  1.00 81.84           N  
ATOM     96  CA  CYS E  35     100.994 133.386 124.566  1.00 79.99           C  
ATOM     97  C   CYS E  35     101.996 132.862 123.546  1.00 79.21           C  
ATOM     98  O   CYS E  35     102.962 132.191 123.914  1.00 81.51           O  
ATOM     99  CB  CYS E  35      99.793 132.448 124.670  1.00 83.38           C  
ATOM    100  SG  CYS E  35      98.832 132.633 126.191  1.00 81.82           S  
ATOM    101  N   ILE E  36     101.777 133.138 122.260  1.00 77.37           N  
ATOM    102  CA  ILE E  36     102.729 132.695 121.241  1.00 83.02           C  
ATOM    103  C   ILE E  36     104.073 133.393 121.428  1.00 84.18           C  
ATOM    104  O   ILE E  36     105.144 132.764 121.359  1.00 81.27           O  
ATOM    105  CB  ILE E  36     102.157 132.934 119.832  1.00 83.35           C  
ATOM    106  N   ILE E  37     104.036 134.708 121.666  1.00 82.22           N  
ATOM    107  CA  ILE E  37     105.266 135.454 121.908  1.00 76.79           C  
ATOM    108  C   ILE E  37     105.963 134.927 123.154  1.00 74.04           C  
ATOM    109  O   ILE E  37     107.190 134.794 123.191  1.00 76.41           O  
ATOM    110  CB  ILE E  37     104.961 136.960 122.013  1.00 70.98           C  
ATOM    111  CG1 ILE E  37     104.645 137.530 120.631  1.00 74.74           C  
ATOM    112  CG2 ILE E  37     106.131 137.703 122.629  1.00 74.11           C  
ATOM    113  CD1 ILE E  37     104.148 138.955 120.663  1.00 75.09           C  
ATOM    114  N   SER E  38     105.189 134.582 124.182  1.00 75.18           N  
ATOM    115  CA  SER E  38     105.778 134.018 125.389  1.00 80.48           C  
ATOM    116  C   SER E  38     106.395 132.652 125.117  1.00 83.16           C  
ATOM    117  O   SER E  38     107.445 132.319 125.673  1.00 84.00           O  
ATOM    118  CB  SER E  38     104.723 133.924 126.489  1.00 80.79           C  
ATOM    119  N   LEU E  39     105.750 131.840 124.281  1.00 84.29           N  
ATOM    120  CA  LEU E  39     106.280 130.515 123.983  1.00 82.40           C  
ATOM    121  C   LEU E  39     107.640 130.619 123.310  1.00 82.88           C  
ATOM    122  O   LEU E  39     108.609 129.970 123.730  1.00 83.55           O  
ATOM    123  CB  LEU E  39     105.296 129.744 123.105  1.00 79.90           C  
ATOM    124  CG  LEU E  39     104.229 128.938 123.848  1.00 82.51           C  
ATOM    125  CD1 LEU E  39     102.930 128.908 123.059  1.00 82.45           C  
ATOM    126  CD2 LEU E  39     104.725 127.528 124.125  1.00 83.99           C  
ATOM    127  N   VAL E  40     107.740 131.460 122.277  1.00 79.62           N  
ATOM    128  CA  VAL E  40     109.049 131.657 121.656  1.00 77.89           C  
ATOM    129  C   VAL E  40     110.007 132.309 122.650  1.00 75.52           C  
ATOM    130  O   VAL E  40     111.224 132.091 122.598  1.00 71.39           O  
ATOM    131  CB  VAL E  40     108.927 132.454 120.340  1.00 75.63           C  
ATOM    132  CG1 VAL E  40     108.071 133.683 120.510  1.00 75.96           C  
ATOM    133  CG2 VAL E  40     110.299 132.822 119.784  1.00 74.91           C  
ATOM    134  N   GLY E  41     109.471 133.077 123.604  1.00 79.92           N  
ATOM    135  CA  GLY E  41     110.317 133.674 124.624  1.00 80.30           C  
ATOM    136  C   GLY E  41     110.999 132.652 125.512  1.00 81.55           C  
ATOM    137  O   GLY E  41     112.215 132.706 125.703  1.00 83.46           O  
ATOM    138  N   LEU E  42     110.231 131.716 126.080  1.00 77.73           N  
ATOM    139  CA  LEU E  42     110.867 130.660 126.868  1.00 77.32           C  
ATOM    140  C   LEU E  42     111.740 129.767 126.003  1.00 82.05           C  
ATOM    141  O   LEU E  42     112.755 129.256 126.478  1.00 80.35           O  
ATOM    142  CB  LEU E  42     109.881 129.789 127.656  1.00 76.36           C  
ATOM    143  CG  LEU E  42     108.858 130.193 128.721  1.00 80.48           C  
ATOM    144  CD1 LEU E  42     107.753 131.031 128.216  1.00 78.01           C  
ATOM    145  CD2 LEU E  42     108.301 128.945 129.395  1.00 81.53           C  
ATOM    146  N   THR E  43     111.374 129.558 124.736  1.00 85.28           N  
ATOM    147  CA  THR E  43     112.251 128.781 123.864  1.00 83.62           C  
ATOM    148  C   THR E  43     113.630 129.429 123.760  1.00 85.62           C  
ATOM    149  O   THR E  43     114.660 128.786 124.018  1.00 83.36           O  
ATOM    150  CB  THR E  43     111.619 128.631 122.480  1.00 84.29           C  
ATOM    151  OG1 THR E  43     110.283 128.131 122.615  1.00 84.58           O  
ATOM    152  CG2 THR E  43     112.433 127.675 121.623  1.00 85.05           C  
ATOM    153  N   GLY E  44     113.661 130.719 123.416  1.00 80.15           N  
ATOM    154  CA  GLY E  44     114.930 131.417 123.292  1.00 75.98           C  
ATOM    155  C   GLY E  44     115.671 131.526 124.610  1.00 73.82           C  
ATOM    156  O   GLY E  44     116.892 131.349 124.665  1.00 76.03           O  
ATOM    157  N   ASN E  45     114.946 131.817 125.691  1.00 67.51           N  
ATOM    158  CA  ASN E  45     115.584 131.929 126.996  1.00 66.59           C  
ATOM    159  C   ASN E  45     116.171 130.595 127.432  1.00 74.16           C  
ATOM    160  O   ASN E  45     117.265 130.550 128.000  1.00 75.53           O  
ATOM    161  CB  ASN E  45     114.585 132.446 128.029  1.00 77.45           C  
ATOM    162  CG  ASN E  45     114.311 133.931 127.881  1.00 80.12           C  
ATOM    163  OD1 ASN E  45     115.130 134.765 128.266  1.00 75.10           O  
ATOM    164  ND2 ASN E  45     113.152 134.267 127.327  1.00 81.09           N  
ATOM    165  N   ALA E  46     115.471 129.495 127.155  1.00 80.04           N  
ATOM    166  CA  ALA E  46     115.971 128.179 127.526  1.00 79.04           C  
ATOM    167  C   ALA E  46     117.227 127.829 126.743  1.00 80.15           C  
ATOM    168  O   ALA E  46     118.205 127.336 127.315  1.00 79.93           O  
ATOM    169  CB  ALA E  46     114.885 127.126 127.307  1.00 79.59           C  
ATOM    170  N   VAL E  47     117.227 128.076 125.428  1.00 78.41           N  
ATOM    171  CA  VAL E  47     118.417 127.716 124.661  1.00 76.43           C  
ATOM    172  C   VAL E  47     119.603 128.582 125.078  1.00 74.30           C  
ATOM    173  O   VAL E  47     120.723 128.080 125.241  1.00 74.75           O  
ATOM    174  CB  VAL E  47     118.163 127.784 123.142  1.00 76.00           C  
ATOM    175  CG1 VAL E  47     117.462 129.054 122.749  1.00 75.71           C  
ATOM    176  CG2 VAL E  47     119.471 127.637 122.374  1.00 76.86           C  
ATOM    177  N   VAL E  48     119.381 129.884 125.288  1.00 78.03           N  
ATOM    178  CA  VAL E  48     120.495 130.747 125.675  1.00 78.19           C  
ATOM    179  C   VAL E  48     120.985 130.399 127.078  1.00 75.39           C  
ATOM    180  O   VAL E  48     122.190 130.444 127.352  1.00 74.47           O  
ATOM    181  CB  VAL E  48     120.115 132.236 125.545  1.00 73.37           C  
ATOM    182  CG1 VAL E  48     119.070 132.636 126.562  1.00 71.99           C  
ATOM    183  CG2 VAL E  48     121.347 133.105 125.699  1.00 72.86           C  
ATOM    184  N   LEU E  49     120.072 130.033 127.982  1.00 72.14           N  
ATOM    185  CA  LEU E  49     120.476 129.623 129.322  1.00 69.79           C  
ATOM    186  C   LEU E  49     121.292 128.339 129.276  1.00 72.21           C  
ATOM    187  O   LEU E  49     122.313 128.219 129.962  1.00 72.08           O  
ATOM    188  CB  LEU E  49     119.237 129.444 130.200  1.00 67.64           C  
ATOM    189  CG  LEU E  49     119.347 129.804 131.682  1.00 71.22           C  
ATOM    190  CD1 LEU E  49     120.115 131.098 131.864  1.00 70.27           C  
ATOM    191  CD2 LEU E  49     117.965 129.912 132.304  1.00 69.11           C  
ATOM    192  N   TRP E  50     120.861 127.373 128.462  1.00 81.65           N  
ATOM    193  CA  TRP E  50     121.598 126.121 128.336  1.00 81.48           C  
ATOM    194  C   TRP E  50     122.987 126.358 127.760  1.00 83.56           C  
ATOM    195  O   TRP E  50     123.969 125.772 128.230  1.00 87.50           O  
ATOM    196  CB  TRP E  50     120.811 125.142 127.464  1.00 78.33           C  
ATOM    197  CG  TRP E  50     121.634 124.027 126.901  1.00 79.62           C  
ATOM    198  CD1 TRP E  50     122.410 123.148 127.597  1.00 81.17           C  
ATOM    199  CD2 TRP E  50     121.769 123.673 125.519  1.00 83.70           C  
ATOM    200  NE1 TRP E  50     123.016 122.267 126.736  1.00 84.17           N  
ATOM    201  CE2 TRP E  50     122.640 122.569 125.454  1.00 84.04           C  
ATOM    202  CE3 TRP E  50     121.237 124.182 124.330  1.00 83.69           C  
ATOM    203  CZ2 TRP E  50     122.992 121.965 124.249  1.00 79.87           C  
ATOM    204  CZ3 TRP E  50     121.587 123.581 123.135  1.00 79.68           C  
ATOM    205  CH2 TRP E  50     122.456 122.485 123.103  1.00 78.21           C  
ATOM    206  N   LEU E  51     123.093 127.215 126.742  1.00 77.99           N  
ATOM    207  CA  LEU E  51     124.397 127.472 126.138  1.00 75.90           C  
ATOM    208  C   LEU E  51     125.317 128.233 127.086  1.00 78.80           C  
ATOM    209  O   LEU E  51     126.479 127.856 127.263  1.00 79.99           O  
ATOM    210  CB  LEU E  51     124.234 128.236 124.826  1.00 74.86           C  
ATOM    211  CG  LEU E  51     123.449 127.537 123.717  1.00 79.08           C  
ATOM    212  CD1 LEU E  51     123.241 128.473 122.540  1.00 78.76           C  
ATOM    213  CD2 LEU E  51     124.166 126.270 123.278  1.00 80.96           C  
ATOM    214  N   LEU E  52     124.819 129.302 127.709  1.00 77.46           N  
ATOM    215  CA  LEU E  52     125.689 130.156 128.508  1.00 71.49           C  
ATOM    216  C   LEU E  52     126.023 129.516 129.850  1.00 69.51           C  
ATOM    217  O   LEU E  52     127.089 129.788 130.414  1.00 72.50           O  
ATOM    218  CB  LEU E  52     125.024 131.522 128.694  1.00 71.72           C  
ATOM    219  CG  LEU E  52     125.860 132.801 128.821  1.00 68.99           C  
ATOM    220  CD1 LEU E  52     124.940 134.006 128.795  1.00 72.73           C  
ATOM    221  CD2 LEU E  52     126.708 132.831 130.077  1.00 68.92           C  
ATOM    222  N   GLY E  53     125.143 128.658 130.367  1.00 77.86           N  
ATOM    223  CA  GLY E  53     125.384 128.066 131.672  1.00 85.01           C  
ATOM    224  C   GLY E  53     126.623 127.194 131.714  1.00 85.07           C  
ATOM    225  O   GLY E  53     127.396 127.244 132.675  1.00 83.39           O  
ATOM    226  N   TYR E  54     126.834 126.388 130.676  1.00 81.19           N  
ATOM    227  CA  TYR E  54     127.934 125.432 130.652  1.00 82.50           C  
ATOM    228  C   TYR E  54     128.863 125.630 129.465  1.00 82.27           C  
ATOM    229  O   TYR E  54     130.084 125.509 129.615  1.00 84.23           O  
ATOM    230  CB  TYR E  54     127.372 124.003 130.654  1.00 85.24           C  
ATOM    231  CG  TYR E  54     126.010 123.899 131.301  1.00 84.61           C  
ATOM    232  CD1 TYR E  54     125.870 123.948 132.682  1.00 83.89           C  
ATOM    233  CD2 TYR E  54     124.862 123.766 130.531  1.00 81.70           C  
ATOM    234  CE1 TYR E  54     124.627 123.859 133.278  1.00 82.77           C  
ATOM    235  CE2 TYR E  54     123.616 123.676 131.117  1.00 82.25           C  
ATOM    236  CZ  TYR E  54     123.504 123.723 132.490  1.00 83.40           C  
ATOM    237  OH  TYR E  54     122.262 123.633 133.077  1.00 82.41           O  
ATOM    238  N   ARG E  55     128.323 125.932 128.289  1.00 85.55           N  
ATOM    239  CA  ARG E  55     129.138 126.131 127.090  1.00 90.14           C  
ATOM    240  C   ARG E  55     129.569 127.589 126.945  1.00 89.15           C  
ATOM    241  O   ARG E  55     129.377 128.214 125.902  1.00 88.07           O  
ATOM    242  CB  ARG E  55     128.371 125.663 125.859  1.00 87.87           C  
ATOM    243  CG  ARG E  55     128.306 124.153 125.685  1.00 82.71           C  
ATOM    244  CD  ARG E  55     127.111 123.562 126.417  1.00 81.55           C  
ATOM    245  NE  ARG E  55     127.087 122.107 126.339  1.00 86.34           N  
ATOM    246  CZ  ARG E  55     126.374 121.326 127.139  1.00 87.15           C  
ATOM    247  NH1 ARG E  55     125.619 121.827 128.101  1.00 83.27           N1+
ATOM    248  NH2 ARG E  55     126.422 120.008 126.970  1.00 86.86           N  
ATOM    249  N   MET E  56     130.160 128.142 128.000  1.00 73.40           N  
ATOM    250  CA  MET E  56     130.595 129.533 128.003  1.00 71.85           C  
ATOM    251  C   MET E  56     131.677 129.697 129.063  1.00 75.96           C  
ATOM    252  O   MET E  56     131.976 128.771 129.822  1.00 72.02           O  
ATOM    253  CB  MET E  56     129.420 130.482 128.247  1.00 73.90           C  
ATOM    254  N   ARG E  57     132.262 130.896 129.111  1.00 75.83           N  
ATOM    255  CA  ARG E  57     133.365 131.186 130.015  1.00 75.46           C  
ATOM    256  C   ARG E  57     133.051 132.225 131.081  1.00 73.99           C  
ATOM    257  O   ARG E  57     133.852 132.379 132.010  1.00 72.54           O  
ATOM    258  CB  ARG E  57     134.597 131.659 129.224  1.00 68.93           C  
ATOM    259  N   ARG E  58     131.925 132.937 130.980  1.00 68.43           N  
ATOM    260  CA  ARG E  58     131.529 133.967 131.944  1.00 70.23           C  
ATOM    261  C   ARG E  58     132.615 135.042 132.061  1.00 68.77           C  
ATOM    262  O   ARG E  58     133.233 135.235 133.109  1.00 67.43           O  
ATOM    263  CB  ARG E  58     131.227 133.362 133.321  1.00 69.25           C  
ATOM    264  CG  ARG E  58     130.525 132.013 133.321  1.00 69.65           C  
ATOM    265  CD  ARG E  58     129.257 132.006 132.482  1.00 68.02           C  
ATOM    266  NE  ARG E  58     128.458 130.809 132.719  1.00 68.97           N  
ATOM    267  CZ  ARG E  58     127.902 130.486 133.881  1.00 68.85           C  
ATOM    268  NH1 ARG E  58     127.974 131.287 134.932  1.00 67.57           N1+
ATOM    269  NH2 ARG E  58     127.247 129.334 133.988  1.00 68.07           N  
ATOM    270  N   ASN E  59     132.837 135.741 130.947  1.00 63.15           N  
ATOM    271  CA  ASN E  59     134.011 136.602 130.870  1.00 64.31           C  
ATOM    272  C   ASN E  59     133.870 137.866 131.710  1.00 63.49           C  
ATOM    273  O   ASN E  59     134.542 138.005 132.737  1.00 67.53           O  
ATOM    274  CB  ASN E  59     134.278 136.979 129.411  1.00 62.08           C  
ATOM    275  CG  ASN E  59     133.000 137.220 128.630  1.00 60.74           C  
ATOM    276  OD1 ASN E  59     131.905 137.202 129.191  1.00 61.45           O  
ATOM    277  ND2 ASN E  59     133.133 137.444 127.329  1.00 64.51           N  
ATOM    278  N   ALA E  60     133.005 138.791 131.296  1.00 50.20           N  
ATOM    279  CA  ALA E  60     132.695 139.954 132.124  1.00 51.72           C  
ATOM    280  C   ALA E  60     131.236 140.378 132.100  1.00 47.00           C  
ATOM    281  O   ALA E  60     130.782 140.994 133.070  1.00 40.57           O  
ATOM    282  CB  ALA E  60     133.562 141.150 131.711  1.00 51.59           C  
ATOM    283  N   VAL E  61     130.482 140.073 131.048  1.00 51.93           N  
ATOM    284  CA  VAL E  61     129.137 140.605 130.870  1.00 47.33           C  
ATOM    285  C   VAL E  61     128.195 139.437 130.624  1.00 50.75           C  
ATOM    286  O   VAL E  61     126.990 139.524 130.884  1.00 56.54           O  
ATOM    287  CB  VAL E  61     129.099 141.624 129.713  1.00 50.78           C  
ATOM    288  CG1 VAL E  61     127.679 142.082 129.422  1.00 49.85           C  
ATOM    289  CG2 VAL E  61     129.986 142.816 130.026  1.00 52.18           C  
ATOM    290  N   SER E  62     128.749 138.319 130.149  1.00 50.21           N  
ATOM    291  CA  SER E  62     127.939 137.137 129.889  1.00 49.08           C  
ATOM    292  C   SER E  62     127.230 136.640 131.140  1.00 50.80           C  
ATOM    293  O   SER E  62     126.199 135.971 131.028  1.00 61.94           O  
ATOM    294  CB  SER E  62     128.809 136.033 129.295  1.00 58.25           C  
ATOM    295  OG  SER E  62     130.033 135.928 129.997  1.00 64.21           O  
ATOM    296  N   ILE E  63     127.750 136.958 132.327  1.00 47.72           N  
ATOM    297  CA  ILE E  63     127.007 136.686 133.553  1.00 50.22           C  
ATOM    298  C   ILE E  63     125.713 137.489 133.572  1.00 44.03           C  
ATOM    299  O   ILE E  63     124.648 136.974 133.943  1.00 48.47           O  
ATOM    300  CB  ILE E  63     127.881 136.987 134.785  1.00 42.65           C  
ATOM    301  CG1 ILE E  63     128.984 135.937 134.927  1.00 50.66           C  
ATOM    302  CG2 ILE E  63     127.032 137.041 136.043  1.00 46.00           C  
ATOM    303  CD1 ILE E  63     130.352 136.520 135.196  1.00 49.37           C  
ATOM    304  N   TYR E  64     125.789 138.766 133.179  1.00 36.00           N  
ATOM    305  CA  TYR E  64     124.595 139.602 133.120  1.00 39.74           C  
ATOM    306  C   TYR E  64     123.582 139.040 132.136  1.00 43.16           C  
ATOM    307  O   TYR E  64     122.386 138.977 132.437  1.00 49.88           O  
ATOM    308  CB  TYR E  64     124.956 141.031 132.724  1.00 39.16           C  
ATOM    309  CG  TYR E  64     125.834 141.772 133.697  1.00 42.22           C  
ATOM    310  CD1 TYR E  64     125.415 142.029 134.993  1.00 31.65           C  
ATOM    311  CD2 TYR E  64     127.083 142.228 133.311  1.00 50.41           C  
ATOM    312  CE1 TYR E  64     126.223 142.715 135.875  1.00 32.34           C  
ATOM    313  CE2 TYR E  64     127.894 142.908 134.181  1.00 47.60           C  
ATOM    314  CZ  TYR E  64     127.463 143.152 135.460  1.00 41.24           C  
ATOM    315  OH  TYR E  64     128.289 143.836 136.317  1.00 45.79           O  
ATOM    316  N   ILE E  65     124.039 138.628 130.953  1.00 45.05           N  
ATOM    317  CA  ILE E  65     123.121 138.040 129.984  1.00 44.09           C  
ATOM    318  C   ILE E  65     122.517 136.760 130.541  1.00 51.63           C  
ATOM    319  O   ILE E  65     121.325 136.493 130.362  1.00 55.88           O  
ATOM    320  CB  ILE E  65     123.830 137.798 128.639  1.00 46.03           C  
ATOM    321  CG1 ILE E  65     124.149 139.128 127.956  1.00 54.89           C  
ATOM    322  CG2 ILE E  65     122.970 136.944 127.726  1.00 49.98           C  
ATOM    323  CD1 ILE E  65     125.606 139.502 128.002  1.00 53.25           C  
ATOM    324  N   LEU E  66     123.317 135.968 131.254  1.00 58.32           N  
ATOM    325  CA  LEU E  66     122.831 134.702 131.792  1.00 56.80           C  
ATOM    326  C   LEU E  66     121.697 134.919 132.791  1.00 59.39           C  
ATOM    327  O   LEU E  66     120.608 134.346 132.652  1.00 60.21           O  
ATOM    328  CB  LEU E  66     123.988 133.944 132.445  1.00 56.54           C  
ATOM    329  CG  LEU E  66     123.651 132.677 133.230  1.00 61.56           C  
ATOM    330  CD1 LEU E  66     123.701 131.456 132.328  1.00 61.95           C  
ATOM    331  CD2 LEU E  66     124.597 132.519 134.408  1.00 62.07           C  
ATOM    332  N   ASN E  67     121.924 135.763 133.801  1.00 54.09           N  
ATOM    333  CA  ASN E  67     120.874 135.894 134.809  1.00 55.28           C  
ATOM    334  C   ASN E  67     119.722 136.750 134.302  1.00 56.10           C  
ATOM    335  O   ASN E  67     118.582 136.565 134.743  1.00 58.50           O  
ATOM    336  CB  ASN E  67     121.411 136.454 136.129  1.00 51.22           C  
