GenomeNet

Database: PDB
Entry: 6G79
LinkDB: 6G79
Original site: 6G79 
HEADER    MEMBRANE PROTEIN                        05-APR-18   6G79              
TITLE     COUPLING SPECIFICITY OF HETEROTRIMERIC GO TO THE SEROTONIN 5-HT1B     
TITLE    2 RECEPTOR                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT  
COMPND   3 BETA-1;                                                              
COMPND   4 CHAIN: B;                                                            
COMPND   5 SYNONYM: TRANSDUCIN BETA CHAIN 1;                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT  
COMPND   9 GAMMA-2;                                                             
COMPND  10 CHAIN: G;                                                            
COMPND  11 SYNONYM: G GAMMA-I;                                                  
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA;     
COMPND  15 CHAIN: A;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: 5-HYDROXYTRYPTAMINE RECEPTOR 1B;                           
COMPND  19 CHAIN: S;                                                            
COMPND  20 SYNONYM: 5-HT1B,S12,SEROTONIN 1D BETA RECEPTOR,5-HT-1D-BETA,SEROTONIN
COMPND  21 RECEPTOR 1B;                                                         
COMPND  22 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: GNB1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: GNG2;                                                          
SOURCE  13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: GNAO1;                                                         
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: HTR1B, HTR1DB;                                                 
SOURCE  27 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    G-PROTEIN COUPLED RECEPTOR, 5-HT1B, MINI-GO, SEROTONIN, MEMBRANE      
KEYWDS   2 PROTEIN                                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.GARCIA-NAFRIA,R.NEHME,P.EDWARDS,C.G.TATE                            
REVDAT   3   19-SEP-18 6G79    1       REMARK DBREF  SEQADV HELIX               
REVDAT   3 2                   1       SHEET  ATOM                              
REVDAT   2   04-JUL-18 6G79    1       JRNL                                     
REVDAT   1   20-JUN-18 6G79    0                                                
JRNL        AUTH   J.GARCIA-NAFRIA,R.NEHME,P.C.EDWARDS,C.G.TATE                 
JRNL        TITL   CRYO-EM STRUCTURE OF THE SEROTONIN 5-HT1BRECEPTOR COUPLED TO 
JRNL        TITL 2 HETEROTRIMERIC GO.                                           
JRNL        REF    NATURE                        V. 558   620 2018              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   29925951                                                     
JRNL        DOI    10.1038/S41586-018-0241-9                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : RELION, EPU, GCTF, COOT, RELION,          
REMARK   3                            RELION, RELION, RELION, REFMAC            
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)  : 3.780                          
REMARK   3   NUMBER OF PARTICLES               : 730118                         
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 6G79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009500.                                   
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                 : SEROTONIN 5-HT1B RECEPTOR BOUND   
REMARK 245                                    TO A MINI-GO HETEROTRIMER; 5-     
REMARK 245                                    HT1B RECEPTOR; BETA SUBUNIT;      
REMARK 245                                    MINI-GO; GAMMA SUBUNIT            
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 2.20                              
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      : 5737                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON III (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                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 30.00                          
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G, A, S                            
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     SER B     2                                                      
REMARK 465     LYS B   127                                                      
REMARK 465     THR B   128                                                      
REMARK 465     ARG B   129                                                      
REMARK 465     GLU B   130                                                      
REMARK 465     GLY B   131                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     ASN G     4                                                      
REMARK 465     ASN G     5                                                      
REMARK 465     THR G     6                                                      
REMARK 465     GLU G    63                                                      
REMARK 465     LYS G    64                                                      
REMARK 465     LYS G    65                                                      
REMARK 465     PHE G    66                                                      
REMARK 465     PHE G    67                                                      
REMARK 465     SER G    68                                                      
REMARK 465     ALA G    69                                                      
REMARK 465     ILE G    70                                                      
