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Database: PDB
Entry: 6JT0
LinkDB: 6JT0
Original site: 6JT0 
HEADER    SIGNALING PROTEIN                       08-APR-19   6JT0              
TITLE     STRUCTURE OF HUMAN SOLUBLE GUANYLATE CYCLASE IN THE UNLIGANDED STATE  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GUANYLATE CYCLASE SOLUBLE SUBUNIT ALPHA-1;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GCS-ALPHA-1,GUANYLATE CYCLASE SOLUBLE SUBUNIT ALPHA-3,GCS-  
COMPND   5 ALPHA-3,SOLUBLE GUANYLATE CYCLASE LARGE SUBUNIT;                     
COMPND   6 EC: 4.6.1.2;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: GENBANK: AAH28384.1;                                  
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1;                  
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: GCS-BETA-1,GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-3,GCS-    
COMPND  13 BETA-3,SOLUBLE GUANYLATE CYCLASE SMALL SUBUNIT;                      
COMPND  14 EC: 4.6.1.2;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GUCY1A1, GUC1A3, GUCSA3, GUCY1A3;                              
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: GUCY1B1, GUC1B3, GUCSB3, GUCY1B3;                              
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    SOLUBLE GUANYLATE CYCLASE, SIGNALING PROTEIN                          
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    L.CHEN,Y.KANG,R.LIU,J.-X.WU                                           
REVDAT   5   06-NOV-19 6JT0    1       CRYST1                                   
REVDAT   4   23-OCT-19 6JT0    1       JRNL                                     
REVDAT   3   16-OCT-19 6JT0    1       JRNL                                     
REVDAT   2   09-OCT-19 6JT0    1       JRNL                                     
REVDAT   1   28-AUG-19 6JT0    0                                                
JRNL        AUTH   Y.KANG,R.LIU,J.X.WU,L.CHEN                                   
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE MECHANISM OF HUMAN SOLUBLE      
JRNL        TITL 2 GUANYLATE CYCLASE.                                           
JRNL        REF    NATURE                        V. 574   206 2019              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   31514202                                                     
JRNL        DOI    10.1038/S41586-019-1584-6                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION                                    
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)  : 4.000                          
REMARK   3   NUMBER OF PARTICLES               : 229111                         
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6JT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300011711.                                   
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                 : HUMAN SOLUBLE GUANYLATE CYCLASE   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 QUANTUM (4K X 4K)     
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
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)  : 50.00                          
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     MET A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     CYS A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     PHE A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     CYS A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     THR A    43                                                      
REMARK 465     MET A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     CYS A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ILE A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     GLU A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ASN A    54                                                      
REMARK 465     ILE A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     SER A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     ARG A    62                                                      
REMARK 465     LYS A    63                                                      
REMARK 465     THR A    64                                                      
REMARK 465     SER A    65                                                      
REMARK 465     ARG A    66                                                      
REMARK 465     SER A    67                                                      
REMARK 465     ARG A    68                                                      
REMARK 465     ILE A   102                                                      