ATOM    337  CG  ASN E  67     122.467 137.495 135.936  1.00 50.68           C  
ATOM    338  OD1 ASN E  67     122.534 138.122 134.892  1.00 55.70           O  
ATOM    339  ND2 ASN E  67     123.311 137.682 136.940  1.00 47.57           N  
ATOM    340  N   LEU E  68     119.981 137.665 133.363  1.00 45.14           N  
ATOM    341  CA  LEU E  68     118.890 138.385 132.722  1.00 44.52           C  
ATOM    342  C   LEU E  68     118.008 137.434 131.928  1.00 52.12           C  
ATOM    343  O   LEU E  68     116.781 137.561 131.947  1.00 60.27           O  
ATOM    344  CB  LEU E  68     119.452 139.480 131.820  1.00 44.72           C  
ATOM    345  CG  LEU E  68     118.521 140.025 130.739  1.00 45.90           C  
ATOM    346  CD1 LEU E  68     117.541 141.009 131.347  1.00 53.12           C  
ATOM    347  CD2 LEU E  68     119.319 140.669 129.622  1.00 49.54           C  
ATOM    348  N   ALA E  69     118.613 136.466 131.236  1.00 51.53           N  
ATOM    349  CA  ALA E  69     117.836 135.472 130.508  1.00 52.85           C  
ATOM    350  C   ALA E  69     117.063 134.570 131.459  1.00 58.08           C  
ATOM    351  O   ALA E  69     115.938 134.165 131.156  1.00 60.94           O  
ATOM    352  CB  ALA E  69     118.755 134.646 129.610  1.00 59.94           C  
ATOM    353  N   ALA E  70     117.651 134.236 132.610  1.00 58.68           N  
ATOM    354  CA  ALA E  70     116.917 133.454 133.604  1.00 61.28           C  
ATOM    355  C   ALA E  70     115.698 134.218 134.115  1.00 54.27           C  
ATOM    356  O   ALA E  70     114.583 133.677 134.179  1.00 52.52           O  
ATOM    357  CB  ALA E  70     117.843 133.079 134.761  1.00 59.89           C  
ATOM    358  N   ALA E  71     115.892 135.489 134.473  1.00 49.56           N  
ATOM    359  CA  ALA E  71     114.777 136.308 134.934  1.00 51.75           C  
ATOM    360  C   ALA E  71     113.732 136.477 133.841  1.00 53.38           C  
ATOM    361  O   ALA E  71     112.527 136.499 134.116  1.00 64.15           O  
ATOM    362  CB  ALA E  71     115.286 137.668 135.405  1.00 52.44           C  
ATOM    363  N   ASP E  72     114.173 136.591 132.589  1.00 59.35           N  
ATOM    364  CA  ASP E  72     113.232 136.716 131.485  1.00 62.42           C  
ATOM    365  C   ASP E  72     112.457 135.421 131.281  1.00 68.16           C  
ATOM    366  O   ASP E  72     111.270 135.448 130.942  1.00 69.60           O  
ATOM    367  CB  ASP E  72     113.978 137.103 130.211  1.00 68.23           C  
ATOM    368  CG  ASP E  72     114.150 138.600 130.070  1.00 68.75           C  
ATOM    369  OD1 ASP E  72     113.133 139.313 129.984  1.00 64.95           O  
ATOM    370  OD2 ASP E  72     115.308 139.065 130.037  1.00 70.07           O1-
ATOM    371  N   PHE E  73     113.113 134.275 131.467  1.00 68.76           N  
ATOM    372  CA  PHE E  73     112.400 133.006 131.411  1.00 68.10           C  
ATOM    373  C   PHE E  73     111.320 132.958 132.477  1.00 70.23           C  
ATOM    374  O   PHE E  73     110.191 132.527 132.212  1.00 71.43           O  
ATOM    375  CB  PHE E  73     113.377 131.843 131.580  1.00 62.76           C  
ATOM    376  N   LEU E  74     111.646 133.425 133.684  1.00 64.45           N  
ATOM    377  CA  LEU E  74     110.634 133.541 134.732  1.00 64.28           C  
ATOM    378  C   LEU E  74     109.486 134.442 134.285  1.00 63.47           C  
ATOM    379  O   LEU E  74     108.309 134.122 134.492  1.00 70.39           O  
ATOM    380  CB  LEU E  74     111.270 134.074 136.015  1.00 62.24           C  
ATOM    381  CG  LEU E  74     112.365 133.205 136.636  1.00 69.49           C  
ATOM    382  CD1 LEU E  74     112.873 133.832 137.921  1.00 67.52           C  
ATOM    383  CD2 LEU E  74     111.863 131.790 136.887  1.00 68.97           C  
ATOM    384  N   PHE E  75     109.820 135.579 133.670  1.00 56.20           N  
ATOM    385  CA  PHE E  75     108.810 136.499 133.148  1.00 55.57           C  
ATOM    386  C   PHE E  75     107.849 135.817 132.183  1.00 64.21           C  
ATOM    387  O   PHE E  75     106.630 135.829 132.393  1.00 69.23           O  
ATOM    388  CB  PHE E  75     109.486 137.680 132.458  1.00 63.32           C  
ATOM    389  CG  PHE E  75     108.636 138.910 132.400  1.00 63.67           C  
ATOM    390  CD1 PHE E  75     107.700 139.058 131.389  1.00 67.07           C  
ATOM    391  CD2 PHE E  75     108.756 139.907 133.341  1.00 62.66           C  
ATOM    392  CE1 PHE E  75     106.908 140.179 131.315  1.00 67.18           C  
ATOM    393  CE2 PHE E  75     107.961 141.030 133.269  1.00 61.62           C  
ATOM    394  CZ  PHE E  75     107.038 141.167 132.256  1.00 64.48           C  
ATOM    395  N   LEU E  76     108.371 135.258 131.091  1.00 66.28           N  
ATOM    396  CA  LEU E  76     107.472 134.681 130.096  1.00 68.03           C  
ATOM    397  C   LEU E  76     106.735 133.463 130.642  1.00 71.91           C  
ATOM    398  O   LEU E  76     105.586 133.211 130.250  1.00 76.77           O  
ATOM    399  CB  LEU E  76     108.206 134.314 128.801  1.00 76.15           C  
ATOM    400  CG  LEU E  76     108.897 135.278 127.821  1.00 77.87           C  
ATOM    401  CD1 LEU E  76     107.894 136.222 127.172  1.00 75.47           C  
ATOM    402  CD2 LEU E  76     110.053 136.044 128.389  1.00 75.14           C  
ATOM    403  N   SER E  77     107.359 132.701 131.546  1.00 67.57           N  
ATOM    404  CA  SER E  77     106.648 131.604 132.194  1.00 73.40           C  
ATOM    405  C   SER E  77     105.450 132.127 132.970  1.00 72.21           C  
ATOM    406  O   SER E  77     104.345 131.579 132.880  1.00 72.44           O  
ATOM    407  CB  SER E  77     107.593 130.844 133.122  1.00 73.69           C  
ATOM    408  OG  SER E  77     108.083 131.696 134.142  1.00 73.49           O  
ATOM    409  N   PHE E  78     105.650 133.207 133.728  1.00 66.53           N  
ATOM    410  CA  PHE E  78     104.548 133.799 134.471  1.00 68.37           C  
ATOM    411  C   PHE E  78     103.496 134.368 133.531  1.00 62.32           C  
ATOM    412  O   PHE E  78     102.312 134.391 133.870  1.00 65.43           O  
ATOM    413  CB  PHE E  78     105.073 134.888 135.402  1.00 69.84           C  
ATOM    414  CG  PHE E  78     105.048 134.506 136.850  1.00 63.00           C  
ATOM    415  CD1 PHE E  78     103.935 134.760 137.633  1.00 66.03           C  
ATOM    416  CD2 PHE E  78     106.146 133.904 137.431  1.00 58.95           C  
ATOM    417  CE1 PHE E  78     103.921 134.404 138.962  1.00 66.70           C  
ATOM    418  CE2 PHE E  78     106.139 133.551 138.759  1.00 66.57           C  
ATOM    419  CZ  PHE E  78     105.025 133.802 139.527  1.00 70.07           C  
ATOM    420  N   GLN E  79     103.910 134.831 132.352  1.00 68.80           N  
ATOM    421  CA  GLN E  79     102.951 135.322 131.365  1.00 75.23           C  
ATOM    422  C   GLN E  79     102.046 134.194 130.869  1.00 77.46           C  
ATOM    423  O   GLN E  79     100.821 134.358 130.766  1.00 78.88           O  
ATOM    424  CB  GLN E  79     103.701 135.976 130.204  1.00 75.09           C  
ATOM    425  CG  GLN E  79     104.236 137.374 130.515  1.00 72.15           C  
ATOM    426  CD  GLN E  79     103.146 138.408 130.731  1.00 74.78           C  
ATOM    427  OE1 GLN E  79     102.139 138.425 130.025  1.00 75.86           O  
ATOM    428  NE2 GLN E  79     103.314 139.233 131.753  1.00 71.09           N  
ATOM    429  N   ILE E  80     102.637 133.038 130.538  1.00 74.20           N  
ATOM    430  CA  ILE E  80     101.811 131.899 130.127  1.00 73.17           C  
ATOM    431  C   ILE E  80     101.004 131.313 131.273  1.00 76.85           C  
ATOM    432  O   ILE E  80      99.978 130.668 131.026  1.00 84.17           O  
ATOM    433  CB  ILE E  80     102.596 130.741 129.482  1.00 79.30           C  
ATOM    434  CG1 ILE E  80     103.749 131.257 128.633  1.00 81.36           C  
ATOM    435  CG2 ILE E  80     101.681 129.880 128.612  1.00 81.53           C  
ATOM    436  CD1 ILE E  80     104.472 130.148 127.911  1.00 78.52           C  
ATOM    437  N   ILE E  81     101.442 131.481 132.519  1.00 74.02           N  
ATOM    438  CA  ILE E  81     100.568 131.119 133.631  1.00 77.58           C  
ATOM    439  C   ILE E  81      99.405 132.101 133.740  1.00 82.10           C  
ATOM    440  O   ILE E  81      98.261 131.702 133.984  1.00 83.83           O  
ATOM    441  CB  ILE E  81     101.360 131.022 134.948  1.00 77.53           C  
ATOM    442  CG1 ILE E  81     102.540 130.062 134.794  1.00 78.86           C  
ATOM    443  CG2 ILE E  81     100.456 130.567 136.081  1.00 78.63           C  
ATOM    444  CD1 ILE E  81     103.329 129.847 136.068  1.00 78.04           C  
ATOM    445  N   ARG E  82      99.670 133.394 133.545  1.00 83.88           N  
ATOM    446  CA  ARG E  82      98.668 134.424 133.801  1.00 80.87           C  
ATOM    447  C   ARG E  82      97.576 134.448 132.739  1.00 80.34           C  
ATOM    448  O   ARG E  82      96.395 134.246 133.043  1.00 83.77           O  
ATOM    449  CB  ARG E  82      99.335 135.799 133.892  1.00 82.25           C  
ATOM    450  CG  ARG E  82      98.426 136.855 134.498  1.00 81.41           C  
ATOM    451  CD  ARG E  82      98.508 138.179 133.753  1.00 74.52           C  
ATOM    452  NE  ARG E  82      97.532 139.139 134.255  1.00 73.49           N  
ATOM    453  CZ  ARG E  82      96.225 139.056 134.039  1.00 78.55           C  
ATOM    454  NH1 ARG E  82      95.705 138.090 133.299  1.00 81.95           N1+
ATOM    455  NH2 ARG E  82      95.420 139.968 134.575  1.00 77.68           N  
ATOM    456  N   LEU E  83      97.957 134.695 131.485  1.00 71.50           N  
ATOM    457  CA  LEU E  83      96.977 135.070 130.462  1.00 74.35           C  
ATOM    458  C   LEU E  83      95.846 134.071 130.231  1.00 78.52           C  
ATOM    459  O   LEU E  83      94.690 134.514 130.110  1.00 78.56           O  
ATOM    460  CB  LEU E  83      97.691 135.397 129.147  1.00 78.72           C  
ATOM    461  CG  LEU E  83      98.350 136.777 129.052  1.00 83.16           C  
ATOM    462  CD1 LEU E  83      97.276 137.848 129.153  1.00 80.62           C  
ATOM    463  CD2 LEU E  83      99.386 137.010 130.117  1.00 81.33           C  
ATOM    464  N   PRO E  84      96.072 132.754 130.134  1.00 86.64           N  
ATOM    465  CA  PRO E  84      94.943 131.865 129.807  1.00 88.61           C  
ATOM    466  C   PRO E  84      93.873 131.803 130.885  1.00 92.59           C  
ATOM    467  O   PRO E  84      92.768 131.322 130.602  1.00 89.16           O  
ATOM    468  CB  PRO E  84      95.602 130.494 129.588  1.00 88.22           C  
ATOM    469  CG  PRO E  84      96.994 130.611 130.051  1.00 89.99           C  
ATOM    470  CD  PRO E  84      97.270 131.994 130.524  1.00 85.25           C  
ATOM    471  N   LEU E  85      94.151 132.277 132.099  1.00 93.26           N  
ATOM    472  CA  LEU E  85      93.144 132.357 133.150  1.00 86.16           C  
ATOM    473  C   LEU E  85      92.297 133.621 133.075  1.00 84.38           C  
ATOM    474  O   LEU E  85      91.378 133.779 133.885  1.00 91.06           O  
ATOM    475  CB  LEU E  85      93.802 132.258 134.529  1.00 86.94           C  
ATOM    476  CG  LEU E  85      94.128 130.835 134.992  1.00 90.43           C  
ATOM    477  CD1 LEU E  85      95.464 130.362 134.450  1.00 87.99           C  
ATOM    478  CD2 LEU E  85      94.100 130.743 136.512  1.00 92.72           C  
ATOM    479  N   ARG E  86      92.580 134.522 132.132  1.00 73.70           N  
ATOM    480  CA  ARG E  86      91.747 135.710 131.978  1.00 78.76           C  
ATOM    481  C   ARG E  86      90.416 135.385 131.311  1.00 80.38           C  
ATOM    482  O   ARG E  86      89.417 136.070 131.559  1.00 82.10           O  
ATOM    483  CB  ARG E  86      92.494 136.777 131.178  1.00 79.55           C  
ATOM    484  CG  ARG E  86      91.756 138.103 131.073  1.00 80.27           C  
ATOM    485  CD  ARG E  86      92.627 139.272 131.494  1.00 80.23           C  
ATOM    486  NE  ARG E  86      91.991 140.550 131.195  1.00 84.26           N  
ATOM    487  CZ  ARG E  86      92.529 141.734 131.455  1.00 81.65           C  
ATOM    488  NH1 ARG E  86      93.714 141.842 132.029  1.00 79.16           N1+
ATOM    489  NH2 ARG E  86      91.858 142.836 131.133  1.00 76.69           N  
ATOM    490  N   LEU E  87      90.376 134.351 130.474  1.00 83.77           N  
ATOM    491  CA  LEU E  87      89.167 134.027 129.727  1.00 83.39           C  
ATOM    492  C   LEU E  87      88.241 133.082 130.484  1.00 80.68           C  
ATOM    493  O   LEU E  87      87.024 133.108 130.266  1.00 73.76           O  
ATOM    494  CB  LEU E  87      89.541 133.418 128.372  1.00 83.96           C  
ATOM    495  CG  LEU E  87      88.470 133.386 127.278  1.00 85.52           C  
ATOM    496  CD1 LEU E  87      88.096 134.793 126.843  1.00 84.02           C  
ATOM    497  CD2 LEU E  87      88.959 132.574 126.088  1.00 84.40           C  
ATOM    498  N   ILE E  88      88.786 132.249 131.368  1.00 89.16           N  
ATOM    499  CA  ILE E  88      88.019 131.229 132.075  1.00 90.21           C  
ATOM    500  C   ILE E  88      88.274 131.373 133.571  1.00 90.65           C  
ATOM    501  O   ILE E  88      89.415 131.597 133.992  1.00 89.06           O  
ATOM    502  CB  ILE E  88      88.381 129.813 131.585  1.00 89.44           C  
ATOM    503  CG1 ILE E  88      87.608 128.749 132.365  1.00 85.12           C  
ATOM    504  CG2 ILE E  88      89.881 129.572 131.685  1.00 88.91           C  
ATOM    505  CD1 ILE E  88      86.110 128.811 132.158  1.00 86.47           C  
ATOM    506  N   ASN E  89      87.206 131.259 134.366  1.00104.64           N  
ATOM    507  CA  ASN E  89      87.274 131.280 135.830  1.00106.61           C  
ATOM    508  C   ASN E  89      87.901 132.583 136.339  1.00104.14           C  
ATOM    509  O   ASN E  89      88.978 132.607 136.939  1.00102.86           O  
ATOM    510  CB  ASN E  89      88.028 130.057 136.365  1.00107.31           C  
ATOM    511  CG  ASN E  89      87.179 128.801 136.365  1.00106.55           C  
ATOM    512  OD1 ASN E  89      86.544 128.465 135.368  1.00106.78           O  
ATOM    513  ND2 ASN E  89      87.164 128.100 137.493  1.00104.29           N  
ATOM    514  N   ILE E  90      87.185 133.676 136.072  1.00 91.45           N  
ATOM    515  CA  ILE E  90      87.601 134.979 136.575  1.00 90.93           C  
ATOM    516  C   ILE E  90      87.517 134.981 138.095  1.00 92.53           C  
ATOM    517  O   ILE E  90      86.527 134.528 138.683  1.00 88.21           O  
ATOM    518  CB  ILE E  90      86.743 136.086 135.942  1.00 92.98           C  
ATOM    519  CG1 ILE E  90      87.162 137.465 136.456  1.00 93.30           C  
ATOM    520  CG2 ILE E  90      85.256 135.823 136.162  1.00 94.74           C  
ATOM    521  CD1 ILE E  90      87.050 138.555 135.414  1.00 89.00           C  
ATOM    522  N   SER E  91      88.571 135.480 138.741  1.00 93.81           N  
ATOM    523  CA  SER E  91      88.689 135.408 140.194  1.00 93.62           C  
ATOM    524  C   SER E  91      88.998 136.768 140.810  1.00 91.42           C  
ATOM    525  O   SER E  91      88.597 137.043 141.946  1.00 90.00           O  
ATOM    526  CB  SER E  91      89.766 134.397 140.574  1.00 89.09           C  
ATOM    527  OG  SER E  91      90.901 134.569 139.750  1.00 86.53           O  
ATOM    528  N   HIS E  92      89.748 137.597 140.082  1.00 88.95           N  
ATOM    529  CA  HIS E  92      89.967 139.003 140.411  1.00 91.72           C  
ATOM    530  C   HIS E  92      90.867 139.208 141.627  1.00 96.51           C  
ATOM    531  O   HIS E  92      91.132 140.351 142.006  1.00 98.78           O  
ATOM    532  CB  HIS E  92      88.629 139.713 140.642  1.00 94.97           C  
ATOM    533  CG  HIS E  92      88.015 140.270 139.397  1.00 96.05           C  
ATOM    534  ND1 HIS E  92      86.661 140.210 139.147  1.00 94.76           N  
ATOM    535  CD2 HIS E  92      88.568 140.891 138.329  1.00 95.28           C  
ATOM    536  CE1 HIS E  92      86.405 140.774 137.981  1.00 92.90           C  
ATOM    537  NE2 HIS E  92      87.545 141.196 137.464  1.00 93.78           N  
ATOM    538  N   LEU E  93      91.335 138.129 142.258  1.00 86.94           N  
ATOM    539  CA  LEU E  93      92.227 138.282 143.406  1.00 80.86           C  
ATOM    540  C   LEU E  93      93.581 137.639 143.134  1.00 80.87           C  
ATOM    541  O   LEU E  93      94.634 138.279 143.283  1.00 85.82           O  
ATOM    542  CB  LEU E  93      91.582 137.680 144.655  1.00 80.18           C  
ATOM    543  CG  LEU E  93      90.292 138.320 145.182  1.00 85.58           C  
ATOM    544  CD1 LEU E  93      90.073 137.966 146.644  1.00 82.85           C  
ATOM    545  CD2 LEU E  93      90.309 139.828 145.006  1.00 83.10           C  
ATOM    546  N   ILE E  94      93.572 136.371 142.719  1.00 82.22           N  
ATOM    547  CA  ILE E  94      94.821 135.702 142.373  1.00 85.04           C  
ATOM    548  C   ILE E  94      95.505 136.436 141.229  1.00 83.03           C  
ATOM    549  O   ILE E  94      96.730 136.399 141.096  1.00 79.77           O  
ATOM    550  CB  ILE E  94      94.576 134.218 142.041  1.00 84.70           C  
ATOM    551  CG1 ILE E  94      93.688 134.070 140.807  1.00 84.48           C  
ATOM    552  CG2 ILE E  94      93.957 133.501 143.230  1.00 80.54           C  
ATOM    553  CD1 ILE E  94      94.437 133.759 139.526  1.00 79.73           C  
ATOM    554  N   ARG E  95      94.720 137.129 140.398  1.00 75.80           N  
ATOM    555  CA  ARG E  95      95.276 137.953 139.330  1.00 74.93           C  
ATOM    556  C   ARG E  95      96.165 139.050 139.897  1.00 76.63           C  
ATOM    557  O   ARG E  95      97.286 139.282 139.418  1.00 80.87           O  
ATOM    558  CB  ARG E  95      94.133 138.553 138.513  1.00 79.31           C  
ATOM    559  CG  ARG E  95      93.246 137.515 137.866  1.00 78.68           C  
ATOM    560  CD  ARG E  95      92.763 137.979 136.514  1.00 78.49           C  
ATOM    561  NE  ARG E  95      91.584 137.236 136.091  1.00 74.85           N  
ATOM    562  CZ  ARG E  95      90.835 137.559 135.048  1.00 77.14           C  
ATOM    563  NH1 ARG E  95      91.092 138.630 134.318  1.00 76.79           N1+
ATOM    564  NH2 ARG E  95      89.800 136.788 134.731  1.00 77.52           N  
ATOM    565  N   LYS E  96      95.664 139.737 140.927  1.00 67.55           N  
ATOM    566  CA  LYS E  96      96.478 140.712 141.639  1.00 66.24           C  
ATOM    567  C   LYS E  96      97.711 140.056 142.236  1.00 72.28           C  
ATOM    568  O   LYS E  96      98.804 140.635 142.217  1.00 68.68           O  
ATOM    569  CB  LYS E  96      95.652 141.404 142.721  1.00 67.49           C  
ATOM    570  CG  LYS E  96      94.173 141.492 142.420  1.00 69.97           C  
ATOM    571  CD  LYS E  96      93.913 142.649 141.469  1.00 69.13           C  
ATOM    572  CE  LYS E  96      92.438 142.994 141.391  1.00 68.33           C  
ATOM    573  NZ  LYS E  96      91.888 143.362 142.726  1.00 67.51           N1+
ATOM    574  N   ILE E  97      97.562 138.839 142.766  1.00 76.90           N  
ATOM    575  CA  ILE E  97      98.755 138.171 143.283  1.00 72.78           C  
ATOM    576  C   ILE E  97      99.784 137.932 142.180  1.00 67.61           C  
ATOM    577  O   ILE E  97     100.980 138.176 142.392  1.00 69.47           O  