REMARK 465     LEU G    71                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ILE A   171                                                      
REMARK 465     ILE A   172                                                      
REMARK 465     HIS A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     SER A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     GLU A   290                                                      
REMARK 465     TYR A   291                                                      
REMARK 465     THR A   292                                                      
REMARK 465     MET S    33                                                      
REMARK 465     SER S    34                                                      
REMARK 465     ALA S    35                                                      
REMARK 465     LYS S    36                                                      
REMARK 465     ASP S    37                                                      
REMARK 465     TYR S    38                                                      
REMARK 465     ILE S    39                                                      
REMARK 465     TYR S    40                                                      
REMARK 465     GLN S    41                                                      
REMARK 465     ASP S    42                                                      
REMARK 465     SER S    43                                                      
REMARK 465     ILE S    44                                                      
REMARK 465     ARG S   188                                                      
REMARK 465     GLN S   189                                                      
REMARK 465     ALA S   190                                                      
REMARK 465     LYS S   191                                                      
REMARK 465     ALA S   192                                                      
REMARK 465     GLU S   193                                                      
REMARK 465     GLU S   194                                                      
REMARK 465     GLU S   195                                                      
REMARK 465     VAL S   196                                                      
REMARK 465     LYS S   241                                                      
REMARK 465     GLN S   242                                                      
REMARK 465     THR S   243                                                      
REMARK 465     PRO S   244                                                      
REMARK 465     ASN S   245                                                      
REMARK 465     ARG S   246                                                      
REMARK 465     THR S   247                                                      
REMARK 465     GLY S   248                                                      
REMARK 465     LYS S   249                                                      
REMARK 465     ARG S   250                                                      
REMARK 465     LEU S   251                                                      
REMARK 465     THR S   252                                                      
REMARK 465     ARG S   253                                                      
REMARK 465     ALA S   254                                                      
REMARK 465     GLN S   255                                                      
REMARK 465     LEU S   256                                                      
REMARK 465     ILE S   257                                                      
REMARK 465     THR S   258                                                      
REMARK 465     ASP S   259                                                      
REMARK 465     SER S   260                                                      
REMARK 465     PRO S   261                                                      
REMARK 465     GLY S   262                                                      
REMARK 465     SER S   263                                                      
REMARK 465     THR S   264                                                      
REMARK 465     SER S   265                                                      
REMARK 465     SER S   266                                                      
REMARK 465     VAL S   267                                                      
REMARK 465     THR S   268                                                      
REMARK 465     SER S   269                                                      
REMARK 465     ILE S   270                                                      
REMARK 465     ASN S   271                                                      
REMARK 465     SER S   272                                                      
REMARK 465     ARG S   273                                                      
REMARK 465     VAL S   274                                                      
REMARK 465     PRO S   275                                                      
REMARK 465     ASP S   276                                                      
REMARK 465     VAL S   277                                                      
REMARK 465     PRO S   278                                                      
REMARK 465     SER S   279                                                      
REMARK 465     GLU S   280                                                      
REMARK 465     SER S   281                                                      
REMARK 465     GLY S   282                                                      