REMARK 465     LYS A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     ARG A   106                                                      
REMARK 465     LYS A   107                                                      
REMARK 465     SER A   108                                                      
REMARK 465     LEU A   109                                                      
REMARK 465     GLU A   110                                                      
REMARK 465     ARG A   111                                                      
REMARK 465     GLU A   112                                                      
REMARK 465     ASP A   113                                                      
REMARK 465     HIS A   175                                                      
REMARK 465     CYS A   176                                                      
REMARK 465     GLN A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     ALA A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     ARG A   182                                                      
REMARK 465     GLY A   183                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     LEU A   185                                                      
REMARK 465     GLU A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     MET A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     LYS A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     SER A   265                                                      
REMARK 465     LEU A   266                                                      
REMARK 465     SER A   267                                                      
REMARK 465     PRO A   268                                                      
REMARK 465     SER A   269                                                      
REMARK 465     LYS A   270                                                      
REMARK 465     PRO A   271                                                      
REMARK 465     GLN A   272                                                      
REMARK 465     SER A   273                                                      
REMARK 465     PHE A   314                                                      
REMARK 465     GLN A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASN A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     VAL A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     LYS A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 465     GLN A   661                                                      
REMARK 465     GLN A   662                                                      
REMARK 465     GLY A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     ASN A   665                                                      
REMARK 465     SER A   666                                                      
REMARK 465     LYS A   667                                                      
REMARK 465     PRO A   668                                                      
REMARK 465     CYS A   669                                                      
REMARK 465     PHE A   670                                                      
REMARK 465     GLN A   671                                                      
REMARK 465     LYS A   672                                                      
REMARK 465     LYS A   673                                                      
REMARK 465     ASP A   674                                                      
REMARK 465     VAL A   675                                                      
REMARK 465     GLU A   676                                                      
REMARK 465     ASP A   677                                                      
REMARK 465     GLY A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     ALA A   680                                                      
REMARK 465     ASN A   681                                                      
REMARK 465     PHE A   682                                                      
REMARK 465     LEU A   683                                                      
REMARK 465     GLY A   684                                                      
REMARK 465     LYS A   685                                                      
REMARK 465     ALA A   686                                                      
REMARK 465     SER A   687                                                      
REMARK 465     GLY A   688                                                      
REMARK 465     ILE A   689                                                      