ATOM    578  CB  ILE E  97      98.416 136.861 144.023  1.00 74.65           C  
ATOM    579  CG1 ILE E  97      97.032 136.915 144.675  1.00 73.90           C  
ATOM    580  CG2 ILE E  97      99.489 136.545 145.059  1.00 76.80           C  
ATOM    581  CD1 ILE E  97      96.887 137.979 145.746  1.00 70.90           C  
ATOM    582  N   LEU E  98      99.367 137.457 140.999  1.00 65.98           N  
ATOM    583  CA  LEU E  98     100.370 137.176 139.972  1.00 72.00           C  
ATOM    584  C   LEU E  98     101.041 138.452 139.485  1.00 73.39           C  
ATOM    585  O   LEU E  98     102.253 138.459 139.258  1.00 73.72           O  
ATOM    586  CB  LEU E  98      99.844 136.393 138.758  1.00 78.33           C  
ATOM    587  CG  LEU E  98      98.942 135.163 138.565  1.00 79.56           C  
ATOM    588  CD1 LEU E  98      97.471 135.457 138.474  1.00 76.87           C  
ATOM    589  CD2 LEU E  98      99.406 134.355 137.355  1.00 73.21           C  
ATOM    590  N   VAL E  99     100.284 139.538 139.294  1.00 68.73           N  
ATOM    591  CA  VAL E  99     100.948 140.756 138.824  1.00 62.00           C  
ATOM    592  C   VAL E  99     101.882 141.297 139.904  1.00 65.58           C  
ATOM    593  O   VAL E  99     102.988 141.774 139.609  1.00 70.47           O  
ATOM    594  CB  VAL E  99      99.934 141.817 138.349  1.00 61.08           C  
ATOM    595  CG1 VAL E  99      99.411 141.474 136.951  1.00 61.17           C  
ATOM    596  CG2 VAL E  99      98.803 141.991 139.329  1.00 72.02           C  
ATOM    597  N   SER E 100     101.477 141.189 141.173  1.00 66.53           N  
ATOM    598  CA  SER E 100     102.355 141.598 142.262  1.00 69.42           C  
ATOM    599  C   SER E 100     103.669 140.828 142.249  1.00 73.08           C  
ATOM    600  O   SER E 100     104.744 141.428 142.363  1.00 69.67           O  
ATOM    601  CB  SER E 100     101.652 141.403 143.598  1.00 79.94           C  
ATOM    602  OG  SER E 100     102.471 141.867 144.653  1.00 81.91           O  
ATOM    603  N   VAL E 101     103.610 139.499 142.134  1.00 75.06           N  
ATOM    604  CA  VAL E 101     104.863 138.746 142.159  1.00 65.25           C  
ATOM    605  C   VAL E 101     105.658 138.992 140.881  1.00 61.85           C  
ATOM    606  O   VAL E 101     106.889 139.078 140.919  1.00 70.86           O  
ATOM    607  CB  VAL E 101     104.629 137.241 142.399  1.00 67.35           C  
ATOM    608  CG1 VAL E 101     103.539 136.701 141.512  1.00 65.43           C  
ATOM    609  CG2 VAL E 101     105.926 136.455 142.225  1.00 65.60           C  
ATOM    610  N   MET E 102     104.977 139.134 139.738  1.00 67.52           N  
ATOM    611  CA  MET E 102     105.642 139.335 138.454  1.00 70.73           C  
ATOM    612  C   MET E 102     106.335 140.685 138.373  1.00 67.87           C  
ATOM    613  O   MET E 102     107.233 140.868 137.543  1.00 60.55           O  
ATOM    614  CB  MET E 102     104.623 139.204 137.320  1.00 65.07           C  
ATOM    615  CG  MET E 102     105.208 138.890 135.956  1.00 63.69           C  
ATOM    616  SD  MET E 102     103.937 138.908 134.678  1.00 82.73           S  
ATOM    617  CE  MET E 102     102.611 138.049 135.522  1.00 71.75           C  
ATOM    618  N   THR E 103     105.922 141.638 139.208  1.00 60.65           N  
ATOM    619  CA  THR E 103     106.647 142.897 139.307  1.00 57.68           C  
ATOM    620  C   THR E 103     108.124 142.689 139.634  1.00 58.09           C  
ATOM    621  O   THR E 103     108.966 143.447 139.141  1.00 64.78           O  
ATOM    622  CB  THR E 103     105.967 143.789 140.353  1.00 66.27           C  
ATOM    623  OG1 THR E 103     104.847 144.453 139.754  1.00 70.33           O  
ATOM    624  CG2 THR E 103     106.925 144.828 140.923  1.00 64.66           C  
ATOM    625  N   PHE E 104     108.463 141.653 140.402  1.00 46.54           N  
ATOM    626  CA  PHE E 104     109.853 141.455 140.812  1.00 44.05           C  
ATOM    627  C   PHE E 104     110.749 140.985 139.669  1.00 49.81           C  
ATOM    628  O   PHE E 104     111.822 141.585 139.473  1.00 56.83           O  
ATOM    629  CB  PHE E 104     109.885 140.507 142.020  1.00 46.86           C  
ATOM    630  CG  PHE E 104     111.168 139.736 142.174  1.00 54.35           C  
ATOM    631  CD1 PHE E 104     112.364 140.392 142.402  1.00 55.68           C  
ATOM    632  CD2 PHE E 104     111.167 138.350 142.143  1.00 54.08           C  
ATOM    633  CE1 PHE E 104     113.537 139.685 142.556  1.00 54.59           C  
ATOM    634  CE2 PHE E 104     112.340 137.638 142.304  1.00 54.90           C  
ATOM    635  CZ  PHE E 104     113.525 138.309 142.512  1.00 53.94           C  
ATOM    636  N   PRO E 105     110.406 139.947 138.895  1.00 46.02           N  
ATOM    637  CA  PRO E 105     111.249 139.615 137.735  1.00 41.86           C  
ATOM    638  C   PRO E 105     111.337 140.731 136.710  1.00 50.26           C  
ATOM    639  O   PRO E 105     112.377 140.871 136.058  1.00 53.99           O  
ATOM    640  CB  PRO E 105     110.573 138.366 137.156  1.00 42.52           C  
ATOM    641  CG  PRO E 105     109.857 137.770 138.299  1.00 49.34           C  
ATOM    642  CD  PRO E 105     109.353 138.936 139.087  1.00 48.97           C  
ATOM    643  N   TYR E 106     110.280 141.527 136.539  1.00 59.18           N  
ATOM    644  CA  TYR E 106     110.342 142.639 135.594  1.00 52.18           C  
ATOM    645  C   TYR E 106     111.366 143.670 136.048  1.00 43.31           C  
ATOM    646  O   TYR E 106     112.162 144.176 135.245  1.00 44.19           O  
ATOM    647  CB  TYR E 106     108.954 143.267 135.440  1.00 59.39           C  
ATOM    648  CG  TYR E 106     108.916 144.591 134.711  1.00 54.10           C  
ATOM    649  CD1 TYR E 106     109.198 145.786 135.360  1.00 52.39           C  
ATOM    650  CD2 TYR E 106     108.523 144.650 133.382  1.00 51.40           C  
ATOM    651  CE1 TYR E 106     109.143 146.989 134.691  1.00 58.30           C  
ATOM    652  CE2 TYR E 106     108.470 145.844 132.707  1.00 48.81           C  
ATOM    653  CZ  TYR E 106     108.777 147.012 133.364  1.00 58.21           C  
ATOM    654  OH  TYR E 106     108.718 148.209 132.689  1.00 66.14           O  
ATOM    655  N   PHE E 107     111.353 143.993 137.341  1.00 39.25           N  
ATOM    656  CA  PHE E 107     112.342 144.912 137.884  1.00 36.81           C  
ATOM    657  C   PHE E 107     113.743 144.342 137.737  1.00 42.80           C  
ATOM    658  O   PHE E 107     114.685 145.071 137.410  1.00 46.78           O  
ATOM    659  CB  PHE E 107     112.030 145.206 139.349  1.00 41.52           C  
ATOM    660  CG  PHE E 107     111.278 146.486 139.563  1.00 49.04           C  
ATOM    661  CD1 PHE E 107     109.927 146.563 139.278  1.00 48.07           C  
ATOM    662  CD2 PHE E 107     111.919 147.610 140.054  1.00 51.58           C  
ATOM    663  CE1 PHE E 107     109.229 147.735 139.471  1.00 48.67           C  
ATOM    664  CE2 PHE E 107     111.226 148.787 140.251  1.00 49.59           C  
ATOM    665  CZ  PHE E 107     109.879 148.849 139.959  1.00 48.68           C  
ATOM    666  N   THR E 108     113.897 143.035 137.964  1.00 46.07           N  
ATOM    667  CA  THR E 108     115.204 142.407 137.799  1.00 39.95           C  
ATOM    668  C   THR E 108     115.688 142.517 136.358  1.00 47.69           C  
ATOM    669  O   THR E 108     116.854 142.832 136.104  1.00 55.12           O  
ATOM    670  CB  THR E 108     115.146 140.943 138.233  1.00 36.94           C  
ATOM    671  OG1 THR E 108     115.140 140.867 139.663  1.00 49.99           O  
ATOM    672  CG2 THR E 108     116.356 140.191 137.712  1.00 42.50           C  
ATOM    673  N   GLY E 109     114.798 142.263 135.398  1.00 44.14           N  
ATOM    674  CA  GLY E 109     115.187 142.344 134.000  1.00 36.19           C  
ATOM    675  C   GLY E 109     115.570 143.748 133.575  1.00 36.30           C  
ATOM    676  O   GLY E 109     116.565 143.944 132.869  1.00 44.25           O  
ATOM    677  N   LEU E 110     114.789 144.746 133.995  1.00 38.02           N  
ATOM    678  CA  LEU E 110     115.156 146.122 133.682  1.00 35.71           C  
ATOM    679  C   LEU E 110     116.472 146.511 134.344  1.00 38.37           C  
ATOM    680  O   LEU E 110     117.294 147.207 133.733  1.00 48.27           O  
ATOM    681  CB  LEU E 110     114.048 147.082 134.105  1.00 42.79           C  
ATOM    682  CG  LEU E 110     112.791 147.091 133.235  1.00 44.31           C  
ATOM    683  CD1 LEU E 110     112.024 148.383 133.448  1.00 45.54           C  
ATOM    684  CD2 LEU E 110     113.123 146.887 131.766  1.00 42.58           C  
ATOM    685  N   SER E 111     116.691 146.065 135.583  1.00 28.26           N  
ATOM    686  CA  SER E 111     117.949 146.342 136.263  1.00 29.18           C  
ATOM    687  C   SER E 111     119.119 145.710 135.527  1.00 36.25           C  
ATOM    688  O   SER E 111     120.188 146.315 135.421  1.00 42.01           O  
ATOM    689  CB  SER E 111     117.885 145.835 137.702  1.00 38.02           C  
ATOM    690  OG  SER E 111     116.716 146.299 138.353  1.00 44.98           O  
ATOM    691  N   MET E 112     118.937 144.493 135.014  1.00 38.19           N  
ATOM    692  CA  MET E 112     120.010 143.843 134.269  1.00 39.17           C  
ATOM    693  C   MET E 112     120.277 144.533 132.940  1.00 38.79           C  
ATOM    694  O   MET E 112     121.435 144.638 132.527  1.00 42.59           O  
ATOM    695  CB  MET E 112     119.687 142.368 134.049  1.00 39.50           C  
ATOM    696  CG  MET E 112     119.586 141.577 135.333  1.00 37.06           C  
ATOM    697  SD  MET E 112     121.157 141.519 136.203  1.00 42.74           S  
ATOM    698  CE  MET E 112     120.842 140.186 137.345  1.00 44.38           C  
ATOM    699  N   LEU E 113     119.233 144.998 132.253  1.00 42.29           N  
ATOM    700  CA  LEU E 113     119.448 145.761 131.025  1.00 35.98           C  
ATOM    701  C   LEU E 113     120.229 147.038 131.307  1.00 38.51           C  
ATOM    702  O   LEU E 113     121.181 147.375 130.590  1.00 43.45           O  
ATOM    703  CB  LEU E 113     118.109 146.083 130.365  1.00 41.37           C  
ATOM    704  CG  LEU E 113     117.352 144.885 129.798  1.00 46.24           C  
ATOM    705  CD1 LEU E 113     116.150 145.336 128.992  1.00 44.27           C  
ATOM    706  CD2 LEU E 113     118.287 144.063 128.939  1.00 49.37           C  
ATOM    707  N   SER E 114     119.843 147.757 132.363  1.00 29.42           N  
ATOM    708  CA  SER E 114     120.570 148.965 132.736  1.00 18.55           C  
ATOM    709  C   SER E 114     122.006 148.646 133.127  1.00 25.87           C  
ATOM    710  O   SER E 114     122.929 149.400 132.797  1.00 46.48           O  
ATOM    711  CB  SER E 114     119.852 149.675 133.880  1.00 32.40           C  
ATOM    712  OG  SER E 114     120.737 150.545 134.559  1.00 36.46           O  
ATOM    713  N   ALA E 115     122.210 147.540 133.846  1.00 21.24           N  
ATOM    714  CA  ALA E 115     123.553 147.146 134.250  1.00 24.72           C  
ATOM    715  C   ALA E 115     124.413 146.812 133.043  1.00 26.43           C  
ATOM    716  O   ALA E 115     125.582 147.197 132.985  1.00 23.83           O  
ATOM    717  CB  ALA E 115     123.486 145.957 135.207  1.00 29.79           C  
ATOM    718  N   ILE E 116     123.849 146.106 132.063  1.00 30.21           N  
ATOM    719  CA  ILE E 116     124.584 145.804 130.839  1.00 18.82           C  
ATOM    720  C   ILE E 116     124.963 147.089 130.118  1.00 29.51           C  
ATOM    721  O   ILE E 116     126.102 147.250 129.662  1.00 50.35           O  
ATOM    722  CB  ILE E 116     123.753 144.879 129.932  1.00 28.41           C  
ATOM    723  CG1 ILE E 116     123.679 143.474 130.520  1.00 28.29           C  
ATOM    724  CG2 ILE E 116     124.337 144.837 128.532  1.00 38.65           C  
ATOM    725  CD1 ILE E 116     122.578 142.627 129.928  1.00 39.22           C  
ATOM    726  N   SER E 117     124.016 148.022 130.003  1.00 28.75           N  
ATOM    727  CA  SER E 117     124.296 149.272 129.302  1.00 27.80           C  
ATOM    728  C   SER E 117     125.410 150.052 129.989  1.00 29.83           C  
ATOM    729  O   SER E 117     126.390 150.454 129.347  1.00 45.91           O  
ATOM    730  CB  SER E 117     123.025 150.113 129.207  1.00 37.57           C  
ATOM    731  OG  SER E 117     121.901 149.297 128.935  1.00 50.76           O  
ATOM    732  N   THR E 118     125.290 150.264 131.302  1.00 20.99           N  
ATOM    733  CA  THR E 118     126.317 151.034 131.996  1.00 28.51           C  
ATOM    734  C   THR E 118     127.634 150.276 132.057  1.00 37.18           C  
ATOM    735  O   THR E 118     128.700 150.896 132.097  1.00 42.30           O  
ATOM    736  CB  THR E 118     125.865 151.412 133.408  1.00 31.83           C  
ATOM    737  OG1 THR E 118     126.911 152.144 134.057  1.00 38.44           O  
ATOM    738  CG2 THR E 118     125.570 150.177 134.230  1.00 42.17           C  
ATOM    739  N   GLU E 119     127.590 148.944 132.018  1.00 35.79           N  
ATOM    740  CA  GLU E 119     128.815 148.164 132.090  1.00 31.99           C  
ATOM    741  C   GLU E 119     129.583 148.258 130.779  1.00 32.14           C  
ATOM    742  O   GLU E 119     130.808 148.418 130.777  1.00 37.45           O  
ATOM    743  CB  GLU E 119     128.473 146.710 132.415  1.00 31.20           C  
ATOM    744  CG  GLU E 119     128.806 146.253 133.836  1.00 40.46           C  
ATOM    745  CD  GLU E 119     130.180 146.659 134.318  1.00 48.85           C  
ATOM    746  OE1 GLU E 119     131.100 146.759 133.492  1.00 46.95           O  
ATOM    747  OE2 GLU E 119     130.340 146.874 135.538  1.00 44.49           O1-
ATOM    748  N   ARG E 120     128.870 148.177 129.652  1.00 30.62           N  
ATOM    749  CA  ARG E 120     129.491 148.422 128.356  1.00 22.31           C  
ATOM    750  C   ARG E 120     130.024 149.846 128.265  1.00 26.53           C  
ATOM    751  O   ARG E 120     131.110 150.079 127.719  1.00 38.47           O  
ATOM    752  CB  ARG E 120     128.486 148.157 127.235  1.00 30.84           C  
ATOM    753  CG  ARG E 120     128.146 146.691 127.001  1.00 31.99           C  
ATOM    754  CD  ARG E 120     129.393 145.851 126.755  1.00 39.04           C  
ATOM    755  NE  ARG E 120     129.245 144.988 125.588  1.00 44.75           N  
ATOM    756  CZ  ARG E 120     130.255 144.437 124.928  1.00 40.89           C  
ATOM    757  NH1 ARG E 120     131.509 144.627 125.301  1.00 36.29           N1+
ATOM    758  NH2 ARG E 120     130.000 143.677 123.867  1.00 31.68           N  
ATOM    759  N   CYS E 121     129.269 150.815 128.789  1.00 26.23           N  
ATOM    760  CA  CYS E 121     129.739 152.197 128.777  1.00 24.67           C  
ATOM    761  C   CYS E 121     131.029 152.349 129.572  1.00 31.78           C  
ATOM    762  O   CYS E 121     131.950 153.051 129.143  1.00 43.83           O  
ATOM    763  CB  CYS E 121     128.659 153.125 129.328  1.00 26.32           C  
ATOM    764  SG  CYS E 121     129.229 154.808 129.642  1.00 47.35           S  
ATOM    765  N   LEU E 122     131.113 151.704 130.738  1.00 36.89           N  
ATOM    766  CA  LEU E 122     132.330 151.772 131.541  1.00 34.61           C  
ATOM    767  C   LEU E 122     133.486 151.050 130.862  1.00 30.26           C  
ATOM    768  O   LEU E 122     134.639 151.484 130.962  1.00 35.46           O  
ATOM    769  CB  LEU E 122     132.079 151.189 132.931  1.00 32.89           C  
ATOM    770  CG  LEU E 122     131.149 151.981 133.852  1.00 41.44           C  
ATOM    771  CD1 LEU E 122     130.931 151.241 135.160  1.00 41.27           C  
ATOM    772  CD2 LEU E 122     131.706 153.372 134.107  1.00 37.45           C  
ATOM    773  N   SER E 123     133.203 149.935 130.185  1.00 19.82           N  
ATOM    774  CA  SER E 123     134.257 149.222 129.472  1.00 17.59           C  
ATOM    775  C   SER E 123     134.827 150.069 128.344  1.00 17.62           C  
ATOM    776  O   SER E 123     136.042 150.074 128.117  1.00 28.80           O  
ATOM    777  CB  SER E 123     133.723 147.899 128.928  1.00 23.47           C  
ATOM    778  OG  SER E 123     132.810 148.119 127.870  1.00 27.19           O  
ATOM    779  N   VAL E 124     133.966 150.779 127.618  1.00 26.23           N  
ATOM    780  CA  VAL E 124     134.439 151.644 126.542  1.00 23.38           C  
ATOM    781  C   VAL E 124     135.159 152.870 127.096  1.00 20.92           C  
ATOM    782  O   VAL E 124     136.180 153.301 126.550  1.00 26.07           O  
ATOM    783  CB  VAL E 124     133.266 152.034 125.627  1.00 24.93           C  
ATOM    784  CG1 VAL E 124     133.702 153.075 124.615  1.00 23.94           C  
ATOM    785  CG2 VAL E 124     132.727 150.800 124.923  1.00 32.04           C  
ATOM    786  N   LEU E 125     134.646 153.450 128.183  1.00 21.24           N  
ATOM    787  CA  LEU E 125     135.240 154.667 128.729  1.00 20.26           C  
ATOM    788  C   LEU E 125     136.655 154.418 129.231  1.00 29.78           C  
ATOM    789  O   LEU E 125     137.586 155.153 128.884  1.00 37.63           O  
ATOM    790  CB  LEU E 125     134.364 155.219 129.853  1.00 32.75           C  
ATOM    791  CG  LEU E 125     133.151 156.058 129.451  1.00 41.56           C  
ATOM    792  CD1 LEU E 125     132.460 156.613 130.684  1.00 41.37           C  
ATOM    793  CD2 LEU E 125     133.561 157.181 128.514  1.00 32.68           C  
ATOM    794  N   TRP E 126     136.837 153.389 130.057  1.00 30.43           N  
ATOM    795  CA  TRP E 126     138.149 153.012 130.582  1.00 29.15           C  
ATOM    796  C   TRP E 126     138.370 151.535 130.296  1.00 37.96           C  
ATOM    797  O   TRP E 126     137.981 150.671 131.094  1.00 47.92           O  
ATOM    798  CB  TRP E 126     138.259 153.309 132.075  1.00 29.87           C  
ATOM    799  CG  TRP E 126     137.930 154.723 132.423  1.00 41.22           C  
ATOM    800  CD1 TRP E 126     138.652 155.833 132.103  1.00 41.26           C  
ATOM    801  CD2 TRP E 126     136.794 155.181 133.163  1.00 39.74           C  
ATOM    802  NE1 TRP E 126     138.035 156.956 132.596  1.00 37.75           N  
ATOM    803  CE2 TRP E 126     136.892 156.582 133.252  1.00 28.76           C  
ATOM    804  CE3 TRP E 126     135.703 154.543 133.759  1.00 39.78           C  
ATOM    805  CZ2 TRP E 126     135.942 157.355 133.911  1.00 33.61           C  
ATOM    806  CZ3 TRP E 126     134.761 155.311 134.411  1.00 32.64           C  
ATOM    807  CH2 TRP E 126     134.886 156.702 134.482  1.00 43.83           C  
ATOM    808  N   PRO E 127     138.983 151.204 129.158  1.00 12.64           N  
ATOM    809  CA  PRO E 127     139.194 149.786 128.838  1.00  9.77           C  
ATOM    810  C   PRO E 127     140.305 149.151 129.649  1.00 25.73           C  
ATOM    811  O   PRO E 127     140.213 147.963 129.980  1.00 41.19           O  
ATOM    812  CB  PRO E 127     139.534 149.808 127.340  1.00 27.25           C  
ATOM    813  CG  PRO E 127     139.308 151.232 126.882  1.00 26.74           C  
ATOM    814  CD  PRO E 127     139.471 152.084 128.089  1.00 17.58           C  
ATOM    815  N   ILE E 128     141.358 149.904 129.973  1.00 16.16           N  
ATOM    816  CA  ILE E 128     142.464 149.346 130.743  1.00 14.12           C  
ATOM    817  C   ILE E 128     141.992 148.938 132.132  1.00 33.52           C  
ATOM    818  O   ILE E 128     142.297 147.840 132.611  1.00 43.89           O  