REMARK 465     SER S   283                                                      
REMARK 465     PRO S   284                                                      
REMARK 465     VAL S   285                                                      
REMARK 465     TYR S   286                                                      
REMARK 465     VAL S   287                                                      
REMARK 465     ASN S   288                                                      
REMARK 465     GLN S   289                                                      
REMARK 465     VAL S   290                                                      
REMARK 465     LYS S   291                                                      
REMARK 465     VAL S   292                                                      
REMARK 465     ARG S   293                                                      
REMARK 465     VAL S   294                                                      
REMARK 465     SER S   295                                                      
REMARK 465     ASP S   296                                                      
REMARK 465     ALA S   297                                                      
REMARK 465     LEU S   298                                                      
REMARK 465     LEU S   299                                                      
REMARK 465     GLU S   300                                                      
REMARK 465     LYS S   301                                                      
REMARK 465     LYS S   302                                                      
REMARK 465     LYS S   303                                                      
REMARK 465     LEU S   304                                                      
REMARK 465     ILE S   339                                                      
REMARK 465     CYS S   340                                                      
REMARK 465     LYS S   341                                                      
REMARK 465     ASP S   342                                                      
REMARK 465     ALA S   343                                                      
REMARK 465     CYS S   344                                                      
REMARK 465     PHE S   386                                                      
REMARK 465     LYS S   387                                                      
REMARK 465     CYS S   388                                                      
REMARK 465     THR S   389                                                      
REMARK 465     SER S   390                                                      
REMARK 465     GLU S   391                                                      
REMARK 465     ASN S   392                                                      
REMARK 465     LEU S   393                                                      
REMARK 465     TYR S   394                                                      
REMARK 465     PHE S   395                                                      
REMARK 465     GLN S   396                                                      
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 B   3    CG   CD   OE1  OE2                                  
REMARK 470     LEU B   4    CG   CD1  CD2                                       
REMARK 470     ASP B   5    CG   OD1  OD2                                       
REMARK 470     GLN B   6    CG   CD   OE1  NE2                                  
REMARK 470     LEU B   7    CG   CD1  CD2                                       
REMARK 470     ARG B   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B   9    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  10    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  12    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  13    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  14    CG   CD1  CD2                                       
REMARK 470     LYS B  15    CG   CD   CE   NZ                                   
REMARK 470     ASN B  16    CG   OD1  ND2                                       
REMARK 470     GLN B  17    CG   CD   OE1  NE2                                  
REMARK 470     ILE B  18    CG1  CG2  CD1                                       
REMARK 470     ARG B  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  20    CG   OD1  OD2                                       
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     ASP B  27    CG   OD1  OD2                                       
REMARK 470     GLN B  32    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  35    CG   OD1  ND2                                       
REMARK 470     ASN B  36    CG   OD1  ND2                                       
REMARK 470     ASP B  38    CG   OD1  OD2                                       
REMARK 470     ARG B  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  44    CG   CD   OE1  NE2                                  
REMARK 470     MET B  45    CG   SD   CE                                        
REMARK 470     ARG B  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  57    CG   CD   CE   NZ                                   
REMARK 470     THR B  65    OG1  CG2                                            
REMARK 470     ARG B  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  76    CG   OD1  OD2                                       
REMARK 470     ASP B  83    CG   OD1  OD2                                       
REMARK 470     ARG B  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 118    CG   OD1  OD2                                       