REMARK 465     ASP A   690                                                      
REMARK 465     GLU B   188                                                      
REMARK 465     GLU B   189                                                      
REMARK 465     ASP B   190                                                      
REMARK 465     PHE B   191                                                      
REMARK 465     TYR B   192                                                      
REMARK 465     GLU B   193                                                      
REMARK 465     ASP B   194                                                      
REMARK 465     LEU B   195                                                      
REMARK 465     ASP B   196                                                      
REMARK 465     ARG B   197                                                      
REMARK 465     PHE B   198                                                      
REMARK 465     GLU B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     ASN B   201                                                      
REMARK 465     GLY B   202                                                      
REMARK 465     THR B   203                                                      
REMARK 465     VAL B   287                                                      
REMARK 465     GLU B   288                                                      
REMARK 465     LYS B   289                                                      
REMARK 465     LEU B   290                                                      
REMARK 465     GLU B   291                                                      
REMARK 465     CYS B   292                                                      
REMARK 465     GLU B   293                                                      
REMARK 465     ASP B   294                                                      
REMARK 465     GLU B   295                                                      
REMARK 465     LEU B   296                                                      
REMARK 465     THR B   297                                                      
REMARK 465     GLY B   298                                                      
REMARK 465     THR B   299                                                      
REMARK 465     GLU B   300                                                      
REMARK 465     ILE B   301                                                      
REMARK 465     ASN B   608                                                      
REMARK 465     THR B   609                                                      
REMARK 465     GLY B   610                                                      
REMARK 465     THR B   611                                                      
REMARK 465     GLU B   612                                                      
REMARK 465     GLU B   613                                                      
REMARK 465     THR B   614                                                      
REMARK 465     LYS B   615                                                      
REMARK 465     GLN B   616                                                      
REMARK 465     ASP B   617                                                      
REMARK 465     ASP B   618                                                      
REMARK 465     ASP B   619                                                      
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     GLU A  85    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 114    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 115    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 116    CG   CD   CE   NZ                                   
REMARK 470     THR A 117    OG1  CG2                                            
REMARK 470     ILE A 118    CG1  CG2  CD1                                       
REMARK 470     GLU A 120    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 121    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 123    CG1  CG2                                            
REMARK 470     VAL A 127    CG1  CG2                                            
REMARK 470     GLU A 130    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 131    CG1  CG2                                            
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     GLU A 134    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 147    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 148    CG   OD1  OD2                                       