ATOM    819  CB  ILE E 128     143.628 150.348 130.813  1.00 27.79           C  
ATOM    820  CG1 ILE E 128     144.052 150.762 129.405  1.00 29.62           C  
ATOM    821  CG2 ILE E 128     144.802 149.748 131.568  1.00 31.66           C  
ATOM    822  CD1 ILE E 128     144.619 149.627 128.585  1.00 36.23           C  
ATOM    823  N   TRP E 129     141.238 149.815 132.801  1.00 27.60           N  
ATOM    824  CA  TRP E 129     140.701 149.466 134.112  1.00 14.49           C  
ATOM    825  C   TRP E 129     139.754 148.282 134.014  1.00 12.44           C  
ATOM    826  O   TRP E 129     139.763 147.395 134.875  1.00 47.19           O  
ATOM    827  CB  TRP E 129     139.981 150.660 134.739  1.00 22.77           C  
ATOM    828  CG  TRP E 129     139.210 150.286 135.979  1.00 25.25           C  
ATOM    829  CD1 TRP E 129     139.674 150.288 137.261  1.00 29.17           C  
ATOM    830  CD2 TRP E 129     137.849 149.837 136.048  1.00 27.00           C  
ATOM    831  NE1 TRP E 129     138.689 149.876 138.123  1.00 30.56           N  
ATOM    832  CE2 TRP E 129     137.559 149.592 137.403  1.00 23.83           C  
ATOM    833  CE3 TRP E 129     136.849 149.622 135.097  1.00 30.13           C  
ATOM    834  CZ2 TRP E 129     136.313 149.144 137.829  1.00 22.29           C  
ATOM    835  CZ3 TRP E 129     135.613 149.177 135.523  1.00 29.38           C  
ATOM    836  CH2 TRP E 129     135.356 148.943 136.876  1.00 20.68           C  
ATOM    837  N   TYR E 130     138.920 148.258 132.977  1.00  0.00           N  
ATOM    838  CA  TYR E 130     137.981 147.157 132.805  1.00 11.02           C  
ATOM    839  C   TYR E 130     138.694 145.823 132.665  1.00 28.56           C  
ATOM    840  O   TYR E 130     138.331 144.843 133.326  1.00 34.38           O  
ATOM    841  CB  TYR E 130     137.107 147.409 131.583  1.00 14.29           C  
ATOM    842  CG  TYR E 130     135.851 146.590 131.579  1.00 12.76           C  
ATOM    843  CD1 TYR E 130     134.750 146.973 132.316  1.00 16.85           C  
ATOM    844  CD2 TYR E 130     135.772 145.419 130.841  1.00 24.54           C  
ATOM    845  CE1 TYR E 130     133.611 146.221 132.313  1.00 10.94           C  
ATOM    846  CE2 TYR E 130     134.629 144.659 130.833  1.00 23.08           C  
ATOM    847  CZ  TYR E 130     133.549 145.067 131.573  1.00 17.54           C  
ATOM    848  OH  TYR E 130     132.397 144.318 131.576  1.00 25.86           O  
ATOM    849  N   ARG E 131     139.709 145.761 131.812  1.00 29.40           N  
ATOM    850  CA  ARG E 131     140.336 144.485 131.503  1.00 24.19           C  
ATOM    851  C   ARG E 131     141.355 144.065 132.553  1.00 26.32           C  
ATOM    852  O   ARG E 131     141.518 142.864 132.798  1.00 38.77           O  
ATOM    853  CB  ARG E 131     140.982 144.553 130.116  1.00 20.29           C  
ATOM    854  CG  ARG E 131     142.020 143.490 129.832  1.00 32.44           C  
ATOM    855  CD  ARG E 131     141.983 143.097 128.368  1.00 35.13           C  
ATOM    856  NE  ARG E 131     140.621 143.104 127.846  1.00 38.23           N  
ATOM    857  CZ  ARG E 131     139.807 142.059 127.863  1.00 32.09           C  
ATOM    858  NH1 ARG E 131     140.182 140.899 128.377  1.00 32.23           N1+
ATOM    859  NH2 ARG E 131     138.585 142.179 127.352  1.00 28.77           N  
ATOM    860  N   CYS E 132     142.015 145.018 133.208  1.00 12.36           N  
ATOM    861  CA  CYS E 132     143.066 144.706 134.168  1.00 14.93           C  
ATOM    862  C   CYS E 132     142.613 144.884 135.613  1.00 32.66           C  
ATOM    863  O   CYS E 132     142.689 143.944 136.410  1.00 43.13           O  
ATOM    864  CB  CYS E 132     144.295 145.580 133.890  1.00 12.53           C  
ATOM    865  SG  CYS E 132     144.824 145.592 132.164  1.00 28.92           S  
ATOM    866  N   ARG E 133     142.127 146.071 135.965  1.00 31.02           N  
ATOM    867  CA  ARG E 133     141.941 146.448 137.360  1.00 26.35           C  
ATOM    868  C   ARG E 133     140.545 146.150 137.898  1.00 25.03           C  
ATOM    869  O   ARG E 133     140.245 146.533 139.032  1.00 29.69           O  
ATOM    870  CB  ARG E 133     142.263 147.932 137.550  1.00 24.14           C  
ATOM    871  CG  ARG E 133     143.299 148.469 136.580  1.00 25.19           C  
ATOM    872  CD  ARG E 133     143.729 149.872 136.964  1.00 28.52           C  
ATOM    873  NE  ARG E 133     144.417 150.553 135.874  1.00 30.99           N  
ATOM    874  CZ  ARG E 133     144.830 151.812 135.922  1.00 38.80           C  
ATOM    875  NH1 ARG E 133     144.642 152.560 136.996  1.00 35.70           N1+
ATOM    876  NH2 ARG E 133     145.449 152.333 134.866  1.00 37.66           N  
ATOM    877  N   ARG E 134     139.688 145.491 137.129  1.00 17.06           N  
ATOM    878  CA  ARG E 134     138.403 145.086 137.674  1.00 21.55           C  
ATOM    879  C   ARG E 134     138.598 143.926 138.648  1.00 47.18           C  
ATOM    880  O   ARG E 134     139.477 143.084 138.442  1.00 58.22           O  
ATOM    881  CB  ARG E 134     137.439 144.680 136.563  1.00 17.28           C  
ATOM    882  CG  ARG E 134     136.040 145.238 136.749  1.00 27.42           C  
ATOM    883  CD  ARG E 134     135.118 144.825 135.621  1.00 38.19           C  
ATOM    884  NE  ARG E 134     134.603 143.473 135.800  1.00 34.19           N  
ATOM    885  CZ  ARG E 134     133.333 143.184 136.045  1.00 34.74           C  
ATOM    886  NH1 ARG E 134     132.417 144.131 136.156  1.00 33.58           N1+
ATOM    887  NH2 ARG E 134     132.973 141.911 136.181  1.00 35.15           N  
ATOM    888  N   PRO E 135     137.807 143.862 139.724  1.00 48.45           N  
ATOM    889  CA  PRO E 135     137.982 142.788 140.714  1.00 41.30           C  
ATOM    890  C   PRO E 135     137.674 141.395 140.183  1.00 44.95           C  
ATOM    891  O   PRO E 135     137.900 140.404 140.884  1.00 53.99           O  
ATOM    892  CB  PRO E 135     137.000 143.182 141.830  1.00 43.36           C  
ATOM    893  CG  PRO E 135     136.123 144.244 141.216  1.00 42.42           C  
ATOM    894  CD  PRO E 135     137.025 144.966 140.290  1.00 51.03           C  
ATOM    895  N   THR E 136     137.141 141.311 138.961  1.00 51.14           N  
ATOM    896  CA  THR E 136     136.813 140.050 138.294  1.00 58.81           C  
ATOM    897  C   THR E 136     135.724 139.271 139.025  1.00 62.03           C  
ATOM    898  O   THR E 136     135.399 138.143 138.640  1.00 68.63           O  
ATOM    899  CB  THR E 136     138.057 139.167 138.120  1.00 60.79           C  
ATOM    900  OG1 THR E 136     138.371 138.520 139.360  1.00 52.70           O  
ATOM    901  CG2 THR E 136     139.254 139.981 137.632  1.00 57.49           C  
ATOM    902  N   HIS E 137     135.156 139.857 140.079  1.00 52.05           N  
ATOM    903  CA  HIS E 137     133.968 139.293 140.706  1.00 49.37           C  
ATOM    904  C   HIS E 137     132.931 140.369 140.993  1.00 51.68           C  
ATOM    905  O   HIS E 137     131.934 140.082 141.667  1.00 53.83           O  
ATOM    906  CB  HIS E 137     134.319 138.543 141.999  1.00 47.27           C  
ATOM    907  CG  HIS E 137     135.102 139.355 142.984  1.00 55.03           C  
ATOM    908  ND1 HIS E 137     134.582 140.464 143.616  1.00 57.33           N  
ATOM    909  CD2 HIS E 137     136.363 139.211 143.456  1.00 53.05           C  
ATOM    910  CE1 HIS E 137     135.491 140.972 144.429  1.00 54.08           C  
ATOM    911  NE2 HIS E 137     136.581 140.231 144.350  1.00 55.26           N  
ATOM    912  N   LEU E 138     133.140 141.596 140.508  1.00 43.83           N  
ATOM    913  CA  LEU E 138     132.162 142.659 140.699  1.00 37.56           C  
ATOM    914  C   LEU E 138     130.851 142.330 140.002  1.00 36.28           C  
ATOM    915  O   LEU E 138     129.789 142.781 140.439  1.00 38.51           O  
ATOM    916  CB  LEU E 138     132.750 143.984 140.199  1.00 39.13           C  
ATOM    917  CG  LEU E 138     132.102 145.377 140.245  1.00 43.20           C  
ATOM    918  CD1 LEU E 138     133.106 146.385 139.715  1.00 45.93           C  
ATOM    919  CD2 LEU E 138     130.814 145.506 139.446  1.00 47.63           C  
ATOM    920  N   SER E 139     130.903 141.544 138.926  1.00 43.09           N  
ATOM    921  CA  SER E 139     129.683 141.188 138.210  1.00 42.07           C  
ATOM    922  C   SER E 139     128.718 140.431 139.113  1.00 38.91           C  
ATOM    923  O   SER E 139     127.533 140.766 139.190  1.00 44.64           O  
ATOM    924  CB  SER E 139     130.025 140.360 136.973  1.00 48.88           C  
ATOM    925  OG  SER E 139     128.873 139.714 136.463  1.00 41.10           O  
ATOM    926  N   ALA E 140     129.214 139.414 139.820  1.00 42.28           N  
ATOM    927  CA  ALA E 140     128.349 138.641 140.707  1.00 43.85           C  
ATOM    928  C   ALA E 140     127.851 139.485 141.873  1.00 45.58           C  
ATOM    929  O   ALA E 140     126.689 139.366 142.281  1.00 46.96           O  
ATOM    930  CB  ALA E 140     129.090 137.406 141.215  1.00 41.21           C  
ATOM    931  N   VAL E 141     128.713 140.341 142.424  1.00 39.19           N  
ATOM    932  CA  VAL E 141     128.313 141.177 143.554  1.00 37.50           C  
ATOM    933  C   VAL E 141     127.203 142.135 143.141  1.00 42.20           C  
ATOM    934  O   VAL E 141     126.182 142.262 143.825  1.00 52.26           O  
ATOM    935  CB  VAL E 141     129.528 141.934 144.118  1.00 42.99           C  
ATOM    936  CG1 VAL E 141     129.093 142.887 145.217  1.00 36.65           C  
ATOM    937  CG2 VAL E 141     130.566 140.953 144.637  1.00 49.19           C  
ATOM    938  N   VAL E 142     127.380 142.818 142.009  1.00 44.02           N  
ATOM    939  CA  VAL E 142     126.352 143.753 141.567  1.00 42.34           C  
ATOM    940  C   VAL E 142     125.100 143.005 141.132  1.00 42.10           C  
ATOM    941  O   VAL E 142     123.988 143.514 141.286  1.00 45.66           O  
ATOM    942  CB  VAL E 142     126.886 144.674 140.455  1.00 39.30           C  
ATOM    943  CG1 VAL E 142     127.046 143.918 139.161  1.00 46.16           C  
ATOM    944  CG2 VAL E 142     125.960 145.864 140.267  1.00 43.62           C  
ATOM    945  N   CYS E 143     125.246 141.786 140.610  1.00 40.96           N  
ATOM    946  CA  CYS E 143     124.077 140.990 140.261  1.00 40.38           C  
ATOM    947  C   CYS E 143     123.248 140.662 141.495  1.00 42.83           C  
ATOM    948  O   CYS E 143     122.021 140.812 141.492  1.00 51.36           O  
ATOM    949  CB  CYS E 143     124.516 139.712 139.547  1.00 46.88           C  
ATOM    950  SG  CYS E 143     123.213 138.483 139.363  1.00 61.77           S  
ATOM    951  N   VAL E 144     123.904 140.217 142.570  1.00 33.14           N  
ATOM    952  CA  VAL E 144     123.147 139.875 143.769  1.00 37.64           C  
ATOM    953  C   VAL E 144     122.593 141.130 144.435  1.00 38.94           C  
ATOM    954  O   VAL E 144     121.506 141.093 145.022  1.00 48.56           O  
ATOM    955  CB  VAL E 144     123.988 139.022 144.739  1.00 46.61           C  
ATOM    956  CG1 VAL E 144     124.509 137.780 144.032  1.00 40.83           C  
ATOM    957  CG2 VAL E 144     125.128 139.820 145.339  1.00 50.65           C  
ATOM    958  N   LEU E 145     123.299 142.263 144.343  1.00 33.86           N  
ATOM    959  CA  LEU E 145     122.730 143.512 144.848  1.00 35.52           C  
ATOM    960  C   LEU E 145     121.489 143.916 144.060  1.00 45.80           C  
ATOM    961  O   LEU E 145     120.500 144.375 144.642  1.00 46.65           O  
ATOM    962  CB  LEU E 145     123.768 144.634 144.820  1.00 43.06           C  
ATOM    963  CG  LEU E 145     125.052 144.466 145.634  1.00 50.68           C  
ATOM    964  CD1 LEU E 145     125.666 145.820 145.942  1.00 45.81           C  
ATOM    965  CD2 LEU E 145     124.784 143.699 146.919  1.00 46.24           C  
ATOM    966  N   LEU E 146     121.522 143.760 142.734  1.00 55.54           N  
ATOM    967  CA  LEU E 146     120.349 144.068 141.922  1.00 47.51           C  
ATOM    968  C   LEU E 146     119.190 143.142 142.257  1.00 50.58           C  
ATOM    969  O   LEU E 146     118.041 143.585 142.352  1.00 55.50           O  
ATOM    970  CB  LEU E 146     120.691 143.980 140.436  1.00 39.38           C  
ATOM    971  CG  LEU E 146     121.621 145.064 139.893  1.00 49.75           C  
ATOM    972  CD1 LEU E 146     121.733 144.965 138.383  1.00 48.10           C  
ATOM    973  CD2 LEU E 146     121.131 146.440 140.307  1.00 57.12           C  
ATOM    974  N   TRP E 147     119.470 141.851 142.447  1.00 42.18           N  
ATOM    975  CA  TRP E 147     118.412 140.922 142.834  1.00 37.26           C  
ATOM    976  C   TRP E 147     117.821 141.300 144.187  1.00 38.59           C  
ATOM    977  O   TRP E 147     116.596 141.288 144.365  1.00 43.63           O  
ATOM    978  CB  TRP E 147     118.951 139.493 142.868  1.00 40.13           C  
ATOM    979  CG  TRP E 147     119.032 138.833 141.527  1.00 34.42           C  
ATOM    980  CD1 TRP E 147     120.137 138.712 140.743  1.00 35.58           C  
ATOM    981  CD2 TRP E 147     117.967 138.193 140.817  1.00 33.27           C  
ATOM    982  NE1 TRP E 147     119.830 138.041 139.588  1.00 38.55           N  
ATOM    983  CE2 TRP E 147     118.502 137.711 139.608  1.00 34.94           C  
ATOM    984  CE3 TRP E 147     116.613 137.981 141.086  1.00 39.30           C  
ATOM    985  CZ2 TRP E 147     117.732 137.031 138.670  1.00 39.46           C  
ATOM    986  CZ3 TRP E 147     115.849 137.306 140.152  1.00 43.57           C  
ATOM    987  CH2 TRP E 147     116.411 136.839 138.960  1.00 44.60           C  
ATOM    988  N   GLY E 148     118.676 141.653 145.148  1.00 49.01           N  
ATOM    989  CA  GLY E 148     118.186 142.038 146.461  1.00 50.37           C  
ATOM    990  C   GLY E 148     117.355 143.305 146.428  1.00 51.49           C  
ATOM    991  O   GLY E 148     116.331 143.404 147.107  1.00 60.37           O  
ATOM    992  N   LEU E 149     117.785 144.293 145.641  1.00 43.92           N  
ATOM    993  CA  LEU E 149     117.004 145.515 145.494  1.00 44.53           C  
ATOM    994  C   LEU E 149     115.735 145.282 144.689  1.00 43.94           C  
ATOM    995  O   LEU E 149     114.799 146.082 144.786  1.00 44.29           O  
ATOM    996  CB  LEU E 149     117.848 146.608 144.837  1.00 48.88           C  
ATOM    997  CG  LEU E 149     118.612 147.567 145.757  1.00 54.23           C  
ATOM    998  CD1 LEU E 149     117.720 148.716 146.188  1.00 50.50           C  
ATOM    999  CD2 LEU E 149     119.184 146.850 146.972  1.00 55.97           C  
ATOM   1000  N   SER E 150     115.690 144.217 143.888  1.00 52.75           N  
ATOM   1001  CA  SER E 150     114.454 143.838 143.215  1.00 56.28           C  
ATOM   1002  C   SER E 150     113.487 143.158 144.175  1.00 57.08           C  
ATOM   1003  O   SER E 150     112.267 143.274 144.014  1.00 61.20           O  
ATOM   1004  CB  SER E 150     114.764 142.932 142.025  1.00 56.33           C  
ATOM   1005  OG  SER E 150     115.878 143.416 141.295  1.00 59.83           O  
ATOM   1006  N   LEU E 151     114.009 142.432 145.171  1.00 62.25           N  
ATOM   1007  CA  LEU E 151     113.160 142.029 146.289  1.00 61.52           C  
ATOM   1008  C   LEU E 151     112.544 143.251 146.954  1.00 64.70           C  
ATOM   1009  O   LEU E 151     111.339 143.282 147.227  1.00 66.75           O  
ATOM   1010  CB  LEU E 151     113.950 141.216 147.318  1.00 62.73           C  
ATOM   1011  CG  LEU E 151     115.079 140.264 146.925  1.00 66.73           C  
ATOM   1012  CD1 LEU E 151     115.539 139.473 148.136  1.00 64.51           C  
ATOM   1013  CD2 LEU E 151     114.595 139.307 145.856  1.00 63.55           C  
ATOM   1014  N   LEU E 152     113.358 144.270 147.213  1.00 65.16           N  
ATOM   1015  CA  LEU E 152     112.850 145.554 147.656  1.00 60.95           C  
ATOM   1016  C   LEU E 152     112.161 146.257 146.487  1.00 63.42           C  
ATOM   1017  O   LEU E 152     112.134 145.762 145.357  1.00 61.12           O  
ATOM   1018  CB  LEU E 152     113.991 146.403 148.220  1.00 59.81           C  
ATOM   1019  CG  LEU E 152     113.694 147.588 149.143  1.00 60.08           C  
ATOM   1020  CD1 LEU E 152     112.740 147.182 150.252  1.00 60.33           C  
ATOM   1021  CD2 LEU E 152     114.984 148.157 149.717  1.00 61.89           C  
ATOM   1022  N   PHE E 153     111.572 147.416 146.775  1.00 70.41           N  
ATOM   1023  CA  PHE E 153     110.879 148.234 145.782  1.00 70.09           C  
ATOM   1024  C   PHE E 153     109.743 147.483 145.094  1.00 73.35           C  
ATOM   1025  O   PHE E 153     109.216 147.944 144.077  1.00 79.63           O  
ATOM   1026  CB  PHE E 153     111.857 148.788 144.739  1.00 68.80           C  
ATOM   1027  CG  PHE E 153     112.846 149.769 145.298  1.00 70.42           C  
ATOM   1028  CD1 PHE E 153     112.486 150.629 146.322  1.00 71.32           C  
ATOM   1029  CD2 PHE E 153     114.131 149.839 144.794  1.00 69.77           C  
ATOM   1030  CE1 PHE E 153     113.393 151.535 146.835  1.00 70.65           C  
ATOM   1031  CE2 PHE E 153     115.039 150.745 145.301  1.00 69.96           C  
ATOM   1032  CZ  PHE E 153     114.671 151.592 146.323  1.00 71.37           C  
ATOM   1033  N   SER E 154     109.352 146.330 145.628  1.00 80.30           N  
ATOM   1034  CA  SER E 154     108.171 145.616 145.168  1.00 83.07           C  
ATOM   1035  C   SER E 154     106.927 145.998 145.955  1.00 82.84           C  
ATOM   1036  O   SER E 154     105.859 145.422 145.724  1.00 83.13           O  
ATOM   1037  CB  SER E 154     108.396 144.104 145.254  1.00 78.85           C  
ATOM   1038  N   MET E 155     107.045 146.951 146.877  1.00 82.32           N  
ATOM   1039  CA  MET E 155     105.940 147.407 147.716  1.00 85.82           C  
ATOM   1040  C   MET E 155     105.380 148.739 147.238  1.00 89.75           C  
ATOM   1041  O   MET E 155     105.046 149.608 148.048  1.00 91.45           O  
ATOM   1042  CB  MET E 155     106.383 147.504 149.173  1.00 86.13           C  
ATOM   1043  CG  MET E 155     106.636 146.164 149.852  1.00 88.43           C  
ATOM   1044  SD  MET E 155     107.849 145.125 149.016  1.00 83.08           S  
ATOM   1045  CE  MET E 155     109.370 145.905 149.543  1.00 84.51           C  
ATOM   1046  N   LEU E 156     105.281 148.933 145.921  1.00 85.76           N  
ATOM   1047  CA  LEU E 156     104.710 150.169 145.397  1.00 86.41           C  
ATOM   1048  C   LEU E 156     103.220 150.255 145.704  1.00 91.39           C  
ATOM   1049  O   LEU E 156     102.776 151.129 146.458  1.00 89.44           O  
ATOM   1050  CB  LEU E 156     104.955 150.260 143.890  1.00 85.20           C  
ATOM   1051  N   GLU E 157     102.431 149.340 145.141  1.00 94.98           N  
ATOM   1052  CA  GLU E 157     100.993 149.307 145.369  1.00 92.78           C  
ATOM   1053  C   GLU E 157     100.624 148.734 146.731  1.00 92.31           C  
ATOM   1054  O   GLU E 157      99.579 149.101 147.278  1.00 93.97           O  
ATOM   1055  CB  GLU E 157     100.303 148.497 144.261  1.00 91.35           C  
ATOM   1056  CG  GLU E 157      98.814 148.241 144.470  1.00 89.77           C  
ATOM   1057  CD  GLU E 157      97.981 149.510 144.424  1.00 88.83           C  
ATOM   1058  OE1 GLU E 157      97.841 150.177 145.470  1.00 84.99           O  
ATOM   1059  OE2 GLU E 157      97.459 149.839 143.338  1.00 91.81           O1-