REMARK 470     ASN B 132    CG   OD1  ND2                                       
REMARK 470     ARG B 134    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 138    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 153    CG   OD1  OD2                                       
REMARK 470     ASP B 154    CG   OD1  OD2                                       
REMARK 470     ASN B 155    CG   OD1  ND2                                       
REMARK 470     ASP B 163    CG   OD1  OD2                                       
REMARK 470     ASP B 170    CG   OD1  OD2                                       
REMARK 470     GLU B 172    CG   CD   OE1  OE2                                  
REMARK 470     THR B 173    OG1  CG2                                            
REMARK 470     GLN B 175    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 186    CG   OD1  OD2                                       
REMARK 470     ASP B 195    CG   OD1  OD2                                       
REMARK 470     ASP B 205    CG   OD1  OD2                                       
REMARK 470     ASP B 212    CG   OD1  OD2                                       
REMARK 470     ARG B 214    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 215    CG   CD   OE1  OE2                                  
REMARK 470     MET B 217    CG   SD   CE                                        
REMARK 470     GLU B 226    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 228    CG   OD1  OD2                                       
REMARK 470     ASP B 246    CG   OD1  OD2                                       
REMARK 470     ASP B 247    CG   OD1  OD2                                       
REMARK 470     ARG B 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 254    CG   OD1  OD2                                       
REMARK 470     ARG B 256    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 260    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 268    CG   OD1  ND2                                       
REMARK 470     ILE B 270    CG1  CG2  CD1                                       
REMARK 470     LYS B 280    CG   CD   CE   NZ                                   
REMARK 470     ARG B 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 290    CG   OD1  OD2                                       
REMARK 470     PHE B 292    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     ARG B 304    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 312    CG   OD1  OD2                                       
REMARK 470     ASP B 322    CG   OD1  OD2                                       
REMARK 470     MET B 325    CG   SD   CE                                        
REMARK 470     ASP B 333    CG   OD1  OD2                                       
REMARK 470     LYS B 337    CE   NZ                                             
REMARK 470     ASN B 340    CG   OD1  ND2                                       
REMARK 470     SER G   8    OG                                                  
REMARK 470     GLN G  11    CG   CD   OE1  NE2                                  
REMARK 470     ARG G  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G  14    CG   CD   CE   NZ                                   
REMARK 470     LEU G  15    CG   CD1  CD2                                       
REMARK 470     VAL G  16    CG1  CG2                                            
REMARK 470     GLU G  17    CG   CD   OE1  OE2                                  
REMARK 470     LEU G  19    CG   CD1  CD2                                       
REMARK 470     LYS G  20    CG   CD   CE   NZ                                   
REMARK 470     MET G  21    CG   SD   CE                                        
REMARK 470     GLU G  22    CG   CD   OE1  OE2                                  
REMARK 470     ASN G  24    CG   OD1  ND2                                       
REMARK 470     ASP G  26    CG   OD1  OD2                                       
REMARK 470     ARG G  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G  29    CG   CD   CE   NZ                                   
REMARK 470     SER G  31    OG                                                  
REMARK 470     LYS G  32    CG   CD   CE   NZ                                   
REMARK 470     ASP G  36    CG   OD1  OD2                                       
REMARK 470     MET G  38    CG   SD   CE                                        
REMARK 470     CYS G  41    SG                                                  
REMARK 470     GLU G  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  46    CG   CD   CE   NZ                                   
REMARK 470     GLU G  47    CG   CD   OE1  OE2                                  
REMARK 470     THR G  52    OG1  CG2                                            
REMARK 470     VAL G  54    CG1  CG2                                            
REMARK 470     SER G  57    OG                                                  
REMARK 470     GLU G  58    CG   CD   OE1  OE2                                  
REMARK 470     LEU A   5    CG   CD1  CD2                                       
REMARK 470     GLU A   8    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  14    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     GLU A  20    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     ASP A  42    CG   OD1  OD2                                       
REMARK 470     ASN A  43    CG   OD1  ND2                                       
REMARK 470     LYS A  46    CG   CD   CE   NZ                                   
REMARK 470     THR A  48    OG1  CG2                                            