REMARK 470     ASP A 194    CG   OD1  OD2                                       
REMARK 470     LYS A 195    CG   CD   CE   NZ                                   
REMARK 470     GLU A 196    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 197    CG   OD1  OD2                                       
REMARK 470     ASP A 198    CG   OD1  OD2                                       
REMARK 470     CYS A 239    SG                                                  
REMARK 470     PHE A 240    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS A 241    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 242    CG   OD1  ND2                                       
REMARK 470     ASP A 243    CG   OD1  OD2                                       
REMARK 470     CYS A 244    SG                                                  
REMARK 470     GLU A 246    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 250    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 311    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 312    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 313    CG   OD1  OD2                                       
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     ARG A 362    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 422    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 423    CG   OD1  OD2                                       
REMARK 470     GLU A 445    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 470    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 501    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 515    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 519    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 540    CG   CD   CE   NZ                                   
REMARK 470     GLU A 541    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 555    CE   NZ                                             
REMARK 470     GLU A 562    CG   CD   OE1  OE2                                  
REMARK 470     MET A 564    CG   SD   CE                                        
REMARK 470     LYS A 572    NZ                                                  
REMARK 470     LYS A 590    CG   CD   CE   NZ                                   
REMARK 470     ASP A 628    CG   OD1  OD2                                       
REMARK 470     PHE A 634    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 640    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 641    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 649    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  20    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  23    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  27    CG   CD   CE   NZ                                   
REMARK 470     GLU B  33    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 126    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 127    CG   CD   CE   NZ                                   
REMARK 470     LYS B 129    CG   CD   CE   NZ                                   
REMARK 470     GLU B 140    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 172    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 173    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 182    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     ASN B 247    CG   OD1  ND2                                       
REMARK 470     ASP B 262    CG   OD1  OD2                                       
REMARK 470     GLU B 282    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 357    CG   CD   OE1  OE2                                  
REMARK 470     PHE B 359    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 410    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 415    CG   CD   CE   NZ                                   
REMARK 470     GLU B 441    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 445    CG   CD   CE   NZ                                   
REMARK 470     ASP B 513    CG   OD1  OD2                                       
REMARK 470     GLU B 515    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 554    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 558    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 559    CG   CD   CE   NZ                                   
REMARK 470     LYS B 561    CG   CD   CE   NZ                                   
REMARK 470     GLU B 566    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 576    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 593    CG   CD   CE   NZ                                   