ATOM   1060  N   TRP E 158     101.473 147.886 147.310  1.00 88.39           N  
ATOM   1061  CA  TRP E 158     101.133 147.171 148.539  1.00 85.62           C  
ATOM   1062  C   TRP E 158     101.152 148.099 149.753  1.00 85.47           C  
ATOM   1063  O   TRP E 158     102.031 148.048 150.611  1.00 88.06           O  
ATOM   1064  CB  TRP E 158     102.065 145.986 148.734  1.00 85.12           C  
ATOM   1065  CG  TRP E 158     101.793 144.890 147.772  1.00 87.50           C  
ATOM   1066  CD1 TRP E 158     102.641 144.395 146.831  1.00 82.59           C  
ATOM   1067  CD2 TRP E 158     100.576 144.142 147.656  1.00 89.59           C  
ATOM   1068  NE1 TRP E 158     102.027 143.385 146.134  1.00 84.86           N  
ATOM   1069  CE2 TRP E 158     100.759 143.210 146.621  1.00 86.13           C  
ATOM   1070  CE3 TRP E 158      99.350 144.171 148.328  1.00 87.80           C  
ATOM   1071  CZ2 TRP E 158      99.763 142.313 146.241  1.00 84.56           C  
ATOM   1072  CZ3 TRP E 158      98.363 143.282 147.948  1.00 86.34           C  
ATOM   1073  CH2 TRP E 158      98.575 142.366 146.914  1.00 85.77           C  
ATOM   1074  N   ARG E 159     100.141 148.960 149.807  1.00 99.62           N  
ATOM   1075  CA  ARG E 159      99.816 149.693 151.027  1.00102.47           C  
ATOM   1076  C   ARG E 159      98.863 148.881 151.897  1.00103.58           C  
ATOM   1077  O   ARG E 159      97.822 149.359 152.345  1.00102.56           O  
ATOM   1078  CB  ARG E 159      99.224 151.053 150.678  1.00 99.89           C  
ATOM   1079  N   PHE E 160      99.231 147.625 152.135  1.00104.43           N  
ATOM   1080  CA  PHE E 160      98.430 146.681 152.902  1.00103.35           C  
ATOM   1081  C   PHE E 160      99.218 146.243 154.128  1.00103.51           C  
ATOM   1082  O   PHE E 160     100.207 145.515 154.000  1.00100.59           O  
ATOM   1083  CB  PHE E 160      98.054 145.460 152.057  1.00103.24           C  
ATOM   1084  CG  PHE E 160      96.879 145.680 151.139  1.00104.27           C  
ATOM   1085  CD1 PHE E 160      96.478 146.958 150.784  1.00104.52           C  
ATOM   1086  CD2 PHE E 160      96.177 144.601 150.627  1.00103.51           C  
ATOM   1087  CE1 PHE E 160      95.400 147.155 149.940  1.00102.75           C  
ATOM   1088  CE2 PHE E 160      95.099 144.793 149.783  1.00104.73           C  
ATOM   1089  CZ  PHE E 160      94.710 146.071 149.439  1.00102.90           C  
ATOM   1090  N   CYS E 161      98.782 146.701 155.304  1.00113.57           N  
ATOM   1091  CA  CYS E 161      99.394 146.346 156.591  1.00115.38           C  
ATOM   1092  C   CYS E 161     100.909 146.564 156.589  1.00116.41           C  
ATOM   1093  O   CYS E 161     101.658 145.851 157.262  1.00116.24           O  
ATOM   1094  CB  CYS E 161      99.036 144.908 156.997  1.00113.19           C  
ATOM   1095  SG  CYS E 161     100.000 143.561 156.253  1.00112.65           S  
ATOM   1096  N   ASP E 162     101.369 147.573 155.846  1.00111.68           N  
ATOM   1097  CA  ASP E 162     102.797 147.873 155.802  1.00109.31           C  
ATOM   1098  C   ASP E 162     103.306 148.340 157.161  1.00112.15           C  
ATOM   1099  O   ASP E 162     104.405 147.967 157.587  1.00112.28           O  
ATOM   1100  CB  ASP E 162     103.082 148.920 154.726  1.00107.10           C  
ATOM   1101  CG  ASP E 162     103.771 148.333 153.512  1.00109.54           C  
ATOM   1102  OD1 ASP E 162     103.965 147.100 153.475  1.00108.44           O  
ATOM   1103  OD2 ASP E 162     104.122 149.103 152.595  1.00111.82           O1-
ATOM   1104  N   PHE E 163     102.522 149.161 157.856  1.00113.84           N  
ATOM   1105  CA  PHE E 163     102.885 149.662 159.177  1.00111.82           C  
ATOM   1106  C   PHE E 163     102.583 148.573 160.199  1.00110.22           C  
ATOM   1107  O   PHE E 163     101.423 148.361 160.568  1.00109.10           O  
ATOM   1108  CB  PHE E 163     102.128 150.946 159.506  1.00110.60           C  
ATOM   1109  N   LEU E 164     103.627 147.887 160.654  1.00109.80           N  
ATOM   1110  CA  LEU E 164     103.506 146.797 161.615  1.00111.97           C  
ATOM   1111  C   LEU E 164     104.073 147.196 162.974  1.00112.91           C  
ATOM   1112  O   LEU E 164     104.378 146.347 163.814  1.00112.66           O  
ATOM   1113  CB  LEU E 164     104.199 145.541 161.091  1.00111.30           C  
ATOM   1114  CG  LEU E 164     103.489 144.786 159.965  1.00111.19           C  
ATOM   1115  CD1 LEU E 164     104.498 144.123 159.042  1.00107.57           C  
ATOM   1116  CD2 LEU E 164     102.523 143.759 160.534  1.00111.79           C  
ATOM   1117  N   PHE E 165     104.218 148.497 163.202  1.00114.00           N  
ATOM   1118  CA  PHE E 165     104.778 148.999 164.450  1.00112.77           C  
ATOM   1119  C   PHE E 165     103.809 149.954 165.140  1.00112.19           C  
ATOM   1120  O   PHE E 165     103.899 151.171 164.974  1.00112.17           O  
ATOM   1121  CB  PHE E 165     106.115 149.698 164.194  1.00113.73           C  
ATOM   1122  CG  PHE E 165     106.944 149.049 163.121  1.00116.09           C  
ATOM   1123  CD1 PHE E 165     107.356 147.731 163.245  1.00114.56           C  
ATOM   1124  CD2 PHE E 165     107.310 149.755 161.986  1.00115.20           C  
ATOM   1125  CE1 PHE E 165     108.117 147.132 162.259  1.00113.28           C  
ATOM   1126  CE2 PHE E 165     108.071 149.160 160.996  1.00112.06           C  
ATOM   1127  CZ  PHE E 165     108.474 147.847 161.133  1.00112.15           C  
ATOM   1128  N   SER E 170     106.501 153.447 161.037  1.00102.21           N  
ATOM   1129  CA  SER E 170     105.460 154.444 161.260  1.00104.24           C  
ATOM   1130  C   SER E 170     105.559 155.578 160.243  1.00105.67           C  
ATOM   1131  O   SER E 170     104.551 156.017 159.692  1.00106.23           O  
ATOM   1132  CB  SER E 170     105.545 154.999 162.683  1.00103.81           C  
ATOM   1133  OG  SER E 170     104.617 156.051 162.878  1.00101.58           O  
ATOM   1134  N   SER E 171     106.782 156.049 159.997  1.00112.17           N  
ATOM   1135  CA  SER E 171     107.022 157.103 159.010  1.00111.68           C  
ATOM   1136  C   SER E 171     107.129 156.472 157.621  1.00112.73           C  
ATOM   1137  O   SER E 171     108.202 156.337 157.031  1.00111.80           O  
ATOM   1138  CB  SER E 171     108.268 157.900 159.370  1.00111.44           C  
ATOM   1139  OG  SER E 171     108.492 158.942 158.436  1.00112.18           O  
ATOM   1140  N   TRP E 172     105.968 156.077 157.108  1.00116.51           N  
ATOM   1141  CA  TRP E 172     105.851 155.356 155.851  1.00114.43           C  
ATOM   1142  C   TRP E 172     104.774 156.010 154.995  1.00114.43           C  
ATOM   1143  O   TRP E 172     103.680 156.322 155.476  1.00113.35           O  
ATOM   1144  CB  TRP E 172     105.554 153.867 156.131  1.00114.12           C  
ATOM   1145  CG  TRP E 172     104.104 153.475 156.162  1.00116.50           C  
ATOM   1146  CD1 TRP E 172     103.323 153.339 157.271  1.00116.03           C  
ATOM   1147  CD2 TRP E 172     103.301 153.043 155.056  1.00116.32           C  
ATOM   1148  NE1 TRP E 172     102.062 152.924 156.919  1.00115.64           N  
ATOM   1149  CE2 TRP E 172     102.025 152.725 155.565  1.00115.70           C  
ATOM   1150  CE3 TRP E 172     103.526 152.921 153.682  1.00116.38           C  
ATOM   1151  CZ2 TRP E 172     100.981 152.294 154.750  1.00114.70           C  
ATOM   1152  CZ3 TRP E 172     102.485 152.492 152.874  1.00114.49           C  
ATOM   1153  CH2 TRP E 172     101.231 152.186 153.411  1.00113.61           C  
ATOM   1154  N   CYS E 173     105.103 156.240 153.725  1.00111.99           N  
ATOM   1155  CA  CYS E 173     104.243 157.004 152.825  1.00113.24           C  
ATOM   1156  C   CYS E 173     102.957 156.226 152.576  1.00111.41           C  
ATOM   1157  O   CYS E 173     102.949 155.258 151.809  1.00111.39           O  
ATOM   1158  CB  CYS E 173     104.969 157.302 151.516  1.00112.48           C  
ATOM   1159  SG  CYS E 173     106.551 158.155 151.718  1.00115.49           S  
ATOM   1160  N   GLU E 174     101.865 156.672 153.204  1.00104.97           N  
ATOM   1161  CA  GLU E 174     100.608 155.933 153.207  1.00106.22           C  
ATOM   1162  C   GLU E 174     100.127 155.580 151.802  1.00107.62           C  
ATOM   1163  O   GLU E 174      99.951 154.402 151.473  1.00107.25           O  
ATOM   1164  CB  GLU E 174      99.540 156.743 153.950  1.00105.95           C  
ATOM   1165  CG  GLU E 174      99.648 156.676 155.467  1.00106.97           C  
ATOM   1166  CD  GLU E 174     100.844 157.438 156.008  1.00107.60           C  
ATOM   1167  OE1 GLU E 174     101.295 158.391 155.340  1.00107.76           O  
ATOM   1168  OE2 GLU E 174     101.335 157.079 157.099  1.00105.18           O1-
ATOM   1169  N   THR E 175      99.915 156.587 150.956  1.00101.77           N  
ATOM   1170  CA  THR E 175      99.386 156.330 149.621  1.00 98.94           C  
ATOM   1171  C   THR E 175     100.356 156.785 148.537  1.00 98.48           C  
ATOM   1172  O   THR E 175     100.574 156.070 147.553  1.00 94.61           O  
ATOM   1173  CB  THR E 175      98.032 157.024 149.439  1.00 99.14           C  
ATOM   1174  OG1 THR E 175      97.091 156.499 150.384  1.00 99.20           O  
ATOM   1175  CG2 THR E 175      97.501 156.807 148.031  1.00 99.97           C  
ATOM   1176  N   SER E 176     100.954 157.962 148.715  1.00101.40           N  
ATOM   1177  CA  SER E 176     101.842 158.538 147.706  1.00101.03           C  
ATOM   1178  C   SER E 176     103.272 158.083 147.986  1.00 99.99           C  
ATOM   1179  O   SER E 176     104.168 158.872 148.299  1.00 99.33           O  
ATOM   1180  CB  SER E 176     101.723 160.056 147.689  1.00 98.72           C  
ATOM   1181  OG  SER E 176     101.538 160.572 148.993  1.00 95.74           O  
ATOM   1182  N   ASP E 177     103.484 156.776 147.866  1.00 92.36           N  
ATOM   1183  CA  ASP E 177     104.799 156.158 148.007  1.00 90.58           C  
ATOM   1184  C   ASP E 177     105.402 156.024 146.612  1.00 92.85           C  
ATOM   1185  O   ASP E 177     105.100 155.074 145.883  1.00 94.34           O  
ATOM   1186  CB  ASP E 177     104.693 154.806 148.705  1.00 89.12           C  
ATOM   1187  CG  ASP E 177     106.031 154.293 149.183  1.00 90.72           C  
ATOM   1188  OD1 ASP E 177     106.837 153.856 148.334  1.00 89.78           O  
ATOM   1189  OD2 ASP E 177     106.278 154.324 150.406  1.00 91.76           O1-
ATOM   1190  N   PHE E 178     106.260 156.975 146.247  1.00 84.93           N  
ATOM   1191  CA  PHE E 178     106.839 157.006 144.910  1.00 79.32           C  
ATOM   1192  C   PHE E 178     108.329 156.692 144.940  1.00 78.83           C  
ATOM   1193  O   PHE E 178     109.096 157.226 144.133  1.00 78.34           O  
ATOM   1194  CB  PHE E 178     106.601 158.370 144.259  1.00 77.09           C  
ATOM   1195  N   ILE E 179     108.749 155.834 145.864  1.00 79.89           N  
ATOM   1196  CA  ILE E 179     110.150 155.423 145.953  1.00 83.66           C  
ATOM   1197  C   ILE E 179     110.451 154.352 144.906  1.00 84.60           C  
ATOM   1198  O   ILE E 179     111.498 154.434 144.245  1.00 83.19           O  
ATOM   1199  CB  ILE E 179     110.507 154.951 147.373  1.00 81.41           C  
ATOM   1200  CG1 ILE E 179     109.915 155.901 148.417  1.00 77.11           C  
ATOM   1201  CG2 ILE E 179     112.016 154.849 147.537  1.00 82.31           C  
ATOM   1202  CD1 ILE E 179     110.427 157.322 148.315  1.00 76.46           C  
ATOM   1203  N   PRO E 180     109.608 153.324 144.720  1.00 77.56           N  
ATOM   1204  CA  PRO E 180     109.825 152.429 143.568  1.00 73.39           C  
ATOM   1205  C   PRO E 180     109.751 153.143 142.230  1.00 74.26           C  
ATOM   1206  O   PRO E 180     110.475 152.771 141.298  1.00 76.93           O  
ATOM   1207  CB  PRO E 180     108.716 151.376 143.698  1.00 77.14           C  
ATOM   1208  CG  PRO E 180     108.001 151.653 144.945  1.00 78.93           C  
ATOM   1209  CD  PRO E 180     108.605 152.793 145.661  1.00 71.83           C  
ATOM   1210  N   VAL E 181     108.895 154.159 142.104  1.00 62.43           N  
ATOM   1211  CA  VAL E 181     108.878 154.962 140.885  1.00 58.07           C  
ATOM   1212  C   VAL E 181     110.204 155.687 140.714  1.00 59.03           C  
ATOM   1213  O   VAL E 181     110.725 155.807 139.599  1.00 66.83           O  
ATOM   1214  CB  VAL E 181     107.696 155.947 140.901  1.00 64.04           C  
ATOM   1215  CG1 VAL E 181     107.493 156.546 139.518  1.00 60.64           C  
ATOM   1216  CG2 VAL E 181     106.438 155.248 141.362  1.00 68.00           C  
ATOM   1217  N   ALA E 182     110.762 156.196 141.814  1.00 57.68           N  
ATOM   1218  CA  ALA E 182     112.074 156.828 141.749  1.00 59.96           C  
ATOM   1219  C   ALA E 182     113.137 155.836 141.300  1.00 60.98           C  
ATOM   1220  O   ALA E 182     114.004 156.173 140.489  1.00 67.59           O  
ATOM   1221  CB  ALA E 182     112.437 157.428 143.106  1.00 62.83           C  
ATOM   1222  N   TRP E 183     113.081 154.604 141.809  1.00 54.93           N  
ATOM   1223  CA  TRP E 183     114.037 153.582 141.389  1.00 50.73           C  
ATOM   1224  C   TRP E 183     113.902 153.270 139.904  1.00 51.04           C  
ATOM   1225  O   TRP E 183     114.906 153.145 139.193  1.00 56.22           O  
ATOM   1226  CB  TRP E 183     113.837 152.315 142.220  1.00 58.82           C  
ATOM   1227  CG  TRP E 183     114.707 151.167 141.813  1.00 57.63           C  
ATOM   1228  CD1 TRP E 183     114.302 149.998 141.239  1.00 57.59           C  
ATOM   1229  CD2 TRP E 183     116.126 151.066 141.971  1.00 54.96           C  
ATOM   1230  NE1 TRP E 183     115.382 149.179 141.020  1.00 56.70           N  
ATOM   1231  CE2 TRP E 183     116.514 149.812 141.461  1.00 55.96           C  
ATOM   1232  CE3 TRP E 183     117.107 151.916 142.489  1.00 56.05           C  
ATOM   1233  CZ2 TRP E 183     117.840 149.388 141.454  1.00 54.31           C  
ATOM   1234  CZ3 TRP E 183     118.422 151.493 142.481  1.00 59.19           C  
ATOM   1235  CH2 TRP E 183     118.776 150.241 141.967  1.00 57.14           C  
ATOM   1236  N   LEU E 184     112.667 153.140 139.418  1.00 51.03           N  
ATOM   1237  CA  LEU E 184     112.455 152.841 138.005  1.00 47.20           C  
ATOM   1238  C   LEU E 184     112.939 153.980 137.117  1.00 48.43           C  
ATOM   1239  O   LEU E 184     113.590 153.743 136.089  1.00 58.29           O  
ATOM   1240  CB  LEU E 184     110.977 152.554 137.750  1.00 50.03           C  
ATOM   1241  CG  LEU E 184     110.490 152.693 136.308  1.00 56.99           C  
ATOM   1242  CD1 LEU E 184     111.083 151.601 135.432  1.00 54.35           C  
ATOM   1243  CD2 LEU E 184     108.972 152.664 136.258  1.00 59.09           C  
ATOM   1244  N   ILE E 185     112.632 155.224 137.492  1.00 39.51           N  
ATOM   1245  CA  ILE E 185     113.076 156.353 136.687  1.00 38.40           C  
ATOM   1246  C   ILE E 185     114.590 156.491 136.752  1.00 43.60           C  
ATOM   1247  O   ILE E 185     115.223 156.887 135.767  1.00 47.63           O  
ATOM   1248  CB  ILE E 185     112.347 157.645 137.111  1.00 40.67           C  
ATOM   1249  CG1 ILE E 185     112.252 158.608 135.927  1.00 49.35           C  
ATOM   1250  CG2 ILE E 185     113.031 158.318 138.290  1.00 42.62           C  
ATOM   1251  CD1 ILE E 185     111.416 158.084 134.780  1.00 48.62           C  
ATOM   1252  N   PHE E 186     115.202 156.145 137.888  1.00 46.65           N  
ATOM   1253  CA  PHE E 186     116.656 156.147 137.973  1.00 44.60           C  
ATOM   1254  C   PHE E 186     117.256 155.109 137.039  1.00 43.75           C  
ATOM   1255  O   PHE E 186     118.252 155.378 136.362  1.00 54.12           O  
ATOM   1256  CB  PHE E 186     117.103 155.892 139.411  1.00 43.40           C  
ATOM   1257  CG  PHE E 186     118.447 155.236 139.518  1.00 45.66           C  
ATOM   1258  CD1 PHE E 186     119.606 155.978 139.370  1.00 54.23           C  
ATOM   1259  CD2 PHE E 186     118.554 153.879 139.766  1.00 48.72           C  
ATOM   1260  CE1 PHE E 186     120.846 155.379 139.467  1.00 57.30           C  
ATOM   1261  CE2 PHE E 186     119.791 153.273 139.862  1.00 54.17           C  
ATOM   1262  CZ  PHE E 186     120.939 154.024 139.714  1.00 55.74           C  
ATOM   1263  N   LEU E 187     116.665 153.914 136.993  1.00 37.80           N  
ATOM   1264  CA  LEU E 187     117.151 152.882 136.081  1.00 32.94           C  
ATOM   1265  C   LEU E 187     117.051 153.344 134.633  1.00 35.35           C  
ATOM   1266  O   LEU E 187     118.004 153.211 133.854  1.00 42.08           O  
ATOM   1267  CB  LEU E 187     116.360 151.592 136.287  1.00 42.58           C  
ATOM   1268  CG  LEU E 187     116.805 150.677 137.427  1.00 48.87           C  
ATOM   1269  CD1 LEU E 187     116.033 149.371 137.381  1.00 42.85           C  
ATOM   1270  CD2 LEU E 187     118.300 150.422 137.356  1.00 45.47           C  
ATOM   1271  N   CYS E 188     115.902 153.909 134.260  1.00 31.16           N  
ATOM   1272  CA  CYS E 188     115.717 154.364 132.886  1.00 38.92           C  
ATOM   1273  C   CYS E 188     116.706 155.469 132.534  1.00 44.08           C  
ATOM   1274  O   CYS E 188     117.339 155.440 131.469  1.00 48.27           O  
ATOM   1275  CB  CYS E 188     114.281 154.840 132.681  1.00 45.78           C  
ATOM   1276  SG  CYS E 188     114.004 155.698 131.116  1.00 62.24           S  
ATOM   1277  N   VAL E 189     116.870 156.448 133.427  1.00 40.18           N  
ATOM   1278  CA  VAL E 189     117.734 157.580 133.122  1.00 38.01           C  
ATOM   1279  C   VAL E 189     119.196 157.155 133.105  1.00 37.43           C  
ATOM   1280  O   VAL E 189     119.986 157.664 132.303  1.00 38.41           O  
ATOM   1281  CB  VAL E 189     117.477 158.743 134.101  1.00 43.70           C  
ATOM   1282  CG1 VAL E 189     118.060 158.457 135.474  1.00 44.39           C  
ATOM   1283  CG2 VAL E 189     118.040 160.038 133.538  1.00 49.69           C  
ATOM   1284  N   VAL E 190     119.587 156.215 133.969  1.00 37.26           N  
ATOM   1285  CA  VAL E 190     120.978 155.776 133.975  1.00 34.11           C  
ATOM   1286  C   VAL E 190     121.282 154.957 132.728  1.00 34.38           C  
ATOM   1287  O   VAL E 190     122.368 155.073 132.151  1.00 50.58           O  
ATOM   1288  CB  VAL E 190     121.315 155.020 135.276  1.00 39.66           C  
ATOM   1289  CG1 VAL E 190     120.731 153.625 135.287  1.00 48.11           C  
ATOM   1290  CG2 VAL E 190     122.822 154.969 135.479  1.00 43.40           C  
ATOM   1291  N   LEU E 191     120.327 154.143 132.265  1.00 26.55           N  
ATOM   1292  CA  LEU E 191     120.529 153.446 130.999  1.00 35.35           C  
ATOM   1293  C   LEU E 191     120.658 154.429 129.842  1.00 38.17           C  
ATOM   1294  O   LEU E 191     121.555 154.292 128.996  1.00 48.76           O  
ATOM   1295  CB  LEU E 191     119.383 152.466 130.750  1.00 40.45           C  
ATOM   1296  CG  LEU E 191     119.262 151.868 129.348  1.00 32.83           C  
ATOM   1297  CD1 LEU E 191     118.910 150.402 129.444  1.00 41.82           C  
ATOM   1298  CD2 LEU E 191     118.204 152.600 128.540  1.00 35.79           C  
ATOM   1299  N   CYS E 192     119.778 155.432 129.792  1.00 33.24           N  
ATOM   1300  CA  CYS E 192     119.836 156.404 128.706  1.00 34.30           C  
ATOM   1301  C   CYS E 192     121.144 157.185 128.730  1.00 37.69           C  