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     GLN A  52    CG   CD   OE1  NE2                                  
REMARK 470     MET A  53    CG   SD   CE                                        
REMARK 470     LYS A  54    CG   CD   CE   NZ                                   
REMARK 470     GLU A 187    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 192    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 193    CG   CD   CE   NZ                                   
REMARK 470     ASN A 194    CG   OD1  ND2                                       
REMARK 470     ASP A 201    CG   OD1  OD2                                       
REMARK 470     ARG A 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 208    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     GLU A 217    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 218    CG   OD1  OD2                                       
REMARK 470     ASP A 227    CG   OD1  OD2                                       
REMARK 470     ASP A 230    CG   OD1  OD2                                       
REMARK 470     ASN A 242    CG   OD1  ND2                                       
REMARK 470     ARG A 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 246    CG   CD   OE1  OE2                                  
REMARK 470     MET A 249    CG   SD   CE                                        
REMARK 470     ASP A 252    CG   OD1  OD2                                       
REMARK 470     ASN A 256    CG   OD1  ND2                                       
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     LYS A 272    CG   CD   CE   NZ                                   
REMARK 470     ASP A 273    CG   OD1  OD2                                       
REMARK 470     LEU A 274    CG   CD1  CD2                                       
REMARK 470     GLU A 277    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 278    CG   CD   CE   NZ                                   
REMARK 470     LYS A 280    CG   CD   CE   NZ                                   
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     LEU A 284    CG   CD1  CD2                                       
REMARK 470     THR A 285    OG1  CG2                                            
REMARK 470     PHE A 288    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 295    CG   OD1  ND2                                       
REMARK 470     THR A 296    OG1  CG2                                            
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 309    CG   CD   OE1  OE2                                  
REMARK 470     SER A 314    OG                                                  
REMARK 470     ASN A 316    CG   OD1  ND2                                       
REMARK 470     GLU A 318    CG   CD   OE1  OE2                                  
REMARK 470     CYS A 325    SG                                                  
REMARK 470     THR A 327    OG1  CG2                                            
REMARK 470     ASP A 328    CG   OD1  OD2                                       
REMARK 470     ASP A 337    CG   OD1  OD2                                       
REMARK 470     ARG A 349    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS S  49    CG   CD   CE   NZ                                   
REMARK 470     MET S  54    CG   SD   CE                                        
REMARK 470     THR S  60    OG1  CG2                                            
REMARK 470     LEU S  65    CG   CD1  CD2                                       
REMARK 470     ARG S  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG S  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS S  79    CG   CD   CE   NZ                                   
REMARK 470     MET S 103    CG   SD   CE                                        
REMARK 470     ILE S 105    CG1  CG2  CD1                                       
REMARK 470     MET S 108    CG   SD   CE                                        
REMARK 470     ARG S 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR S 116    OG1  CG2                                            
REMARK 470     LEU S 117    CG   CD1  CD2                                       
REMARK 470     GLN S 119    CG   CD   OE1  NE2                                  
REMARK 470     VAL S 120    CG1  CG2                                            
REMARK 470     ASP S 123    CG   OD1  OD2                                       
REMARK 470     ASP S 153    CG   OD1  OD2                                       
REMARK 470     SER S 158    OG                                                  
REMARK 470     GLU S 198    CG   CD   OE1  OE2                                  
REMARK 470     VAL S 200    CG1  CG2                                            
REMARK 470     ILE S 206    CG1  CG2  CD1                                       
REMARK 470     LEU S 207    CG   CD1  CD2                                       
REMARK 470     TYR S 208    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR S 211    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU S 222    CG   CD1  CD2                                       
REMARK 470     ARG S 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET S 305    CG   SD   CE                                        
REMARK 470     ARG S 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP S 345    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP S 345    CZ3  CH2                                            
REMARK 470     LEU S 348    CG   CD1  CD2                                       
REMARK 470     ASP S 352    CG   OD1  OD2                                       