REMARK 470     LYS B 595    CG   CD   CE   NZ                                   
REMARK 470     LYS B 596    CG   CD   CE   NZ                                   
REMARK 470     LYS B 607    CG   CD   CE   NZ                                   
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    PRO A 238        4.54    -67.78                                   
REMARK 500    ASP A 243       -1.87     69.28                                   
REMARK 500    CYS A 386       37.37    -97.23                                   
REMARK 500    LEU A 398      -80.15    -84.14                                   
REMARK 500    TYR A 399      177.90    165.72                                   
REMARK 500    ASP A 423       -7.78     74.81                                   
REMARK 500    LEU A 425       -4.30     66.26                                   
REMARK 500    GLN A 470        8.70     59.62                                   
REMARK 500    ASP A 521       64.79     60.98                                   
REMARK 500    ALA B  29        3.06    -68.71                                   
REMARK 500    ILE B  42      125.22    -37.90                                   
REMARK 500    ASN B  60       58.88     39.36                                   
REMARK 500    SER B 209       81.50     54.38                                   
REMARK 500    PRO B 210       -7.68    -47.21                                   
REMARK 500    LEU B 304       67.23     60.76                                   
REMARK 500    LEU B 338      -81.78    -66.81                                   
REMARK 500    TYR B 339      178.47    167.05                                   
REMARK 500    GLU B 357        2.28    -65.22                                   
REMARK 500    HIS B 408       20.88   -140.59                                   
REMARK 500    GLU B 487       71.38     57.53                                   
REMARK 500    HIS B 491       52.39    -92.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 1000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-9883   RELATED DB: EMDB                              
REMARK 900 STRUCTURE OF HUMAN SOLUBLE GUANYLATE CYCLASE IN THE UNLIGANDED STATE 
DBREF  6JT0 A    1   690  UNP    Q02108   GCYA1_HUMAN      1    690             
DBREF  6JT0 B    1   619  UNP    Q02153   GCYB1_HUMAN      1    619             
SEQADV 6JT0 MET A   44  UNP  Q02108    VAL    44 VARIANT                        
SEQADV 6JT0 VAL A  554  UNP  Q02108    LEU   554 VARIANT                        
SEQRES   1 A  690  MET PHE CYS THR LYS LEU LYS ASP LEU LYS ILE THR GLY          
SEQRES   2 A  690  GLU CYS PRO PHE SER LEU LEU ALA PRO GLY GLN VAL PRO          
SEQRES   3 A  690  ASN GLU SER SER GLU GLU ALA ALA GLY SER SER GLU SER          
SEQRES   4 A  690  CYS LYS ALA THR MET PRO ILE CYS GLN ASP ILE PRO GLU          
SEQRES   5 A  690  LYS ASN ILE GLN GLU SER LEU PRO GLN ARG LYS THR SER          
SEQRES   6 A  690  ARG SER ARG VAL TYR LEU HIS THR LEU ALA GLU SER ILE          
SEQRES   7 A  690  CYS LYS LEU ILE PHE PRO GLU PHE GLU ARG LEU ASN VAL          
SEQRES   8 A  690  ALA LEU GLN ARG THR LEU ALA LYS HIS LYS ILE LYS GLU          
SEQRES   9 A  690  SER ARG LYS SER LEU GLU ARG GLU ASP PHE GLU LYS THR          
SEQRES  10 A  690  ILE ALA GLU GLN ALA VAL ALA ALA GLY VAL PRO VAL GLU          
SEQRES  11 A  690  VAL ILE LYS GLU SER LEU GLY GLU GLU VAL PHE LYS ILE          
SEQRES  12 A  690  CYS TYR GLU GLU ASP GLU ASN ILE LEU GLY VAL VAL GLY          
SEQRES  13 A  690  GLY THR LEU LYS ASP PHE LEU ASN SER PHE SER THR LEU          
SEQRES  14 A  690  LEU LYS GLN SER SER HIS CYS GLN GLU ALA GLY LYS ARG          
SEQRES  15 A  690  GLY ARG LEU GLU ASP ALA SER ILE LEU CYS LEU ASP LYS          
SEQRES  16 A  690  GLU ASP ASP PHE LEU HIS VAL TYR TYR PHE PHE PRO LYS          
SEQRES  17 A  690  ARG THR THR SER LEU ILE LEU PRO GLY ILE ILE LYS ALA          
SEQRES  18 A  690  ALA ALA HIS VAL LEU TYR GLU THR GLU VAL GLU VAL SER          
SEQRES  19 A  690  LEU MET PRO PRO CYS PHE HIS ASN ASP CYS SER GLU PHE          
SEQRES  20 A  690  VAL ASN GLN PRO TYR LEU LEU TYR SER VAL HIS MET LYS          
SEQRES  21 A  690  SER THR LYS PRO SER LEU SER PRO SER LYS PRO GLN SER          
SEQRES  22 A  690  SER LEU VAL ILE PRO THR SER LEU PHE CYS LYS THR PHE          
SEQRES  23 A  690  PRO PHE HIS PHE MET PHE ASP LYS ASP MET THR ILE LEU          
SEQRES  24 A  690  GLN PHE GLY ASN GLY ILE ARG ARG LEU MET ASN ARG ARG          
SEQRES  25 A  690  ASP PHE GLN GLY LYS PRO ASN PHE GLU GLU TYR PHE GLU          
SEQRES  26 A  690  ILE LEU THR PRO LYS ILE ASN GLN THR PHE SER GLY ILE          