ATOM   1302  O   CYS E 192     121.775 157.385 127.684  1.00 47.19           O  
ATOM   1303  CB  CYS E 192     118.642 157.352 128.787  1.00 45.28           C  
ATOM   1304  SG  CYS E 192     117.052 156.581 128.404  1.00 73.82           S  
ATOM   1305  N   VAL E 193     121.577 157.622 129.914  1.00 34.99           N  
ATOM   1306  CA  VAL E 193     122.802 158.408 129.999  1.00 38.31           C  
ATOM   1307  C   VAL E 193     124.023 157.545 129.709  1.00 37.87           C  
ATOM   1308  O   VAL E 193     124.996 158.027 129.123  1.00 47.33           O  
ATOM   1309  CB  VAL E 193     122.901 159.117 131.365  1.00 42.56           C  
ATOM   1310  CG1 VAL E 193     123.314 158.153 132.465  1.00 42.43           C  
ATOM   1311  CG2 VAL E 193     123.872 160.283 131.284  1.00 48.07           C  
ATOM   1312  N   SER E 194     123.999 156.263 130.086  1.00 33.68           N  
ATOM   1313  CA  SER E 194     125.109 155.380 129.748  1.00 29.08           C  
ATOM   1314  C   SER E 194     125.215 155.185 128.243  1.00 34.99           C  
ATOM   1315  O   SER E 194     126.314 155.240 127.678  1.00 44.03           O  
ATOM   1316  CB  SER E 194     124.943 154.037 130.453  1.00 35.26           C  
ATOM   1317  OG  SER E 194     124.799 154.213 131.850  1.00 49.66           O  
ATOM   1318  N   SER E 195     124.080 154.966 127.573  1.00 27.16           N  
ATOM   1319  CA  SER E 195     124.110 154.835 126.120  1.00 23.99           C  
ATOM   1320  C   SER E 195     124.594 156.122 125.462  1.00 35.23           C  
ATOM   1321  O   SER E 195     125.391 156.085 124.515  1.00 44.32           O  
ATOM   1322  CB  SER E 195     122.727 154.450 125.601  1.00 28.20           C  
ATOM   1323  OG  SER E 195     122.462 153.080 125.840  1.00 28.27           O  
ATOM   1324  N   LEU E 196     124.133 157.272 125.959  1.00 35.79           N  
ATOM   1325  CA  LEU E 196     124.554 158.545 125.383  1.00 32.42           C  
ATOM   1326  C   LEU E 196     126.047 158.777 125.577  1.00 34.11           C  
ATOM   1327  O   LEU E 196     126.730 159.257 124.665  1.00 47.12           O  
ATOM   1328  CB  LEU E 196     123.748 159.688 125.997  1.00 38.07           C  
ATOM   1329  CG  LEU E 196     122.662 160.297 125.109  1.00 39.58           C  
ATOM   1330  CD1 LEU E 196     121.759 159.211 124.548  1.00 41.31           C  
ATOM   1331  CD2 LEU E 196     121.853 161.323 125.884  1.00 41.36           C  
ATOM   1332  N   VAL E 197     126.574 158.447 126.758  1.00 34.08           N  
ATOM   1333  CA  VAL E 197     127.998 158.632 127.014  1.00 31.96           C  
ATOM   1334  C   VAL E 197     128.822 157.693 126.145  1.00 30.31           C  
ATOM   1335  O   VAL E 197     129.882 158.071 125.631  1.00 42.88           O  
ATOM   1336  CB  VAL E 197     128.300 158.440 128.511  1.00 40.71           C  
ATOM   1337  CG1 VAL E 197     129.793 158.296 128.741  1.00 39.13           C  
ATOM   1338  CG2 VAL E 197     127.756 159.610 129.312  1.00 42.89           C  
ATOM   1339  N   LEU E 198     128.352 156.456 125.964  1.00 24.21           N  
ATOM   1340  CA  LEU E 198     129.043 155.536 125.068  1.00 28.72           C  
ATOM   1341  C   LEU E 198     129.084 156.085 123.648  1.00 35.68           C  
ATOM   1342  O   LEU E 198     130.128 156.042 122.987  1.00 47.18           O  
ATOM   1343  CB  LEU E 198     128.360 154.169 125.100  1.00 37.19           C  
ATOM   1344  CG  LEU E 198     128.548 153.239 123.902  1.00 38.12           C  
ATOM   1345  CD1 LEU E 198     129.998 152.826 123.760  1.00 37.73           C  
ATOM   1346  CD2 LEU E 198     127.656 152.019 124.039  1.00 39.51           C  
ATOM   1347  N   LEU E 199     127.959 156.620 123.169  1.00 33.47           N  
ATOM   1348  CA  LEU E 199     127.932 157.192 121.826  1.00 28.21           C  
ATOM   1349  C   LEU E 199     128.866 158.390 121.711  1.00 32.28           C  
ATOM   1350  O   LEU E 199     129.565 158.545 120.704  1.00 39.94           O  
ATOM   1351  CB  LEU E 199     126.506 157.587 121.454  1.00 35.72           C  
ATOM   1352  CG  LEU E 199     125.832 156.619 120.487  1.00 41.56           C  
ATOM   1353  CD1 LEU E 199     126.602 156.561 119.182  1.00 44.10           C  
ATOM   1354  CD2 LEU E 199     125.762 155.247 121.118  1.00 39.63           C  
ATOM   1355  N   VAL E 200     128.888 159.252 122.729  1.00 41.53           N  
ATOM   1356  CA  VAL E 200     129.756 160.426 122.686  1.00 41.93           C  
ATOM   1357  C   VAL E 200     131.221 160.011 122.662  1.00 40.28           C  
ATOM   1358  O   VAL E 200     132.025 160.567 121.904  1.00 47.21           O  
ATOM   1359  CB  VAL E 200     129.451 161.364 123.869  1.00 45.32           C  
ATOM   1360  CG1 VAL E 200     130.508 162.449 123.970  1.00 47.50           C  
ATOM   1361  CG2 VAL E 200     128.074 161.985 123.707  1.00 40.54           C  
ATOM   1362  N   ARG E 201     131.595 159.032 123.488  1.00 40.32           N  
ATOM   1363  CA  ARG E 201     132.981 158.575 123.504  1.00 41.44           C  
ATOM   1364  C   ARG E 201     133.366 157.921 122.183  1.00 46.16           C  
ATOM   1365  O   ARG E 201     134.481 158.121 121.686  1.00 52.90           O  
ATOM   1366  CB  ARG E 201     133.207 157.609 124.667  1.00 41.66           C  
ATOM   1367  CG  ARG E 201     134.650 157.149 124.816  1.00 46.37           C  
ATOM   1368  CD  ARG E 201     135.499 158.186 125.536  1.00 49.41           C  
ATOM   1369  NE  ARG E 201     136.451 158.832 124.641  1.00 53.26           N  
ATOM   1370  CZ  ARG E 201     137.182 159.891 124.962  1.00 54.36           C  
ATOM   1371  NH1 ARG E 201     137.100 160.452 126.157  1.00 52.07           N1+
ATOM   1372  NH2 ARG E 201     138.016 160.401 124.060  1.00 44.17           N  
ATOM   1373  N   ILE E 202     132.463 157.129 121.601  1.00 44.00           N  
ATOM   1374  CA  ILE E 202     132.759 156.488 120.323  1.00 40.53           C  
ATOM   1375  C   ILE E 202     132.880 157.526 119.214  1.00 49.50           C  
ATOM   1376  O   ILE E 202     133.768 157.439 118.358  1.00 58.93           O  
ATOM   1377  CB  ILE E 202     131.692 155.427 119.997  1.00 40.62           C  
ATOM   1378  CG1 ILE E 202     131.874 154.203 120.896  1.00 45.14           C  
ATOM   1379  CG2 ILE E 202     131.750 155.035 118.530  1.00 45.72           C  
ATOM   1380  CD1 ILE E 202     132.910 153.223 120.396  1.00 43.17           C  
ATOM   1381  N   LEU E 203     132.006 158.529 119.217  1.00 46.71           N  
ATOM   1382  CA  LEU E 203     131.998 159.536 118.164  1.00 43.53           C  
ATOM   1383  C   LEU E 203     133.025 160.640 118.382  1.00 46.21           C  
ATOM   1384  O   LEU E 203     133.126 161.540 117.542  1.00 44.66           O  
ATOM   1385  CB  LEU E 203     130.602 160.151 118.036  1.00 41.85           C  
ATOM   1386  CG  LEU E 203     129.504 159.219 117.522  1.00 41.21           C  
ATOM   1387  CD1 LEU E 203     128.371 160.018 116.899  1.00 45.45           C  
ATOM   1388  CD2 LEU E 203     130.066 158.214 116.528  1.00 45.15           C  
ATOM   1389  N   CYS E 204     133.778 160.602 119.477  1.00 61.49           N  
ATOM   1390  CA  CYS E 204     134.836 161.570 119.746  1.00 60.71           C  
ATOM   1391  C   CYS E 204     136.207 160.901 119.745  1.00 64.90           C  
ATOM   1392  O   CYS E 204     137.070 161.208 120.570  1.00 66.17           O  
ATOM   1393  CB  CYS E 204     134.591 162.288 121.069  1.00 60.15           C  
ATOM   1394  SG  CYS E 204     133.246 163.491 121.019  1.00 71.15           S  
ATOM   1395  N   GLY E 205     136.417 159.975 118.813  1.00 72.39           N  
ATOM   1396  CA  GLY E 205     137.686 159.285 118.694  1.00 75.88           C  
ATOM   1397  C   GLY E 205     137.995 158.878 117.268  1.00 78.79           C  
ATOM   1398  O   GLY E 205     137.297 159.290 116.336  1.00 78.78           O  
ATOM   1399  N   SER E 206     139.041 158.077 117.084  1.00 84.60           N  
ATOM   1400  CA  SER E 206     139.399 157.604 115.756  1.00 81.94           C  
ATOM   1401  C   SER E 206     138.301 156.710 115.193  1.00 83.79           C  
ATOM   1402  O   SER E 206     137.740 155.861 115.889  1.00 81.36           O  
ATOM   1403  CB  SER E 206     140.720 156.840 115.796  1.00 80.37           C  
ATOM   1404  OG  SER E 206     140.505 155.483 116.144  1.00 84.02           O  
ATOM   1405  N   ARG E 207     137.999 156.910 113.914  1.00 88.95           N  
ATOM   1406  CA  ARG E 207     136.916 156.183 113.257  1.00 87.18           C  
ATOM   1407  C   ARG E 207     137.469 154.922 112.607  1.00 88.46           C  
ATOM   1408  O   ARG E 207     137.830 154.922 111.429  1.00 90.18           O  
ATOM   1409  CB  ARG E 207     136.231 157.074 112.227  1.00 85.40           C  
ATOM   1410  N   LYS E 208     137.539 153.836 113.375  1.00 95.20           N  
ATOM   1411  CA  LYS E 208     137.819 152.526 112.803  1.00 98.42           C  
ATOM   1412  C   LYS E 208     136.730 152.080 111.840  1.00100.04           C  
ATOM   1413  O   LYS E 208     136.977 151.210 110.997  1.00101.91           O  
ATOM   1414  CB  LYS E 208     137.986 151.486 113.914  1.00 95.94           C  
ATOM   1415  N   MET E 209     135.535 152.651 111.966  1.00 94.96           N  
ATOM   1416  CA  MET E 209     134.377 152.489 111.098  1.00 94.41           C  
ATOM   1417  C   MET E 209     133.817 151.073 110.974  1.00 95.09           C  
ATOM   1418  O   MET E 209     133.517 150.640 109.855  1.00 95.31           O  
ATOM   1419  CB  MET E 209     134.716 153.006 109.697  1.00 94.40           C  
ATOM   1420  N   PRO E 210     133.654 150.308 112.071  1.00 92.22           N  
ATOM   1421  CA  PRO E 210     132.489 149.415 112.123  1.00 90.99           C  
ATOM   1422  C   PRO E 210     131.310 150.179 112.701  1.00 90.72           C  
ATOM   1423  O   PRO E 210     130.573 149.655 113.542  1.00 87.21           O  
ATOM   1424  CB  PRO E 210     132.921 148.268 113.046  1.00 89.76           C  
ATOM   1425  CG  PRO E 210     134.228 148.623 113.593  1.00 92.04           C  
ATOM   1426  CD  PRO E 210     134.718 149.896 113.005  1.00 90.24           C  
ATOM   1427  N   LEU E 211     131.120 151.421 112.254  1.00 81.96           N  
ATOM   1428  CA  LEU E 211     130.146 152.293 112.895  1.00 80.59           C  
ATOM   1429  C   LEU E 211     128.797 152.183 112.205  1.00 79.15           C  
ATOM   1430  O   LEU E 211     128.149 153.194 111.917  1.00 81.97           O  
ATOM   1431  CB  LEU E 211     130.641 153.741 112.885  1.00 80.68           C  
ATOM   1432  CG  LEU E 211     131.845 154.069 113.774  1.00 79.10           C  
ATOM   1433  CD1 LEU E 211     131.781 155.511 114.251  1.00 78.86           C  
ATOM   1434  CD2 LEU E 211     131.940 153.119 114.959  1.00 76.53           C  
ATOM   1435  N   THR E 212     128.375 150.965 111.945  1.00 71.26           N  
ATOM   1436  CA  THR E 212     127.012 150.618 111.571  1.00 74.22           C  
ATOM   1437  C   THR E 212     126.470 149.504 112.447  1.00 73.85           C  
ATOM   1438  O   THR E 212     125.289 149.525 112.800  1.00 77.59           O  
ATOM   1439  CB  THR E 212     126.923 150.198 110.092  1.00 77.06           C  
ATOM   1440  OG1 THR E 212     127.371 148.844 109.950  1.00 77.42           O  
ATOM   1441  CG2 THR E 212     127.773 151.107 109.213  1.00 75.48           C  
ATOM   1442  N   ARG E 213     127.311 148.532 112.807  1.00 67.15           N  
ATOM   1443  CA  ARG E 213     126.924 147.539 113.800  1.00 64.22           C  
ATOM   1444  C   ARG E 213     126.725 148.185 115.163  1.00 68.43           C  
ATOM   1445  O   ARG E 213     125.782 147.847 115.885  1.00 72.33           O  
ATOM   1446  CB  ARG E 213     127.981 146.435 113.871  1.00 66.36           C  
ATOM   1447  CG  ARG E 213     127.649 145.272 114.799  1.00 72.00           C  
ATOM   1448  CD  ARG E 213     128.270 145.459 116.181  1.00 76.14           C  
ATOM   1449  NE  ARG E 213     129.728 145.447 116.140  1.00 76.95           N  
ATOM   1450  CZ  ARG E 213     130.508 145.618 117.198  1.00 71.22           C  
ATOM   1451  NH1 ARG E 213     130.003 145.808 118.406  1.00 67.88           N1+
ATOM   1452  NH2 ARG E 213     131.829 145.600 117.041  1.00 66.22           N  
ATOM   1453  N   LEU E 214     127.610 149.112 115.536  1.00 62.45           N  
ATOM   1454  CA  LEU E 214     127.474 149.790 116.822  1.00 60.10           C  
ATOM   1455  C   LEU E 214     126.221 150.655 116.863  1.00 61.08           C  
ATOM   1456  O   LEU E 214     125.530 150.706 117.886  1.00 60.64           O  
ATOM   1457  CB  LEU E 214     128.718 150.631 117.108  1.00 58.98           C  
ATOM   1458  CG  LEU E 214     128.640 151.576 118.308  1.00 52.50           C  
ATOM   1459  CD1 LEU E 214     129.882 151.437 119.165  1.00 56.48           C  
ATOM   1460  CD2 LEU E 214     128.466 153.014 117.856  1.00 56.59           C  
ATOM   1461  N   TYR E 215     125.921 151.353 115.766  1.00 65.68           N  
ATOM   1462  CA  TYR E 215     124.722 152.184 115.725  1.00 62.64           C  
ATOM   1463  C   TYR E 215     123.467 151.340 115.894  1.00 59.39           C  
ATOM   1464  O   TYR E 215     122.591 151.661 116.708  1.00 62.22           O  
ATOM   1465  CB  TYR E 215     124.668 152.963 114.410  1.00 63.92           C  
ATOM   1466  CG  TYR E 215     125.487 154.237 114.401  1.00 68.00           C  
ATOM   1467  CD1 TYR E 215     126.456 154.474 115.366  1.00 68.55           C  
ATOM   1468  CD2 TYR E 215     125.286 155.203 113.424  1.00 64.76           C  
ATOM   1469  CE1 TYR E 215     127.203 155.635 115.357  1.00 65.08           C  
ATOM   1470  CE2 TYR E 215     126.027 156.366 113.408  1.00 66.68           C  
ATOM   1471  CZ  TYR E 215     126.984 156.577 114.376  1.00 67.78           C  
ATOM   1472  OH  TYR E 215     127.723 157.737 114.362  1.00 69.29           O  
ATOM   1473  N   VAL E 216     123.372 150.239 115.146  1.00 59.29           N  
ATOM   1474  CA  VAL E 216     122.134 149.468 115.140  1.00 61.02           C  
ATOM   1475  C   VAL E 216     121.919 148.781 116.483  1.00 61.64           C  
ATOM   1476  O   VAL E 216     120.793 148.730 116.982  1.00 67.12           O  
ATOM   1477  CB  VAL E 216     122.111 148.464 113.970  1.00 64.93           C  
ATOM   1478  CG1 VAL E 216     123.265 147.483 114.052  1.00 64.17           C  
ATOM   1479  CG2 VAL E 216     120.781 147.726 113.928  1.00 66.33           C  
ATOM   1480  N   THR E 217     122.983 148.263 117.105  1.00 59.02           N  
ATOM   1481  CA  THR E 217     122.793 147.536 118.358  1.00 61.49           C  
ATOM   1482  C   THR E 217     122.366 148.476 119.480  1.00 65.17           C  
ATOM   1483  O   THR E 217     121.439 148.168 120.238  1.00 69.29           O  
ATOM   1484  CB  THR E 217     124.058 146.761 118.745  1.00 64.53           C  
ATOM   1485  OG1 THR E 217     123.849 146.114 120.006  1.00 70.59           O  
ATOM   1486  CG2 THR E 217     125.264 147.674 118.870  1.00 61.43           C  
ATOM   1487  N   ILE E 218     123.016 149.637 119.593  1.00 55.01           N  
ATOM   1488  CA  ILE E 218     122.645 150.590 120.634  1.00 55.81           C  
ATOM   1489  C   ILE E 218     121.243 151.126 120.386  1.00 58.48           C  
ATOM   1490  O   ILE E 218     120.429 151.231 121.314  1.00 60.91           O  
ATOM   1491  CB  ILE E 218     123.681 151.725 120.722  1.00 51.76           C  
ATOM   1492  CG1 ILE E 218     124.691 151.443 121.834  1.00 55.41           C  
ATOM   1493  CG2 ILE E 218     122.999 153.054 120.986  1.00 50.20           C  
ATOM   1494  CD1 ILE E 218     125.483 150.172 121.641  1.00 63.31           C  
ATOM   1495  N   LEU E 219     120.933 151.463 119.131  1.00 66.49           N  
ATOM   1496  CA  LEU E 219     119.602 151.968 118.821  1.00 63.55           C  
ATOM   1497  C   LEU E 219     118.540 150.923 119.124  1.00 64.17           C  
ATOM   1498  O   LEU E 219     117.489 151.245 119.686  1.00 69.70           O  
ATOM   1499  CB  LEU E 219     119.529 152.406 117.360  1.00 66.43           C  
ATOM   1500  CG  LEU E 219     118.684 153.648 117.071  1.00 62.48           C  
ATOM   1501  CD1 LEU E 219     118.708 154.608 118.250  1.00 63.45           C  
ATOM   1502  CD2 LEU E 219     119.165 154.338 115.805  1.00 62.67           C  
ATOM   1503  N   LEU E 220     118.802 149.662 118.776  1.00 60.01           N  
ATOM   1504  CA  LEU E 220     117.837 148.601 119.029  1.00 57.51           C  
ATOM   1505  C   LEU E 220     117.654 148.359 120.520  1.00 58.33           C  
ATOM   1506  O   LEU E 220     116.527 148.153 120.979  1.00 65.98           O  
ATOM   1507  CB  LEU E 220     118.275 147.318 118.325  1.00 59.09           C  
ATOM   1508  CG  LEU E 220     117.167 146.309 118.019  1.00 61.86           C  
ATOM   1509  CD1 LEU E 220     116.216 146.860 116.969  1.00 68.55           C  
ATOM   1510  CD2 LEU E 220     117.761 144.988 117.561  1.00 59.58           C  
ATOM   1511  N   THR E 221     118.741 148.377 121.294  1.00 58.56           N  
ATOM   1512  CA  THR E 221     118.614 148.175 122.735  1.00 61.55           C  
ATOM   1513  C   THR E 221     117.810 149.300 123.374  1.00 63.31           C  
ATOM   1514  O   THR E 221     116.889 149.054 124.164  1.00 68.82           O  
ATOM   1515  CB  THR E 221     119.994 148.069 123.382  1.00 63.47           C  
ATOM   1516  OG1 THR E 221     120.812 149.162 122.950  1.00 66.99           O  
ATOM   1517  CG2 THR E 221     120.662 146.757 123.001  1.00 65.70           C  
ATOM   1518  N   VAL E 222     118.128 150.548 123.024  1.00 60.85           N  
ATOM   1519  CA  VAL E 222     117.393 151.673 123.591  1.00 60.17           C  
ATOM   1520  C   VAL E 222     115.932 151.630 123.162  1.00 63.93           C  
ATOM   1521  O   VAL E 222     115.029 151.886 123.966  1.00 67.97           O  
ATOM   1522  CB  VAL E 222     118.066 153.001 123.205  1.00 65.48           C  
ATOM   1523  CG1 VAL E 222     117.246 154.176 123.707  1.00 71.34           C  
ATOM   1524  CG2 VAL E 222     119.474 153.061 123.773  1.00 62.69           C  
ATOM   1525  N   LEU E 223     115.671 151.301 121.895  1.00 58.87           N  
ATOM   1526  CA  LEU E 223     114.297 151.258 121.409  1.00 59.19           C  
ATOM   1527  C   LEU E 223     113.502 150.146 122.080  1.00 63.53           C  
ATOM   1528  O   LEU E 223     112.339 150.344 122.443  1.00 72.23           O  
ATOM   1529  CB  LEU E 223     114.288 151.085 119.893  1.00 65.19           C  
ATOM   1530  CG  LEU E 223     113.120 151.739 119.156  1.00 68.17           C  
ATOM   1531  CD1 LEU E 223     113.327 153.241 119.066  1.00 66.38           C  
ATOM   1532  CD2 LEU E 223     112.960 151.134 117.771  1.00 68.61           C  
ATOM   1533  N   VAL E 224     114.109 148.971 122.261  1.00 48.31           N  
ATOM   1534  CA  VAL E 224     113.392 147.867 122.878  1.00 50.33           C  
ATOM   1535  C   VAL E 224     113.265 148.067 124.380  1.00 56.40           C  
ATOM   1536  O   VAL E 224     112.452 147.395 125.023  1.00 64.73           O  
ATOM   1537  CB  VAL E 224     114.080 146.526 122.557  1.00 54.34           C  
ATOM   1538  CG1 VAL E 224     115.348 146.360 123.379  1.00 54.81           C  
ATOM   1539  CG2 VAL E 224     113.123 145.359 122.761  1.00 57.39           C  
ATOM   1540  N   PHE E 225     114.056 148.967 124.966  1.00 54.56           N  
ATOM   1541  CA  PHE E 225     113.856 149.304 126.370  1.00 49.91           C  
ATOM   1542  C   PHE E 225     112.788 150.373 126.567  1.00 50.24           C  