REMARK 470     LEU S 360    CG   CD1  CD2                                       
REMARK 470     MET S 371    CG   SD   CE                                        
REMARK 470     GLU S 374    CG   CD   OE1  OE2                                  
REMARK 470     ASP S 375    CG   OD1  OD2                                       
REMARK 470     GLN S 378    CG   CD   OE1  NE2                                  
REMARK 470     LYS S 382    CG   CD   CE   NZ                                   
REMARK 470     ARG S 385    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B  26       83.92    -68.41                                   
REMARK 500    THR B  87       58.77     39.32                                   
REMARK 500    ASN B 110      -60.09   -126.66                                   
REMARK 500    THR B 164        5.87     80.74                                   
REMARK 500    SER B 201      117.47   -162.93                                   
REMARK 500    PRO B 236      -38.73    -37.97                                   
REMARK 500    SER B 334       45.95     77.31                                   
REMARK 500    HIS A 189       34.90   -141.34                                   
REMARK 500    SER A 207     -162.40   -108.99                                   
REMARK 500    ASP A 218       30.55    -95.70                                   
REMARK 500    ASP A 230      120.90    175.61                                   
REMARK 500    ASP A 262       51.94    -99.99                                   
REMARK 500    LEU A 284       49.83    -91.44                                   
REMARK 500    PHE A 288     -110.90     61.68                                   
REMARK 500    SER A 314      102.68   -162.30                                   
REMARK 500    LYS A 317       76.72   -162.67                                   
REMARK 500    ALA A 326      -89.46     57.37                                   
REMARK 500    THR A 327       52.47   -164.77                                   
REMARK 500    THR S 116       56.36   -157.13                                   
REMARK 500    LEU S 117       25.14   -155.05                                   
REMARK 500    ALA S 154      -74.37     62.64                                   
REMARK 500    PHE S 185       41.61   -146.03                                   
REMARK 500    ASP S 204      -63.13   -144.57                                   
REMARK 500    PHE S 217      -65.44   -158.54                                   
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 EP5 S 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4358   RELATED DB: EMDB                              
REMARK 900 COUPLING SPECIFICITY OF HETEROTRIMERIC GO TO THE SEROTONIN 5-HT1B    
REMARK 900 RECEPTOR                                                             
DBREF  6G79 B    2   340  UNP    P62873   GBB1_HUMAN       2    340             
DBREF  6G79 G    1    71  UNP    P59768   GBG2_HUMAN       1     71             
DBREF  6G79 A    4   173  UNP    P09471   GNAO_HUMAN       4     57             
DBREF1 6G79 A  182   354  UNP                  A0A0P7W0C8_9TELE                 
DBREF2 6G79 A     A0A0P7W0C8                        215         379             
DBREF  6G79 S   34   390  UNP    P28222   5HT1B_HUMAN     34    390             
SEQADV 6G79 SER G   68  UNP  P59768    CYS    68 CONFLICT                       
SEQADV 6G79 ASP A   42  UNP  P09471    GLY    42 CONFLICT                       
SEQADV 6G79 ASN A   43  UNP  P09471    GLU    43 CONFLICT                       
SEQADV 6G79 GLY A  174  UNP  P09471              LINKER                         
SEQADV 6G79 GLY A  175  UNP  P09471              LINKER                         
SEQADV 6G79 SER A  176  UNP  P09471              LINKER                         
SEQADV 6G79 GLY A  177  UNP  P09471              LINKER                         
SEQADV 6G79 GLY A  178  UNP  P09471              LINKER                         
SEQADV 6G79 SER A  179  UNP  P09471              LINKER                         
SEQADV 6G79 GLY A  180  UNP  P09471              LINKER                         
SEQADV 6G79 GLY A  181  UNP  P09471              LINKER                         
SEQADV 6G79 ASP A  227  UNP  A0A0P7W0C ALA   260 CONFLICT                       
SEQADV 6G79     A       UNP  A0A0P7W0C GLY   263 DELETION                       
SEQADV 6G79     A       UNP  A0A0P7W0C TYR   264 DELETION                       
SEQADV 6G79 TYR A  231  UNP  A0A0P7W0C GLN   266 CONFLICT                       
SEQADV 6G79 GLY A  276  UNP  A0A0P7W0C ALA   301 CONFLICT                       
SEQADV 6G79 PRO A  283  UNP  A0A0P7W0C ALA   308 CONFLICT                       
SEQADV 6G79 THR A  285  UNP  A0A0P7W0C SER   310 CONFLICT                       
SEQADV 6G79 ASN A  330  UNP  A0A0P7W0C GLY   355 CONFLICT                       
SEQADV 6G79 ALA A  332  UNP  A0A0P7W0C ILE   357 CONFLICT                       
SEQADV 6G79 ILE A  335  UNP  A0A0P7W0C VAL   360 CONFLICT                       
SEQADV 6G79 MET S   33  UNP  P28222              INITIATING METHIONINE          
SEQADV 6G79 TRP S  138  UNP  P28222    LEU   138 CONFLICT                       
SEQADV 6G79 GLU S  391  UNP  P28222              EXPRESSION TAG                 
SEQADV 6G79 ASN S  392  UNP  P28222              EXPRESSION TAG                 
SEQADV 6G79 LEU S  393  UNP  P28222              EXPRESSION TAG                 
SEQADV 6G79 TYR S  394  UNP  P28222              EXPRESSION TAG                 
SEQADV 6G79 PHE S  395  UNP  P28222              EXPRESSION TAG                 
SEQADV 6G79 GLN S  396  UNP  P28222              EXPRESSION TAG                 