SEQRES  27 A  690  MET THR MET LEU ASN MET GLN PHE VAL VAL ARG VAL ARG          
SEQRES  28 A  690  ARG TRP ASP ASN SER VAL LYS LYS SER SER ARG VAL MET          
SEQRES  29 A  690  ASP LEU LYS GLY GLN MET ILE TYR ILE VAL GLU SER SER          
SEQRES  30 A  690  ALA ILE LEU PHE LEU GLY SER PRO CYS VAL ASP ARG LEU          
SEQRES  31 A  690  GLU ASP PHE THR GLY ARG GLY LEU TYR LEU SER ASP ILE          
SEQRES  32 A  690  PRO ILE HIS ASN ALA LEU ARG ASP VAL VAL LEU ILE GLY          
SEQRES  33 A  690  GLU GLN ALA ARG ALA GLN ASP GLY LEU LYS LYS ARG LEU          
SEQRES  34 A  690  GLY LYS LEU LYS ALA THR LEU GLU GLN ALA HIS GLN ALA          
SEQRES  35 A  690  LEU GLU GLU GLU LYS LYS LYS THR VAL ASP LEU LEU CYS          
SEQRES  36 A  690  SER ILE PHE PRO CYS GLU VAL ALA GLN GLN LEU TRP GLN          
SEQRES  37 A  690  GLY GLN VAL VAL GLN ALA LYS LYS PHE SER ASN VAL THR          
SEQRES  38 A  690  MET LEU PHE SER ASP ILE VAL GLY PHE THR ALA ILE CYS          
SEQRES  39 A  690  SER GLN CYS SER PRO LEU GLN VAL ILE THR MET LEU ASN          
SEQRES  40 A  690  ALA LEU TYR THR ARG PHE ASP GLN GLN CYS GLY GLU LEU          
SEQRES  41 A  690  ASP VAL TYR LYS VAL GLU THR ILE GLY ASP ALA TYR CYS          
SEQRES  42 A  690  VAL ALA GLY GLY LEU HIS LYS GLU SER ASP THR HIS ALA          
SEQRES  43 A  690  VAL GLN ILE ALA LEU MET ALA VAL LYS MET MET GLU LEU          
SEQRES  44 A  690  SER ASP GLU VAL MET SER PRO HIS GLY GLU PRO ILE LYS          
SEQRES  45 A  690  MET ARG ILE GLY LEU HIS SER GLY SER VAL PHE ALA GLY          
SEQRES  46 A  690  VAL VAL GLY VAL LYS MET PRO ARG TYR CYS LEU PHE GLY          
SEQRES  47 A  690  ASN ASN VAL THR LEU ALA ASN LYS PHE GLU SER CYS SER          
SEQRES  48 A  690  VAL PRO ARG LYS ILE ASN VAL SER PRO THR THR TYR ARG          
SEQRES  49 A  690  LEU LEU LYS ASP CYS PRO GLY PHE VAL PHE THR PRO ARG          
SEQRES  50 A  690  SER ARG GLU GLU LEU PRO PRO ASN PHE PRO SER GLU ILE          
SEQRES  51 A  690  PRO GLY ILE CYS HIS PHE LEU ASP ALA TYR GLN GLN GLY          
SEQRES  52 A  690  THR ASN SER LYS PRO CYS PHE GLN LYS LYS ASP VAL GLU          
SEQRES  53 A  690  ASP GLY ASN ALA ASN PHE LEU GLY LYS ALA SER GLY ILE          
SEQRES  54 A  690  ASP                                                          
SEQRES   1 B  619  MET TYR GLY PHE VAL ASN HIS ALA LEU GLU LEU LEU VAL          
SEQRES   2 B  619  ILE ARG ASN TYR GLY PRO GLU VAL TRP GLU ASP ILE LYS          
SEQRES   3 B  619  LYS GLU ALA GLN LEU ASP GLU GLU GLY GLN PHE LEU VAL          
SEQRES   4 B  619  ARG ILE ILE TYR ASP ASP SER LYS THR TYR ASP LEU VAL          
SEQRES   5 B  619  ALA ALA ALA SER LYS VAL LEU ASN LEU ASN ALA GLY GLU          
SEQRES   6 B  619  ILE LEU GLN MET PHE GLY LYS MET PHE PHE VAL PHE CYS          
SEQRES   7 B  619  GLN GLU SER GLY TYR ASP THR ILE LEU ARG VAL LEU GLY          
SEQRES   8 B  619  SER ASN VAL ARG GLU PHE LEU GLN ASN LEU ASP ALA LEU          
SEQRES   9 B  619  HIS ASP HIS LEU ALA THR ILE TYR PRO GLY MET ARG ALA          
SEQRES  10 B  619  PRO SER PHE ARG CYS THR ASP ALA GLU LYS GLY LYS GLY          
SEQRES  11 B  619  LEU ILE LEU HIS TYR TYR SER GLU ARG GLU GLY LEU GLN          
SEQRES  12 B  619  ASP ILE VAL ILE GLY ILE ILE LYS THR VAL ALA GLN GLN          
SEQRES  13 B  619  ILE HIS GLY THR GLU ILE ASP MET LYS VAL ILE GLN GLN          
SEQRES  14 B  619  ARG ASN GLU GLU CYS ASP HIS THR GLN PHE LEU ILE GLU          
SEQRES  15 B  619  GLU LYS GLU SER LYS GLU GLU ASP PHE TYR GLU ASP LEU          
SEQRES  16 B  619  ASP ARG PHE GLU GLU ASN GLY THR GLN GLU SER ARG ILE          
SEQRES  17 B  619  SER PRO TYR THR PHE CYS LYS ALA PHE PRO PHE HIS ILE          
SEQRES  18 B  619  ILE PHE ASP ARG ASP LEU VAL VAL THR GLN CYS GLY ASN          
SEQRES  19 B  619  ALA ILE TYR ARG VAL LEU PRO GLN LEU GLN PRO GLY ASN          
SEQRES  20 B  619  CYS SER LEU LEU SER VAL PHE SER LEU VAL ARG PRO HIS          
SEQRES  21 B  619  ILE ASP ILE SER PHE HIS GLY ILE LEU SER HIS ILE ASN          
SEQRES  22 B  619  THR VAL PHE VAL LEU ARG SER LYS GLU GLY LEU LEU ASP          
SEQRES  23 B  619  VAL GLU LYS LEU GLU CYS GLU ASP GLU LEU THR GLY THR          
SEQRES  24 B  619  GLU ILE SER CYS LEU ARG LEU LYS GLY GLN MET ILE TYR          
SEQRES  25 B  619  LEU PRO GLU ALA ASP SER ILE LEU PHE LEU CYS SER PRO          
SEQRES  26 B  619  SER VAL MET ASN LEU ASP ASP LEU THR ARG ARG GLY LEU          
SEQRES  27 B  619  TYR LEU SER ASP ILE PRO LEU HIS ASP ALA THR ARG ASP          
SEQRES  28 B  619  LEU VAL LEU LEU GLY GLU GLN PHE ARG GLU GLU TYR LYS          
SEQRES  29 B  619  LEU THR GLN GLU LEU GLU ILE LEU THR ASP ARG LEU GLN          