ATOM   1543  O   PHE E 225     112.001 150.283 127.514  1.00 61.99           O  
ATOM   1544  CB  PHE E 225     115.175 149.758 127.000  1.00 56.50           C  
ATOM   1545  CG  PHE E 225     115.162 149.776 128.507  1.00 58.65           C  
ATOM   1546  CD1 PHE E 225     114.447 150.738 129.205  1.00 52.93           C  
ATOM   1547  CD2 PHE E 225     115.855 148.820 129.226  1.00 61.75           C  
ATOM   1548  CE1 PHE E 225     114.433 150.751 130.583  1.00 50.78           C  
ATOM   1549  CE2 PHE E 225     115.847 148.830 130.607  1.00 61.86           C  
ATOM   1550  CZ  PHE E 225     115.134 149.796 131.286  1.00 56.78           C  
ATOM   1551  N   LEU E 226     112.737 151.389 125.706  1.00 45.09           N  
ATOM   1552  CA  LEU E 226     111.753 152.449 125.911  1.00 54.71           C  
ATOM   1553  C   LEU E 226     110.398 152.091 125.310  1.00 61.29           C  
ATOM   1554  O   LEU E 226     109.373 152.163 125.995  1.00 66.10           O  
ATOM   1555  CB  LEU E 226     112.257 153.779 125.345  1.00 59.55           C  
ATOM   1556  CG  LEU E 226     113.731 154.146 125.507  1.00 61.95           C  
ATOM   1557  CD1 LEU E 226     113.999 155.530 124.942  1.00 61.83           C  
ATOM   1558  CD2 LEU E 226     114.146 154.078 126.968  1.00 62.12           C  
ATOM   1559  N   LEU E 227     110.368 151.715 124.031  1.00 58.19           N  
ATOM   1560  CA  LEU E 227     109.101 151.395 123.385  1.00 56.93           C  
ATOM   1561  C   LEU E 227     108.493 150.099 123.904  1.00 61.09           C  
ATOM   1562  O   LEU E 227     107.278 149.911 123.788  1.00 70.15           O  
ATOM   1563  CB  LEU E 227     109.288 151.308 121.871  1.00 60.26           C  
ATOM   1564  CG  LEU E 227     109.020 152.586 121.073  1.00 67.00           C  
ATOM   1565  CD1 LEU E 227     110.056 153.654 121.382  1.00 64.36           C  
ATOM   1566  CD2 LEU E 227     108.988 152.284 119.584  1.00 67.65           C  
ATOM   1567  N   CYS E 228     109.302 149.206 124.467  1.00 57.23           N  
ATOM   1568  CA  CYS E 228     108.821 147.950 125.018  1.00 56.02           C  
ATOM   1569  C   CYS E 228     109.410 147.748 126.406  1.00 59.91           C  
ATOM   1570  O   CYS E 228     110.522 148.192 126.694  1.00 65.67           O  
ATOM   1571  CB  CYS E 228     109.187 146.770 124.113  1.00 55.03           C  
ATOM   1572  SG  CYS E 228     108.230 146.669 122.586  1.00 71.04           S  
ATOM   1573  N   GLY E 229     108.654 147.080 127.270  1.00 65.69           N  
ATOM   1574  CA  GLY E 229     109.118 146.852 128.624  1.00 64.63           C  
ATOM   1575  C   GLY E 229     108.832 148.015 129.550  1.00 59.07           C  
ATOM   1576  O   GLY E 229     108.049 147.882 130.495  1.00 69.48           O  
ATOM   1577  N   LEU E 230     109.458 149.161 129.289  1.00 37.89           N  
ATOM   1578  CA  LEU E 230     109.163 150.359 130.071  1.00 41.18           C  
ATOM   1579  C   LEU E 230     107.681 150.716 130.100  1.00 49.02           C  
ATOM   1580  O   LEU E 230     107.224 151.229 131.137  1.00 61.81           O  
ATOM   1581  CB  LEU E 230     109.988 151.543 129.555  1.00 46.75           C  
ATOM   1582  CG  LEU E 230     110.242 152.650 130.579  1.00 53.32           C  
ATOM   1583  CD1 LEU E 230     111.238 152.191 131.629  1.00 54.61           C  
ATOM   1584  CD2 LEU E 230     110.725 153.916 129.895  1.00 55.48           C  
ATOM   1585  N   PRO E 231     106.898 150.530 129.027  1.00 39.93           N  
ATOM   1586  CA  PRO E 231     105.452 150.763 129.152  1.00 44.35           C  
ATOM   1587  C   PRO E 231     104.804 149.981 130.281  1.00 55.65           C  
ATOM   1588  O   PRO E 231     103.918 150.518 130.948  1.00 59.61           O  
ATOM   1589  CB  PRO E 231     104.919 150.336 127.781  1.00 52.94           C  
ATOM   1590  CG  PRO E 231     106.022 150.651 126.859  1.00 54.63           C  
ATOM   1591  CD  PRO E 231     107.290 150.362 127.615  1.00 50.01           C  
ATOM   1592  N   PHE E 232     105.228 148.740 130.531  1.00 62.65           N  
ATOM   1593  CA  PHE E 232     104.668 147.981 131.648  1.00 56.63           C  
ATOM   1594  C   PHE E 232     104.973 148.651 132.983  1.00 52.00           C  
ATOM   1595  O   PHE E 232     104.092 148.774 133.845  1.00 58.21           O  
ATOM   1596  CB  PHE E 232     105.211 146.552 131.630  1.00 56.61           C  
ATOM   1597  CG  PHE E 232     104.296 145.543 132.264  1.00 55.39           C  
ATOM   1598  CD1 PHE E 232     103.012 145.351 131.783  1.00 57.50           C  
ATOM   1599  CD2 PHE E 232     104.724 144.779 133.334  1.00 53.54           C  
ATOM   1600  CE1 PHE E 232     102.172 144.421 132.362  1.00 53.77           C  
ATOM   1601  CE2 PHE E 232     103.889 143.847 133.917  1.00 53.53           C  
ATOM   1602  CZ  PHE E 232     102.612 143.669 133.430  1.00 52.83           C  
ATOM   1603  N   GLY E 233     106.217 149.094 133.169  1.00 54.40           N  
ATOM   1604  CA  GLY E 233     106.579 149.740 134.419  1.00 58.71           C  
ATOM   1605  C   GLY E 233     105.832 151.040 134.637  1.00 53.91           C  
ATOM   1606  O   GLY E 233     105.299 151.290 135.721  1.00 54.67           O  
ATOM   1607  N   ILE E 234     105.771 151.883 133.603  1.00 52.12           N  
ATOM   1608  CA  ILE E 234     105.051 153.142 133.757  1.00 60.90           C  
ATOM   1609  C   ILE E 234     103.559 152.888 133.924  1.00 67.42           C  
ATOM   1610  O   ILE E 234     102.870 153.648 134.615  1.00 76.52           O  
ATOM   1611  CB  ILE E 234     105.338 154.095 132.581  1.00 61.34           C  
ATOM   1612  CG1 ILE E 234     104.727 153.566 131.284  1.00 62.81           C  
ATOM   1613  CG2 ILE E 234     106.835 154.301 132.423  1.00 61.08           C  
ATOM   1614  CD1 ILE E 234     105.077 154.385 130.063  1.00 63.83           C  
ATOM   1615  N   LEU E 235     103.038 151.818 133.315  1.00 65.88           N  
ATOM   1616  CA  LEU E 235     101.633 151.468 133.483  1.00 65.77           C  
ATOM   1617  C   LEU E 235     101.336 151.115 134.929  1.00 58.08           C  
ATOM   1618  O   LEU E 235     100.375 151.620 135.517  1.00 60.55           O  
ATOM   1619  CB  LEU E 235     101.271 150.307 132.560  1.00 67.81           C  
ATOM   1620  CG  LEU E 235     100.098 149.441 133.017  1.00 65.01           C  
ATOM   1621  CD1 LEU E 235      98.772 150.104 132.678  1.00 65.56           C  
ATOM   1622  CD2 LEU E 235     100.193 148.064 132.397  1.00 62.72           C  
ATOM   1623  N   GLY E 236     102.160 150.253 135.522  1.00 59.76           N  
ATOM   1624  CA  GLY E 236     102.001 149.962 136.937  1.00 66.24           C  
ATOM   1625  C   GLY E 236     102.138 151.205 137.794  1.00 69.81           C  
ATOM   1626  O   GLY E 236     101.371 151.411 138.743  1.00 67.16           O  
ATOM   1627  N   ALA E 237     103.097 152.068 137.449  1.00 76.14           N  
ATOM   1628  CA  ALA E 237     103.338 153.274 138.232  1.00 73.74           C  
ATOM   1629  C   ALA E 237     102.113 154.180 138.252  1.00 71.04           C  
ATOM   1630  O   ALA E 237     101.648 154.582 139.323  1.00 76.62           O  
ATOM   1631  CB  ALA E 237     104.553 154.021 137.682  1.00 75.38           C  
ATOM   1632  N   LEU E 238     101.563 154.509 137.083  1.00 67.82           N  
ATOM   1633  CA  LEU E 238     100.443 155.441 137.113  1.00 71.24           C  
ATOM   1634  C   LEU E 238      99.112 154.740 137.351  1.00 79.27           C  
ATOM   1635  O   LEU E 238      98.092 155.422 137.495  1.00 80.86           O  
ATOM   1636  CB  LEU E 238     100.354 156.281 135.830  1.00 72.37           C  
ATOM   1637  CG  LEU E 238      99.662 155.852 134.528  1.00 73.66           C  
ATOM   1638  CD1 LEU E 238      99.905 156.893 133.436  1.00 76.42           C  
ATOM   1639  CD2 LEU E 238     100.014 154.473 134.041  1.00 73.11           C  
ATOM   1640  N   ILE E 239      99.089 153.405 137.392  1.00 80.80           N  
ATOM   1641  CA  ILE E 239      97.877 152.697 137.781  1.00 76.56           C  
ATOM   1642  C   ILE E 239      97.798 152.491 139.286  1.00 75.95           C  
ATOM   1643  O   ILE E 239      96.697 152.282 139.815  1.00 80.94           O  
ATOM   1644  CB  ILE E 239      97.766 151.343 137.056  1.00 77.96           C  
ATOM   1645  CG1 ILE E 239      96.300 150.942 136.894  1.00 78.03           C  
ATOM   1646  CG2 ILE E 239      98.512 150.258 137.812  1.00 79.67           C  
ATOM   1647  CD1 ILE E 239      96.109 149.594 136.233  1.00 77.23           C  
ATOM   1648  N   TYR E 240      98.927 152.539 139.996  1.00 82.07           N  
ATOM   1649  CA  TYR E 240      98.863 152.535 141.450  1.00 88.10           C  
ATOM   1650  C   TYR E 240      99.017 153.928 142.050  1.00 89.72           C  
ATOM   1651  O   TYR E 240      98.639 154.128 143.209  1.00 88.36           O  
ATOM   1652  CB  TYR E 240      99.914 151.584 142.043  1.00 89.25           C  
ATOM   1653  CG  TYR E 240     101.211 152.231 142.463  1.00 88.47           C  
ATOM   1654  CD1 TYR E 240     102.196 152.535 141.536  1.00 88.99           C  
ATOM   1655  CD2 TYR E 240     101.450 152.532 143.796  1.00 84.49           C  
ATOM   1656  CE1 TYR E 240     103.382 153.124 141.928  1.00 91.62           C  
ATOM   1657  CE2 TYR E 240     102.625 153.122 144.192  1.00 85.56           C  
ATOM   1658  CZ  TYR E 240     103.589 153.412 143.260  1.00 90.14           C  
ATOM   1659  OH  TYR E 240     104.762 154.001 143.671  1.00 87.69           O  
ATOM   1660  N   ARG E 241      99.556 154.892 141.297  1.00 84.52           N  
ATOM   1661  CA  ARG E 241      99.498 156.285 141.729  1.00 81.71           C  
ATOM   1662  C   ARG E 241      98.061 156.785 141.737  1.00 82.67           C  
ATOM   1663  O   ARG E 241      97.588 157.340 142.735  1.00 87.97           O  
ATOM   1664  CB  ARG E 241     100.357 157.161 140.816  1.00 83.80           C  
ATOM   1665  CG  ARG E 241     101.829 157.220 141.177  1.00 83.80           C  
ATOM   1666  CD  ARG E 241     102.071 158.195 142.315  1.00 84.58           C  
ATOM   1667  NE  ARG E 241     101.875 157.558 143.610  1.00 86.04           N  
ATOM   1668  CZ  ARG E 241     102.726 156.701 144.157  1.00 84.49           C  
ATOM   1669  NH1 ARG E 241     103.874 156.401 143.574  1.00 82.11           N1+
ATOM   1670  NH2 ARG E 241     102.417 156.133 145.317  1.00 83.47           N  
ATOM   1671  N   MET E 242      97.352 156.593 140.629  1.00 84.81           N  
ATOM   1672  CA  MET E 242      95.924 156.862 140.536  1.00 87.45           C  
ATOM   1673  C   MET E 242      95.202 155.524 140.572  1.00 89.43           C  
ATOM   1674  O   MET E 242      95.326 154.725 139.637  1.00 91.33           O  
ATOM   1675  CB  MET E 242      95.586 157.629 139.259  1.00 85.98           C  
ATOM   1676  N   HIS E 243      94.446 155.284 141.640  1.00 99.22           N  
ATOM   1677  CA  HIS E 243      93.852 153.971 141.844  1.00100.40           C  
ATOM   1678  C   HIS E 243      92.716 153.736 140.858  1.00101.65           C  
ATOM   1679  O   HIS E 243      91.550 154.014 141.154  1.00102.18           O  
ATOM   1680  CB  HIS E 243      93.362 153.821 143.285  1.00103.05           C  
ATOM   1681  CG  HIS E 243      94.421 154.081 144.311  1.00105.68           C  
ATOM   1682  ND1 HIS E 243      95.515 153.258 144.475  1.00102.74           N  
ATOM   1683  CD2 HIS E 243      94.553 155.069 145.227  1.00102.63           C  
ATOM   1684  CE1 HIS E 243      96.275 153.729 145.447  1.00100.10           C  
ATOM   1685  NE2 HIS E 243      95.714 154.827 145.920  1.00101.47           N  
ATOM   1686  N   LEU E 244      93.061 153.222 139.681  1.00109.38           N  
ATOM   1687  CA  LEU E 244      92.100 152.915 138.633  1.00109.84           C  
ATOM   1688  C   LEU E 244      91.745 151.436 138.695  1.00110.62           C  
ATOM   1689  O   LEU E 244      92.635 150.580 138.749  1.00108.53           O  
ATOM   1690  CB  LEU E 244      92.669 153.267 137.258  1.00108.79           C  
ATOM   1691  CG  LEU E 244      91.690 153.755 136.189  1.00110.89           C  
ATOM   1692  CD1 LEU E 244      90.955 155.000 136.659  1.00111.63           C  
ATOM   1693  CD2 LEU E 244      92.434 154.028 134.893  1.00108.55           C  
ATOM   1694  N   ASN E 245      90.448 151.141 138.683  1.00111.27           N  
ATOM   1695  CA  ASN E 245      89.956 149.770 138.727  1.00110.47           C  
ATOM   1696  C   ASN E 245      89.960 149.105 137.359  1.00112.28           C  
ATOM   1697  O   ASN E 245      89.218 148.137 137.156  1.00115.48           O  
ATOM   1698  CB  ASN E 245      88.544 149.739 139.317  1.00110.05           C  
ATOM   1699  CG  ASN E 245      88.543 149.520 140.816  1.00108.78           C  
ATOM   1700  OD1 ASN E 245      89.333 148.735 141.340  1.00107.78           O  
ATOM   1701  ND2 ASN E 245      87.654 150.215 141.515  1.00110.84           N  
ATOM   1702  N   LEU E 246      90.749 149.637 136.422  1.00106.80           N  
ATOM   1703  CA  LEU E 246      90.887 149.166 135.046  1.00106.19           C  
ATOM   1704  C   LEU E 246      89.640 149.492 134.231  1.00106.39           C  
ATOM   1705  O   LEU E 246      89.654 149.364 133.002  1.00101.51           O  
ATOM   1706  CB  LEU E 246      91.188 147.660 134.993  1.00106.66           C  
ATOM   1707  CG  LEU E 246      92.367 147.092 135.796  1.00105.91           C  
ATOM   1708  CD1 LEU E 246      91.909 146.388 137.067  1.00101.94           C  
ATOM   1709  CD2 LEU E 246      93.191 146.146 134.937  1.00106.26           C  
ATOM   1710  N   GLU E 247      88.580 149.943 134.913  1.00114.94           N  
ATOM   1711  CA  GLU E 247      87.325 150.481 134.348  1.00113.80           C  
ATOM   1712  C   GLU E 247      86.952 149.692 133.091  1.00114.24           C  
ATOM   1713  O   GLU E 247      87.037 148.456 133.103  1.00113.22           O  
ATOM   1714  CB  GLU E 247      87.466 151.993 134.169  1.00113.88           C  
ATOM   1715  CG  GLU E 247      88.510 152.452 133.157  1.00111.84           C  
ATOM   1716  CD  GLU E 247      89.075 153.818 133.482  1.00111.30           C  
ATOM   1717  OE1 GLU E 247      88.560 154.469 134.413  1.00109.94           O  
ATOM   1718  OE2 GLU E 247      90.025 154.247 132.796  1.00110.24           O1-
ATOM   1719  N   VAL E 248      86.524 150.346 132.013  1.00121.02           N  
ATOM   1720  CA  VAL E 248      86.335 149.709 130.716  1.00121.63           C  
ATOM   1721  C   VAL E 248      87.173 150.488 129.712  1.00119.91           C  
ATOM   1722  O   VAL E 248      87.299 150.101 128.544  1.00117.27           O  
ATOM   1723  CB  VAL E 248      84.850 149.671 130.310  1.00122.79           C  
ATOM   1724  CG1 VAL E 248      84.388 151.046 129.848  1.00120.39           C  
ATOM   1725  CG2 VAL E 248      84.610 148.622 129.231  1.00119.50           C  
ATOM   1726  N   LEU E 249      87.745 151.602 130.168  1.00121.96           N  
ATOM   1727  CA  LEU E 249      88.617 152.407 129.322  1.00124.25           C  
ATOM   1728  C   LEU E 249      90.061 151.926 129.369  1.00123.22           C  
ATOM   1729  O   LEU E 249      90.817 152.160 128.421  1.00121.07           O  
ATOM   1730  CB  LEU E 249      88.543 153.877 129.739  1.00121.87           C  
ATOM   1731  CG  LEU E 249      87.154 154.517 129.806  1.00119.93           C  
ATOM   1732  CD1 LEU E 249      87.265 156.019 130.010  1.00119.59           C  
ATOM   1733  CD2 LEU E 249      86.349 154.204 128.555  1.00120.00           C  
ATOM   1734  N   TYR E 250      90.462 151.260 130.453  1.00118.24           N  
ATOM   1735  CA  TYR E 250      91.837 150.812 130.627  1.00117.31           C  
ATOM   1736  C   TYR E 250      91.963 149.292 130.575  1.00117.62           C  
ATOM   1737  O   TYR E 250      92.912 148.723 131.120  1.00116.72           O  
ATOM   1738  CB  TYR E 250      92.417 151.351 131.933  1.00116.28           C  
ATOM   1739  CG  TYR E 250      93.411 152.470 131.718  1.00119.86           C  
ATOM   1740  CD1 TYR E 250      93.040 153.632 131.053  1.00119.12           C  
ATOM   1741  CD2 TYR E 250      94.720 152.360 132.166  1.00118.39           C  
ATOM   1742  CE1 TYR E 250      93.942 154.658 130.849  1.00116.24           C  
ATOM   1743  CE2 TYR E 250      95.630 153.382 131.965  1.00117.39           C  
ATOM   1744  CZ  TYR E 250      95.235 154.527 131.305  1.00116.03           C  
ATOM   1745  OH  TYR E 250      96.137 155.547 131.102  1.00117.30           O  
ATOM   1746  N   CYS E 251      91.012 148.620 129.929  1.00114.97           N  
ATOM   1747  CA  CYS E 251      91.143 147.204 129.620  1.00110.90           C  
ATOM   1748  C   CYS E 251      91.640 146.976 128.200  1.00111.35           C  
ATOM   1749  O   CYS E 251      91.710 145.827 127.753  1.00112.08           O  
ATOM   1750  CB  CYS E 251      89.813 146.479 129.835  1.00112.34           C  
ATOM   1751  SG  CYS E 251      88.384 147.250 129.052  1.00124.08           S  
ATOM   1752  N   HIS E 252      91.980 148.045 127.481  1.00 88.12           N  
ATOM   1753  CA  HIS E 252      92.532 147.948 126.137  1.00 88.22           C  
ATOM   1754  C   HIS E 252      93.994 148.353 126.052  1.00 85.90           C  
ATOM   1755  O   HIS E 252      94.681 147.937 125.118  1.00 84.98           O  
ATOM   1756  CB  HIS E 252      91.722 148.811 125.162  1.00 82.34           C  
ATOM   1757  N   VAL E 253      94.483 149.155 126.998  1.00 75.93           N  
ATOM   1758  CA  VAL E 253      95.887 149.549 126.973  1.00 72.86           C  
ATOM   1759  C   VAL E 253      96.728 148.636 127.860  1.00 72.62           C  
ATOM   1760  O   VAL E 253      97.932 148.476 127.626  1.00 70.46           O  
ATOM   1761  CB  VAL E 253      96.034 151.028 127.375  1.00 74.14           C  
ATOM   1762  CG1 VAL E 253      95.740 151.219 128.854  1.00 75.55           C  
ATOM   1763  CG2 VAL E 253      97.422 151.544 127.025  1.00 76.74           C  
ATOM   1764  N   TYR E 254      96.123 148.023 128.881  1.00 70.71           N  
ATOM   1765  CA  TYR E 254      96.869 147.084 129.712  1.00 69.36           C  
ATOM   1766  C   TYR E 254      97.326 145.882 128.899  1.00 77.33           C  
ATOM   1767  O   TYR E 254      98.451 145.399 129.072  1.00 85.64           O  
ATOM   1768  CB  TYR E 254      96.026 146.630 130.904  1.00 67.09           C  
ATOM   1769  CG  TYR E 254      96.637 145.459 131.640  1.00 70.34           C  
ATOM   1770  CD1 TYR E 254      97.918 145.538 132.160  1.00 70.05           C  
ATOM   1771  CD2 TYR E 254      95.942 144.271 131.800  1.00 72.23           C  
ATOM   1772  CE1 TYR E 254      98.488 144.476 132.824  1.00 66.67           C  
ATOM   1773  CE2 TYR E 254      96.506 143.200 132.464  1.00 70.70           C  
ATOM   1774  CZ  TYR E 254      97.779 143.310 132.974  1.00 68.12           C  
ATOM   1775  OH  TYR E 254      98.346 142.248 133.638  1.00 76.17           O  
ATOM   1776  N   LEU E 255      96.463 145.379 128.014  1.00 70.38           N  
ATOM   1777  CA  LEU E 255      96.851 144.271 127.149  1.00 66.84           C  
ATOM   1778  C   LEU E 255      98.018 144.662 126.253  1.00 78.36           C  
ATOM   1779  O   LEU E 255      98.959 143.880 126.064  1.00 76.11           O  
ATOM   1780  CB  LEU E 255      95.655 143.827 126.309  1.00 63.18           C  
ATOM   1781  CG  LEU E 255      94.337 143.674 127.065  1.00 67.33           C  
ATOM   1782  CD1 LEU E 255      93.212 143.293 126.119  1.00 71.53           C  
ATOM   1783  CD2 LEU E 255      94.482 142.643 128.168  1.00 75.31           C  