SEQRES   1 B  339  SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU          
SEQRES   2 B  339  LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP          
SEQRES   3 B  339  ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL          
SEQRES   4 B  339  GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY          
SEQRES   5 B  339  HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP          
SEQRES   6 B  339  SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU          
SEQRES   7 B  339  ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA          
SEQRES   8 B  339  ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR          
SEQRES   9 B  339  ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP          
SEQRES  10 B  339  ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY          
SEQRES  11 B  339  ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY          
SEQRES  12 B  339  TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE          
SEQRES  13 B  339  VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP          
SEQRES  14 B  339  ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS          
SEQRES  15 B  339  THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR          
SEQRES  16 B  339  ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS          
SEQRES  17 B  339  LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE          
SEQRES  18 B  339  THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE          
SEQRES  19 B  339  PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA          
SEQRES  20 B  339  THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU          
SEQRES  21 B  339  MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR          
SEQRES  22 B  339  SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA          
SEQRES  23 B  339  GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU          
SEQRES  24 B  339  LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN          
SEQRES  25 B  339  ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA          
SEQRES  26 B  339  VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP          
SEQRES  27 B  339  ASN                                                          
SEQRES   1 G   71  MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG          
SEQRES   2 G   71  LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP          
SEQRES   3 G   71  ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA          
SEQRES   4 G   71  TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR          
SEQRES   5 G   71  PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS          
SEQRES   6 G   71  PHE PHE SER ALA ILE LEU                                      
SEQRES   1 A  225  THR LEU SER ALA GLU GLU ARG ALA ALA LEU GLU ARG SER          
SEQRES   2 A  225  LYS ALA ILE GLU LYS ASN LEU LYS GLU ASP GLY ILE SER          
SEQRES   3 A  225  ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU GLY ALA ASP          
SEQRES   4 A  225  ASN SER GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE          
SEQRES   5 A  225  ILE HIS GLY GLY SER GLY GLY SER GLY GLY THR THR GLY          
SEQRES   6 A  225  ILE VAL GLU THR HIS PHE THR PHE LYS ASN LEU HIS PHE          
SEQRES   7 A  225  ARG LEU PHE ASP VAL GLY GLY GLN ARG SER GLU ARG LYS          
SEQRES   8 A  225  LYS TRP ILE HIS CYS PHE GLU ASP VAL THR ALA ILE ILE          
SEQRES   9 A  225  PHE CYS VAL ASP LEU SER ASP TYR ASN ARG MET HIS GLU          
SEQRES  10 A  225  SER LEU MET LEU PHE ASP SER ILE CYS ASN ASN LYS PHE          
SEQRES  11 A  225  PHE ILE ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS          
SEQRES  12 A  225  ASP LEU PHE GLY GLU LYS ILE LYS LYS SER PRO LEU THR          
SEQRES  13 A  225  ILE CYS PHE PRO GLU TYR THR GLY PRO ASN THR TYR GLU          
SEQRES  14 A  225  ASP ALA ALA ALA TYR ILE GLN ALA GLN PHE GLU SER LYS          
SEQRES  15 A  225  ASN ARG SER PRO ASN LYS GLU ILE TYR CYS HIS MET THR          
SEQRES  16 A  225  CYS ALA THR ASP THR ASN ASN ALA GLN VAL ILE PHE ASP          
SEQRES  17 A  225  ALA VAL THR ASP ILE ILE ILE ALA ASN ASN LEU ARG GLY          
SEQRES  18 A  225  CYS GLY LEU TYR                                              
SEQRES   1 S  364  MET SER ALA LYS ASP TYR ILE TYR GLN ASP SER ILE SER          
SEQRES   2 S  364  LEU PRO TRP LYS VAL LEU LEU VAL MET LEU LEU ALA LEU          
SEQRES   3 S  364  ILE THR LEU ALA THR THR LEU SER ASN ALA PHE VAL ILE          
SEQRES   4 S  364  ALA THR VAL TYR ARG THR ARG LYS LEU HIS THR PRO ALA          
SEQRES   5 S  364  ASN TYR LEU ILE ALA SER LEU ALA VAL THR ASP LEU LEU          
SEQRES   6 S  364  VAL SER ILE LEU VAL MET PRO ILE SER THR MET TYR THR          
SEQRES   7 S  364  VAL THR GLY ARG TRP THR LEU GLY GLN VAL VAL CYS ASP          
SEQRES   8 S  364  PHE TRP LEU SER SER ASP ILE THR CYS CYS THR ALA SER          
SEQRES   9 S  364  ILE TRP HIS LEU CYS VAL ILE ALA LEU ASP ARG TYR TRP          
SEQRES  10 S  364  ALA ILE THR ASP ALA VAL GLU TYR SER ALA LYS ARG THR          
SEQRES  11 S  364  PRO LYS ARG ALA ALA VAL MET ILE ALA LEU VAL TRP VAL          
SEQRES  12 S  364  PHE SER ILE SER ILE SER LEU PRO PRO PHE PHE TRP ARG          
SEQRES  13 S  364  GLN ALA LYS ALA GLU GLU GLU VAL SER GLU CYS VAL VAL          
SEQRES  14 S  364  ASN THR ASP HIS ILE LEU TYR THR VAL TYR SER THR VAL          
SEQRES  15 S  364  GLY ALA PHE TYR PHE PRO THR LEU LEU LEU ILE ALA LEU          
SEQRES  16 S  364  TYR GLY ARG ILE TYR VAL GLU ALA ARG SER ARG ILE LEU          
SEQRES  17 S  364  LYS GLN THR PRO ASN ARG THR GLY LYS ARG LEU THR ARG          