SEQRES  30 B  619  LEU THR LEU ARG ALA LEU GLU ASP GLU LYS LYS LYS THR          
SEQRES  31 B  619  ASP THR LEU LEU TYR SER VAL LEU PRO PRO SER VAL ALA          
SEQRES  32 B  619  ASN GLU LEU ARG HIS LYS ARG PRO VAL PRO ALA LYS ARG          
SEQRES  33 B  619  TYR ASP ASN VAL THR ILE LEU PHE SER GLY ILE VAL GLY          
SEQRES  34 B  619  PHE ASN ALA PHE CYS SER LYS HIS ALA SER GLY GLU GLY          
SEQRES  35 B  619  ALA MET LYS ILE VAL ASN LEU LEU ASN ASP LEU TYR THR          
SEQRES  36 B  619  ARG PHE ASP THR LEU THR ASP SER ARG LYS ASN PRO PHE          
SEQRES  37 B  619  VAL TYR LYS VAL GLU THR VAL GLY ASP LYS TYR MET THR          
SEQRES  38 B  619  VAL SER GLY LEU PRO GLU PRO CYS ILE HIS HIS ALA ARG          
SEQRES  39 B  619  SER ILE CYS HIS LEU ALA LEU ASP MET MET GLU ILE ALA          
SEQRES  40 B  619  GLY GLN VAL GLN VAL ASP GLY GLU SER VAL GLN ILE THR          
SEQRES  41 B  619  ILE GLY ILE HIS THR GLY GLU VAL VAL THR GLY VAL ILE          
SEQRES  42 B  619  GLY GLN ARG MET PRO ARG TYR CYS LEU PHE GLY ASN THR          
SEQRES  43 B  619  VAL ASN LEU THR SER ARG THR GLU THR THR GLY GLU LYS          
SEQRES  44 B  619  GLY LYS ILE ASN VAL SER GLU TYR THR TYR ARG CYS LEU          
SEQRES  45 B  619  MET SER PRO GLU ASN SER ASP PRO GLN PHE HIS LEU GLU          
SEQRES  46 B  619  HIS ARG GLY PRO VAL SER MET LYS GLY LYS LYS GLU PRO          
SEQRES  47 B  619  MET GLN VAL TRP PHE LEU SER ARG LYS ASN THR GLY THR          
SEQRES  48 B  619  GLU GLU THR LYS GLN ASP ASP ASP                              
HET    HEM  B1000      43                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   3  HEM    C34 H32 FE N4 O4                                             
HELIX    1 AA1 TYR A   70  PHE A   83  1                                  14    
HELIX    2 AA2 GLU A   85  LYS A  101  1                                  17    
HELIX    3 AA3 GLU A  115  GLY A  126  1                                  12    
HELIX    4 AA4 PRO A  128  GLU A  149  1                                  22    
HELIX    5 AA5 ASN A  150  GLY A  156  1                                   7    
HELIX    6 AA6 THR A  158  SER A  174  1                                  17    
HELIX    7 AA7 ILE A  214  TYR A  227  1                                  14    
HELIX    8 AA8 PRO A  237  ASN A  242  1                                   6    
HELIX    9 AA9 PRO A  278  PHE A  286  1                                   9    
HELIX   10 AB1 GLY A  302  MET A  309  1                                   8    
HELIX   11 AB2 ASN A  319  TYR A  323  1                                   5    
HELIX   12 AB3 THR A  334  MET A  341  1                                   8    
HELIX   13 AB4 ARG A  389  THR A  394  5                                   6    
HELIX   14 AB5 LEU A  409  ALA A  419  1                                  11    
HELIX   15 AB6 LYS A  426  PHE A  458  1                                  33    
HELIX   16 AB7 PRO A  459  GLN A  468  1                                  10    
HELIX   17 AB8 GLY A  489  GLN A  496  1                                   8    
HELIX   18 AB9 SER A  498  ASP A  521  1                                  24    
HELIX   19 AC1 THR A  544  ASP A  561  1                                  18    
HELIX   20 AC2 GLY A  598  SER A  609  1                                  12    
HELIX   21 AC3 SER A  619  LYS A  627  1                                   9    
HELIX   22 AC4 TYR B    2  GLN B   30  1                                  29    
HELIX   23 AC5 ASP B   44  LEU B   59  1                                  16    
HELIX   24 AC6 ASN B   62  SER B   81  1                                  20    
HELIX   25 AC7 TYR B   83  LEU B   90  1                                   8    
HELIX   26 AC8 ASN B   93  ASN B  100  1                                   8    
HELIX   27 AC9 ASP B  102  TYR B  112  1                                  11    
HELIX   28 AD1 ASP B  144  ILE B  157  1                                  14    
HELIX   29 AD2 PRO B  210  PHE B  217  1                                   8    
HELIX   30 AD3 GLY B  233  LEU B  240  1                                   8    
HELIX   31 AD4 PRO B  241  GLN B  244  5                                   4    
HELIX   32 AD5 SER B  264  HIS B  271  1                                   8    
HELIX   33 AD6 ASN B  329  GLY B  337  1                                   9    
HELIX   34 AD7 ASP B  347  LEU B  354  1                                   8    
HELIX   35 AD8 PHE B  359  TYR B  395  1                                  37    
HELIX   36 AD9 PRO B  399  ARG B  407  1                                   9    