ATOM   1784  N   VAL E 256      97.975 145.875 125.697  1.00 85.46           N  
ATOM   1785  CA  VAL E 256      99.060 146.346 124.843  1.00 76.21           C  
ATOM   1786  C   VAL E 256     100.360 146.423 125.629  1.00 76.75           C  
ATOM   1787  O   VAL E 256     101.412 145.983 125.155  1.00 85.77           O  
ATOM   1788  CB  VAL E 256      98.697 147.707 124.219  1.00 76.58           C  
ATOM   1789  CG1 VAL E 256      99.889 148.283 123.471  1.00 77.55           C  
ATOM   1790  CG2 VAL E 256      97.498 147.568 123.297  1.00 78.50           C  
ATOM   1791  N   CYS E 257     100.310 146.980 126.842  1.00 64.61           N  
ATOM   1792  CA  CYS E 257     101.519 147.089 127.653  1.00 64.49           C  
ATOM   1793  C   CYS E 257     102.070 145.715 128.016  1.00 68.34           C  
ATOM   1794  O   CYS E 257     103.288 145.491 127.968  1.00 72.54           O  
ATOM   1795  CB  CYS E 257     101.232 147.901 128.915  1.00 64.31           C  
ATOM   1796  SG  CYS E 257     101.481 149.680 128.731  1.00 80.85           S  
ATOM   1797  N   MET E 258     101.187 144.783 128.384  1.00 63.15           N  
ATOM   1798  CA  MET E 258     101.631 143.441 128.740  1.00 64.46           C  
ATOM   1799  C   MET E 258     102.287 142.748 127.556  1.00 65.58           C  
ATOM   1800  O   MET E 258     103.344 142.123 127.701  1.00 67.89           O  
ATOM   1801  CB  MET E 258     100.451 142.618 129.257  1.00 67.16           C  
ATOM   1802  N   SER E 259     101.685 142.859 126.370  1.00 69.69           N  
ATOM   1803  CA  SER E 259     102.273 142.228 125.194  1.00 71.63           C  
ATOM   1804  C   SER E 259     103.573 142.904 124.779  1.00 72.03           C  
ATOM   1805  O   SER E 259     104.487 142.231 124.295  1.00 74.55           O  
ATOM   1806  CB  SER E 259     101.271 142.226 124.045  1.00 70.73           C  
ATOM   1807  OG  SER E 259      99.972 141.960 124.533  1.00 73.20           O  
ATOM   1808  N   LEU E 260     103.678 144.223 124.953  1.00 68.94           N  
ATOM   1809  CA  LEU E 260     104.939 144.900 124.670  1.00 69.18           C  
ATOM   1810  C   LEU E 260     106.042 144.406 125.595  1.00 70.02           C  
ATOM   1811  O   LEU E 260     107.165 144.144 125.150  1.00 67.79           O  
ATOM   1812  CB  LEU E 260     104.769 146.413 124.800  1.00 63.90           C  
ATOM   1813  CG  LEU E 260     103.982 147.113 123.692  1.00 61.32           C  
ATOM   1814  CD1 LEU E 260     103.856 148.598 123.985  1.00 61.56           C  
ATOM   1815  CD2 LEU E 260     104.630 146.880 122.339  1.00 66.07           C  
ATOM   1816  N   SER E 261     105.737 144.271 126.888  1.00 61.81           N  
ATOM   1817  CA  SER E 261     106.725 143.737 127.821  1.00 55.44           C  
ATOM   1818  C   SER E 261     107.094 142.305 127.461  1.00 60.50           C  
ATOM   1819  O   SER E 261     108.267 141.918 127.537  1.00 68.76           O  
ATOM   1820  CB  SER E 261     106.193 143.810 129.250  1.00 61.69           C  
ATOM   1821  OG  SER E 261     104.803 143.546 129.283  1.00 68.09           O  
ATOM   1822  N   SER E 262     106.103 141.505 127.063  1.00 68.70           N  
ATOM   1823  CA  SER E 262     106.375 140.127 126.670  1.00 68.66           C  
ATOM   1824  C   SER E 262     107.285 140.068 125.451  1.00 68.53           C  
ATOM   1825  O   SER E 262     108.217 139.262 125.407  1.00 72.17           O  
ATOM   1826  CB  SER E 262     105.064 139.392 126.392  1.00 69.55           C  
ATOM   1827  OG  SER E 262     105.310 138.069 125.955  1.00 76.50           O  
ATOM   1828  N   LEU E 263     107.031 140.916 124.453  1.00 66.37           N  
ATOM   1829  CA  LEU E 263     107.865 140.919 123.254  1.00 68.59           C  
ATOM   1830  C   LEU E 263     109.271 141.415 123.563  1.00 68.98           C  
ATOM   1831  O   LEU E 263     110.250 140.906 123.004  1.00 67.35           O  
ATOM   1832  CB  LEU E 263     107.214 141.771 122.164  1.00 68.12           C  
ATOM   1833  CG  LEU E 263     107.880 141.770 120.786  1.00 66.89           C  
ATOM   1834  CD1 LEU E 263     106.834 141.601 119.697  1.00 67.54           C  
ATOM   1835  CD2 LEU E 263     108.678 143.045 120.567  1.00 71.06           C  
ATOM   1836  N   ASN E 264     109.392 142.413 124.442  1.00 65.12           N  
ATOM   1837  CA  ASN E 264     110.712 142.872 124.863  1.00 58.39           C  
ATOM   1838  C   ASN E 264     111.482 141.751 125.540  1.00 53.42           C  
ATOM   1839  O   ASN E 264     112.656 141.514 125.237  1.00 55.09           O  
ATOM   1840  CB  ASN E 264     110.575 144.068 125.805  1.00 59.57           C  
ATOM   1841  CG  ASN E 264     111.897 144.483 126.421  1.00 60.95           C  
ATOM   1842  OD1 ASN E 264     112.960 144.298 125.828  1.00 61.81           O  
ATOM   1843  ND2 ASN E 264     111.837 145.048 127.620  1.00 59.88           N  
ATOM   1844  N   SER E 265     110.826 141.034 126.452  1.00 61.51           N  
ATOM   1845  CA  SER E 265     111.486 139.930 127.136  1.00 62.40           C  
ATOM   1846  C   SER E 265     111.811 138.798 126.170  1.00 64.78           C  
ATOM   1847  O   SER E 265     112.805 138.085 126.346  1.00 69.49           O  
ATOM   1848  CB  SER E 265     110.602 139.437 128.278  1.00 60.91           C  
ATOM   1849  OG  SER E 265     110.692 140.298 129.397  1.00 63.56           O  
ATOM   1850  N   SER E 266     110.976 138.614 125.147  1.00 65.24           N  
ATOM   1851  CA  SER E 266     111.201 137.560 124.165  1.00 65.36           C  
ATOM   1852  C   SER E 266     112.417 137.862 123.301  1.00 69.88           C  
ATOM   1853  O   SER E 266     113.263 136.991 123.068  1.00 68.74           O  
ATOM   1854  CB  SER E 266     109.952 137.395 123.299  1.00 63.10           C  
ATOM   1855  OG  SER E 266     109.880 136.101 122.733  1.00 67.55           O  
ATOM   1856  N   ALA E 267     112.517 139.096 122.808  1.00 70.04           N  
ATOM   1857  CA  ALA E 267     113.629 139.491 121.954  1.00 66.54           C  
ATOM   1858  C   ALA E 267     114.884 139.841 122.738  1.00 65.72           C  
ATOM   1859  O   ALA E 267     115.945 140.007 122.129  1.00 71.63           O  
ATOM   1860  CB  ALA E 267     113.225 140.679 121.078  1.00 65.66           C  
ATOM   1861  N   ASN E 268     114.786 139.962 124.061  1.00 62.89           N  
ATOM   1862  CA  ASN E 268     115.956 140.305 124.866  1.00 59.98           C  
ATOM   1863  C   ASN E 268     117.095 139.302 124.728  1.00 63.73           C  
ATOM   1864  O   ASN E 268     118.245 139.737 124.547  1.00 68.25           O  
ATOM   1865  CB  ASN E 268     115.525 140.474 126.326  1.00 61.13           C  
ATOM   1866  CG  ASN E 268     116.372 141.476 127.065  1.00 65.04           C  
ATOM   1867  OD1 ASN E 268     117.107 142.250 126.456  1.00 65.02           O  
ATOM   1868  ND2 ASN E 268     116.267 141.479 128.388  1.00 63.71           N  
ATOM   1869  N   PRO E 269     116.878 137.984 124.817  1.00 63.93           N  
ATOM   1870  CA  PRO E 269     117.996 137.061 124.569  1.00 61.52           C  
ATOM   1871  C   PRO E 269     118.564 137.171 123.169  1.00 64.55           C  
ATOM   1872  O   PRO E 269     119.774 136.990 122.988  1.00 65.40           O  
ATOM   1873  CB  PRO E 269     117.374 135.679 124.815  1.00 65.72           C  
ATOM   1874  CG  PRO E 269     115.921 135.881 124.614  1.00 67.51           C  
ATOM   1875  CD  PRO E 269     115.649 137.246 125.157  1.00 65.37           C  
ATOM   1876  N   ILE E 270     117.723 137.468 122.175  1.00 66.30           N  
ATOM   1877  CA  ILE E 270     118.185 137.522 120.790  1.00 64.46           C  
ATOM   1878  C   ILE E 270     119.292 138.556 120.644  1.00 60.48           C  
ATOM   1879  O   ILE E 270     120.433 138.218 120.316  1.00 61.74           O  
ATOM   1880  CB  ILE E 270     117.014 137.816 119.837  1.00 62.71           C  
ATOM   1881  CG1 ILE E 270     116.153 136.568 119.648  1.00 65.26           C  
ATOM   1882  CG2 ILE E 270     117.531 138.292 118.489  1.00 57.54           C  
ATOM   1883  CD1 ILE E 270     114.965 136.780 118.734  1.00 62.36           C  
ATOM   1884  N   ILE E 271     118.984 139.816 120.965  1.00 55.48           N  
ATOM   1885  CA  ILE E 271     119.913 140.913 120.708  1.00 62.06           C  
ATOM   1886  C   ILE E 271     121.235 140.684 121.427  1.00 63.21           C  
ATOM   1887  O   ILE E 271     122.310 140.968 120.885  1.00 65.57           O  
ATOM   1888  CB  ILE E 271     119.277 142.254 121.120  1.00 55.42           C  
ATOM   1889  CG1 ILE E 271     118.029 142.535 120.286  1.00 54.43           C  
ATOM   1890  CG2 ILE E 271     120.274 143.390 120.973  1.00 58.12           C  
ATOM   1891  CD1 ILE E 271     116.824 142.913 121.110  1.00 57.77           C  
ATOM   1892  N   TYR E 272     121.183 140.159 122.647  1.00 54.13           N  
ATOM   1893  CA  TYR E 272     122.381 140.073 123.467  1.00 57.02           C  
ATOM   1894  C   TYR E 272     123.172 138.786 123.277  1.00 64.50           C  
ATOM   1895  O   TYR E 272     124.351 138.751 123.645  1.00 68.07           O  
ATOM   1896  CB  TYR E 272     122.015 140.244 124.944  1.00 55.31           C  
ATOM   1897  CG  TYR E 272     121.598 141.656 125.284  1.00 59.93           C  
ATOM   1898  CD1 TYR E 272     122.545 142.655 125.459  1.00 63.99           C  
ATOM   1899  CD2 TYR E 272     120.259 141.993 125.418  1.00 56.06           C  
ATOM   1900  CE1 TYR E 272     122.171 143.948 125.763  1.00 59.18           C  
ATOM   1901  CE2 TYR E 272     119.877 143.284 125.722  1.00 54.72           C  
ATOM   1902  CZ  TYR E 272     120.836 144.256 125.893  1.00 55.64           C  
ATOM   1903  OH  TYR E 272     120.459 145.543 126.198  1.00 60.00           O  
ATOM   1904  N   PHE E 273     122.578 137.732 122.723  1.00 63.54           N  
ATOM   1905  CA  PHE E 273     123.397 136.539 122.536  1.00 64.52           C  
ATOM   1906  C   PHE E 273     123.384 135.999 121.114  1.00 66.95           C  
ATOM   1907  O   PHE E 273     124.439 135.619 120.600  1.00 67.21           O  
ATOM   1908  CB  PHE E 273     122.933 135.444 123.504  1.00 57.78           C  
ATOM   1909  CG  PHE E 273     123.878 134.283 123.605  1.00 62.00           C  
ATOM   1910  CD1 PHE E 273     125.016 134.366 124.387  1.00 65.27           C  
ATOM   1911  CD2 PHE E 273     123.624 133.107 122.921  1.00 65.79           C  
ATOM   1912  CE1 PHE E 273     125.885 133.297 124.484  1.00 68.81           C  
ATOM   1913  CE2 PHE E 273     124.489 132.036 123.013  1.00 66.15           C  
ATOM   1914  CZ  PHE E 273     125.621 132.131 123.796  1.00 68.83           C  
ATOM   1915  N   PHE E 274     122.222 135.967 120.460  1.00 63.29           N  
ATOM   1916  CA  PHE E 274     122.121 135.305 119.168  1.00 58.16           C  
ATOM   1917  C   PHE E 274     122.742 136.136 118.058  1.00 63.46           C  
ATOM   1918  O   PHE E 274     123.277 135.574 117.098  1.00 71.19           O  
ATOM   1919  CB  PHE E 274     120.658 135.004 118.846  1.00 63.06           C  
ATOM   1920  CG  PHE E 274     120.054 133.945 119.721  1.00 65.75           C  
ATOM   1921  CD1 PHE E 274     120.858 133.018 120.363  1.00 64.88           C  
ATOM   1922  CD2 PHE E 274     118.685 133.879 119.906  1.00 63.07           C  
ATOM   1923  CE1 PHE E 274     120.306 132.044 121.170  1.00 63.56           C  
ATOM   1924  CE2 PHE E 274     118.128 132.907 120.712  1.00 62.66           C  
ATOM   1925  CZ  PHE E 274     118.940 131.989 121.345  1.00 64.04           C  
ATOM   1926  N   VAL E 275     122.679 137.463 118.169  1.00 63.86           N  
ATOM   1927  CA  VAL E 275     123.347 138.318 117.194  1.00 64.25           C  
ATOM   1928  C   VAL E 275     124.850 138.080 117.230  1.00 63.94           C  
ATOM   1929  O   VAL E 275     125.500 137.950 116.185  1.00 66.24           O  
ATOM   1930  CB  VAL E 275     122.994 139.794 117.452  1.00 64.07           C  
ATOM   1931  CG1 VAL E 275     124.087 140.710 116.925  1.00 67.21           C  
ATOM   1932  CG2 VAL E 275     121.654 140.134 116.820  1.00 63.89           C  
ATOM   1933  N   GLY E 276     125.423 138.004 118.432  1.00 66.72           N  
ATOM   1934  CA  GLY E 276     126.843 137.719 118.546  1.00 70.70           C  
ATOM   1935  C   GLY E 276     127.203 136.320 118.081  1.00 72.10           C  
ATOM   1936  O   GLY E 276     128.211 136.126 117.395  1.00 72.04           O  
ATOM   1937  N   SER E 277     126.389 135.327 118.448  1.00 76.10           N  
ATOM   1938  CA  SER E 277     126.682 133.950 118.060  1.00 76.79           C  
ATOM   1939  C   SER E 277     126.608 133.770 116.548  1.00 76.40           C  
ATOM   1940  O   SER E 277     127.446 133.080 115.956  1.00 75.16           O  
ATOM   1941  CB  SER E 277     125.721 132.991 118.762  1.00 73.01           C  
ATOM   1942  N   PHE E 278     125.616 134.387 115.904  1.00 77.30           N  
ATOM   1943  CA  PHE E 278     125.440 134.267 114.463  1.00 77.40           C  
ATOM   1944  C   PHE E 278     126.337 135.210 113.674  1.00 81.61           C  
ATOM   1945  O   PHE E 278     126.317 135.166 112.440  1.00 81.61           O  
ATOM   1946  CB  PHE E 278     123.977 134.519 114.090  1.00 74.67           C  
ATOM   1947  N   ARG E 279     127.111 136.064 114.349  1.00 81.66           N  
ATOM   1948  CA  ARG E 279     128.032 136.950 113.647  1.00 81.36           C  
ATOM   1949  C   ARG E 279     129.179 136.191 112.992  1.00 78.82           C  
ATOM   1950  O   ARG E 279     129.806 136.718 112.067  1.00 74.31           O  
ATOM   1951  CB  ARG E 279     128.586 138.003 114.608  1.00 77.21           C  
ATOM   1952  N   GLN E 280     129.466 134.976 113.447  1.00 76.61           N  
ATOM   1953  CA  GLN E 280     130.534 134.174 112.864  1.00 77.19           C  
ATOM   1954  C   GLN E 280     130.105 132.718 112.717  1.00 79.11           C  
ATOM   1955  O   GLN E 280     128.975 132.430 112.322  1.00 76.48           O  
ATOM   1956  CB  GLN E 280     131.801 134.268 113.716  1.00 77.14           C  
TER    1957      GLN E 280                                                      
HETATM 1958  C1  JW0 E 601      95.670 144.211 135.671  1.00103.79           C  
HETATM 1959  C2  JW0 E 601      94.792 144.272 136.918  1.00106.33           C  
HETATM 1960  C3  JW0 E 601      95.104 145.568 137.697  1.00106.67           C  
HETATM 1961  O3  JW0 E 601     106.629 150.107 140.577  1.00104.53           O  
HETATM 1962  C4  JW0 E 601      96.595 145.823 137.975  1.00108.18           C  
HETATM 1963  C5  JW0 E 601      97.478 145.538 136.776  1.00107.28           C  
HETATM 1964  O5  JW0 E 601      94.119 141.761 135.704  1.00106.79           O  
HETATM 1965  C6  JW0 E 601      97.148 144.233 136.193  1.00104.09           C  
HETATM 1966  C10 JW0 E 601      99.017 145.474 137.158  1.00107.13           C  
HETATM 1967  C11 JW0 E 601     100.640 145.485 138.762  1.00107.35           C  
HETATM 1968  C12 JW0 E 601     101.449 146.569 138.113  1.00108.87           C  
HETATM 1969  C13 JW0 E 601     101.236 146.592 136.596  1.00106.91           C  
HETATM 1970  C14 JW0 E 601      99.756 146.348 136.246  1.00105.89           C  
HETATM 1971  C15 JW0 E 601     101.081 145.611 140.240  1.00105.82           C  
HETATM 1972  C16 JW0 E 601     102.569 146.185 140.041  1.00107.05           C  
HETATM 1973  C17 JW0 E 601     102.795 146.186 138.528  1.00107.35           C  
HETATM 1974  C18 JW0 E 601     103.815 147.254 138.099  1.00107.50           C  
HETATM 1975  C19 JW0 E 601     104.446 147.853 139.343  1.00106.23           C  
HETATM 1976  C20 JW0 E 601     105.779 148.529 139.007  1.00105.46           C  
HETATM 1977  C21 JW0 E 601     104.885 146.578 137.246  1.00107.28           C  
HETATM 1978  C22 JW0 E 601     101.000 147.833 138.865  1.00106.60           C  
HETATM 1979  C23 JW0 E 601      97.301 146.644 135.717  1.00107.49           C  
HETATM 1980  C24 JW0 E 601     105.786 149.872 139.699  1.00105.23           C  
HETATM 1981  C7  JW0 E 601      97.018 144.929 139.137  1.00106.35           C  
HETATM 1982  C8  JW0 E 601      98.367 145.273 139.621  1.00105.75           C  
HETATM 1983  C9  JW0 E 601      99.247 145.949 138.551  1.00107.69           C  
HETATM 1984  O1  JW0 E 601     101.949 145.541 136.115  1.00107.86           O  
HETATM 1985  O2  JW0 E 601     104.924 150.737 139.388  1.00106.90           O  
HETATM 1986  O4  JW0 E 601      95.130 143.160 137.667  1.00108.86           O  
HETATM 1987  O6  JW0 E 601      93.388 141.264 137.953  1.00109.25           O1-
HETATM 1988  O7  JW0 E 601      95.729 140.667 137.230  1.00106.79           O  
HETATM 1989  P1  JW0 E 601      94.588 141.658 137.128  1.00115.09           P  
CONECT   13 1751                                                                
CONECT 1751   13                                                                
CONECT 1958 1959 1965                                                           
CONECT 1959 1958 1960 1986                                                      
CONECT 1960 1959 1962                                                           
CONECT 1961 1980                                                                
CONECT 1962 1960 1963 1981                                                      
CONECT 1963 1962 1965 1966 1979                                                 
CONECT 1964 1989                                                                
CONECT 1965 1958 1963                                                           
CONECT 1966 1963 1970 1983                                                      
CONECT 1967 1968 1971 1983                                                      
CONECT 1968 1967 1969 1973 1978                                                 
CONECT 1969 1968 1970 1984                                                      
CONECT 1970 1966 1969                                                           
CONECT 1971 1967 1972                                                           
CONECT 1972 1971 1973                                                           
CONECT 1973 1968 1972 1974                                                      
CONECT 1974 1973 1975 1977                                                      
CONECT 1975 1974 1976                                                           
CONECT 1976 1975 1980                                                           
CONECT 1977 1974                                                                
CONECT 1978 1968                                                                
CONECT 1979 1963                                                                
CONECT 1980 1961 1976 1985                                                      
CONECT 1981 1962 1982                                                           
CONECT 1982 1981 1983                                                           
CONECT 1983 1966 1967 1982                                                      
CONECT 1984 1969                                                                
CONECT 1985 1980                                                                
CONECT 1986 1959 1989                                                           
CONECT 1987 1989                                                                
CONECT 1988 1989                                                                
CONECT 1989 1964 1986 1987 1988                                                 
MASTER      658    0    1   10    0    0    0    6 1988    1   34   55          
END