HELIX   37 AE1 GLY B  429  HIS B  437  1                                   9    
HELIX   38 AE2 SER B  439  THR B  461  1                                  23    
HELIX   39 AE3 HIS B  491  GLY B  508  1                                  18    
HELIX   40 AE4 GLY B  544  GLY B  557  1                                  14    
HELIX   41 AE5 GLU B  566  MET B  573  1                                   8    
SHEET    1 AA1 4 SER A 189  LEU A 193  0                                        
SHEET    2 AA1 4 LEU A 200  PHE A 205 -1  O  HIS A 201   N  LEU A 193           
SHEET    3 AA1 4 TYR A 252  VAL A 257 -1  O  TYR A 255   N  VAL A 202           
SHEET    4 AA1 4 VAL A 233  LEU A 235 -1  N  SER A 234   O  SER A 256           
SHEET    1 AA2 6 ILE A 298  GLN A 300  0                                        
SHEET    2 AA2 6 HIS A 289  PHE A 292 -1  N  MET A 291   O  LEU A 299           
SHEET    3 AA2 6 ALA A 378  PRO A 385 -1  O  ILE A 379   N  PHE A 292           
SHEET    4 AA2 6 MET A 364  ILE A 373 -1  N  ILE A 371   O  LEU A 380           
SHEET    5 AA2 6 PHE A 346  VAL A 350 -1  N  VAL A 350   O  MET A 364           
SHEET    6 AA2 6 PHE A 324  ILE A 326 -1  N  GLU A 325   O  ARG A 349           
SHEET    1 AA3 3 LYS A 475  MET A 482  0                                        
SHEET    2 AA3 3 HIS A 578  ALA A 584 -1  O  GLY A 580   N  VAL A 480           
SHEET    3 AA3 3 LEU A 596  PHE A 597 -1  O  PHE A 597   N  PHE A 583           
SHEET    1 AA4 5 ASP A 486  ILE A 487  0                                        
SHEET    2 AA4 5 MET A 573  ILE A 575 -1  O  ARG A 574   N  ASP A 486           
SHEET    3 AA4 5 LYS A 615  VAL A 618  1  O  ASN A 617   N  ILE A 575           
SHEET    4 AA4 5 HIS A 655  LEU A 657 -1  O  HIS A 655   N  VAL A 618           
SHEET    5 AA4 5 PHE A 634  PRO A 636 -1  N  THR A 635   O  PHE A 656           
SHEET    1 AA5 2 TYR A 523  VAL A 525  0                                        
SHEET    2 AA5 2 CYS A 533  ALA A 535 -1  O  ALA A 535   N  TYR A 523           
SHEET    1 AA6 4 THR B 123  ASP B 124  0                                        
SHEET    2 AA6 4 LEU B 131  TYR B 135 -1  O  ILE B 132   N  THR B 123           
SHEET    3 AA6 4 THR B 177  GLU B 183 -1  O  THR B 177   N  TYR B 135           
SHEET    4 AA6 4 ILE B 162  GLN B 168 -1  N  ILE B 167   O  GLN B 178           
SHEET    1 AA7 5 VAL B 229  CYS B 232  0                                        
SHEET    2 AA7 5 HIS B 220  ASP B 224 -1  N  ILE B 222   O  THR B 230           
SHEET    3 AA7 5 SER B 318  PRO B 325 -1  O  PHE B 321   N  ILE B 221           
SHEET    4 AA7 5 ARG B 305  LEU B 313 -1  N  ILE B 311   O  LEU B 320           
SHEET    5 AA7 5 PHE B 276  ARG B 279 -1  N  PHE B 276   O  GLY B 308           
SHEET    1 AA8 5 TYR B 470  LYS B 471  0                                        
SHEET    2 AA8 5 TYR B 479  SER B 483 -1  O  VAL B 482   N  TYR B 470           
SHEET    3 AA8 5 LYS B 415  SER B 425 -1  N  THR B 421   O  SER B 483           
SHEET    4 AA8 5 ILE B 521  ILE B 533 -1  O  VAL B 528   N  TYR B 417           
SHEET    5 AA8 5 ARG B 539  PHE B 543 -1  O  ARG B 539   N  ILE B 533           
SHEET    1 AA9 7 TYR B 470  LYS B 471  0                                        
SHEET    2 AA9 7 TYR B 479  SER B 483 -1  O  VAL B 482   N  TYR B 470           
SHEET    3 AA9 7 LYS B 415  SER B 425 -1  N  THR B 421   O  SER B 483           
SHEET    4 AA9 7 ILE B 521  ILE B 533 -1  O  VAL B 528   N  TYR B 417           
SHEET    5 AA9 7 ILE B 562  SER B 565  1  O  ASN B 563   N  ILE B 521           
SHEET    6 AA9 7 MET B 599  ARG B 606 -1  O  TRP B 602   N  VAL B 564           
SHEET    7 AA9 7 PHE B 582  VAL B 590 -1  N  VAL B 590   O  MET B 599           
SHEET    1 AB1 2 GLN B 511  VAL B 512  0                                        
SHEET    2 AB1 2 GLU B 515  SER B 516 -1  O  GLU B 515   N  VAL B 512           
CISPEP   1 THR A  328    PRO A  329          0       -14.11                     
CISPEP   2 ARG B  258    PRO B  259          0       -10.41                     
SITE     1 AC1 15 MET B   1  TYR B   2  PHE B  74  LEU B  87                    
SITE     2 AC1 15 LEU B 101  HIS B 105  LEU B 108  MET B 115                    
SITE     3 AC1 15 ARG B 116  PRO B 118  PHE B 120  SER B 137                    
SITE     4 AC1 15 ARG B 139  LEU B 142  ILE B 149                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           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 LINES ARE NOT SHOWN.)
END                                                                             
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