SEQRES  18 S  364  ALA GLN LEU ILE THR ASP SER PRO GLY SER THR SER SER          
SEQRES  19 S  364  VAL THR SER ILE ASN SER ARG VAL PRO ASP VAL PRO SER          
SEQRES  20 S  364  GLU SER GLY SER PRO VAL TYR VAL ASN GLN VAL LYS VAL          
SEQRES  21 S  364  ARG VAL SER ASP ALA LEU LEU GLU LYS LYS LYS LEU MET          
SEQRES  22 S  364  ALA ALA ARG GLU ARG LYS ALA THR LYS THR LEU GLY ILE          
SEQRES  23 S  364  ILE LEU GLY ALA PHE ILE VAL CYS TRP LEU PRO PHE PHE          
SEQRES  24 S  364  ILE ILE SER LEU VAL MET PRO ILE CYS LYS ASP ALA CYS          
SEQRES  25 S  364  TRP PHE HIS LEU ALA ILE PHE ASP PHE PHE THR TRP LEU          
SEQRES  26 S  364  GLY TYR LEU ASN SER LEU ILE ASN PRO ILE ILE TYR THR          
SEQRES  27 S  364  MET SER ASN GLU ASP PHE LYS GLN ALA PHE HIS LYS LEU          
SEQRES  28 S  364  ILE ARG PHE LYS CYS THR SER GLU ASN LEU TYR PHE GLN          
HET    EP5  S 401      30                                                       
HETNAM     EP5 2-[5-[2-[4-(4-CYANOPHENYL)PIPERAZIN-1-YL]-2-                     
HETNAM   2 EP5  OXIDANYLIDENE-ETHOXY]-1~{H}-INDOL-3-YL]ETHYLAZANIUM             
FORMUL   5  EP5    C23 H26 N5 O2 1+                                             
HELIX    1 AA1 GLU B    3  ALA B   26  1                                  24    
HELIX    2 AA2 THR B   29  THR B   34  1                                   6    
HELIX    3 AA3 SER G    8  ASN G   24  1                                  17    
HELIX    4 AA4 LYS G   29  HIS G   44  1                                  16    
HELIX    5 AA5 SER A    6  ASP A   33  1                                  28    
HELIX    6 AA6 GLY A   45  LYS A   54  1                                  10    
HELIX    7 AA7 GLU A  208  HIS A  214  1                                   7    
HELIX    8 AA8 CYS A  215  GLU A  217  5                                   3    
HELIX    9 AA9 ASP A  230  ASN A  256  1                                  17    
HELIX   10 AB1 PHE A  259  THR A  263  5                                   5    
HELIX   11 AB2 LYS A  271  SER A  282  1                                  12    
HELIX   12 AB3 THR A  296  LYS A  311  1                                  16    
HELIX   13 AB4 ASN A  331  GLY A  352  1                                  22    
HELIX   14 AB5 LEU S   46  THR S   77  1                                  32    
HELIX   15 AB6 THR S   82  VAL S  102  1                                  21    
HELIX   16 AB7 VAL S  102  GLY S  113  1                                  12    
HELIX   17 AB8 LEU S  117  ASP S  153  1                                  37    
HELIX   18 AB9 ALA S  154  ARG S  161  1                                   8    
HELIX   19 AC1 THR S  162  LEU S  182  1                                  21    
HELIX   20 AC2 HIS S  205  ALA S  216  1                                  12    
HELIX   21 AC3 PHE S  217  LEU S  240  1                                  24    
HELIX   22 AC4 ALA S  306  MET S  337  1                                  32    
HELIX   23 AC5 LEU S  348  ASN S  373  1                                  26    
HELIX   24 AC6 ASN S  373  ILE S  384  1                                  12    
SHEET    1 AA1 4 THR B  47  LEU B  51  0                                        
SHEET    2 AA1 4 LEU B 336  TRP B 339 -1  O  ILE B 338   N  ARG B  48           
SHEET    3 AA1 4 VAL B 327  SER B 331 -1  N  VAL B 327   O  TRP B 339           
SHEET    4 AA1 4 VAL B 315  VAL B 320 -1  N  GLY B 319   O  ALA B 328           
SHEET    1 AA2 4 ILE B  58  TRP B  63  0                                        
SHEET    2 AA2 4 LEU B  69  SER B  74 -1  O  VAL B  71   N  HIS B  62           
SHEET    3 AA2 4 LYS B  78  ASP B  83 -1  O  TRP B  82   N  LEU B  70           
SHEET    4 AA2 4 ASN B  88  PRO B  94 -1  O  VAL B  90   N  ILE B  81           
SHEET    1 AA3 4 THR B 102  TYR B 105  0                                        
SHEET    2 AA3 4 TYR B 111  GLY B 115 -1  O  ALA B 113   N  ALA B 104           
SHEET    3 AA3 4 ILE B 120  ASN B 125 -1  O  TYR B 124   N  VAL B 112           
SHEET    4 AA3 4 VAL B 135  ALA B 140 -1  O  SER B 136   N  ILE B 123           
SHEET    1 AA4 4 LEU B 146  PHE B 151  0                                        
SHEET    2 AA4 4 GLN B 156  SER B 161 -1  O  SER B 160   N  CYS B 148           
SHEET    3 AA4 4 THR B 165  ASP B 170 -1  O  TRP B 169   N  ILE B 157           
SHEET    4 AA4 4 GLN B 175  THR B 181 -1  O  THR B 178   N  LEU B 168           
SHEET    1 AA5 4 SER B 191  LEU B 192  0                                        
SHEET    2 AA5 4 LEU B 198  VAL B 200 -1  O  VAL B 200   N  SER B 191           
SHEET    3 AA5 4 ALA B 208  ASP B 212 -1  O  TRP B 211   N  PHE B 199           
SHEET    4 AA5 4 CYS B 218  PHE B 222 -1  O  PHE B 222   N  ALA B 208           
SHEET    1 AA6 4 CYS B 233  PHE B 234  0                                        
SHEET    2 AA6 4 ALA B 240  THR B 243 -1  O  ALA B 242   N  CYS B 233           
SHEET    3 AA6 4 CYS B 250  ASP B 254 -1  O  PHE B 253   N  PHE B 241           
SHEET    4 AA6 4 GLN B 259  TYR B 264 -1  O  TYR B 264   N  CYS B 250           
SHEET    1 AA7 4 ILE B 273  PHE B 278  0                                        
SHEET    2 AA7 4 LEU B 284  TYR B 289 -1  O  GLY B 288   N  SER B 275           
SHEET    3 AA7 4 CYS B 294  ASP B 298 -1  O  TRP B 297   N  LEU B 285           
SHEET    4 AA7 4 ASP B 303  LEU B 308 -1  O  LEU B 308   N  CYS B 294           
SHEET    1 AA8 5 PHE A 197  PHE A 200  0                                        
SHEET    2 AA8 5 VAL A  34  GLY A  40  1  N  LEU A  36   O  ARG A 198           
SHEET    3 AA8 5 ALA A 221  ASP A 227  1  O  ILE A 223   N  LEU A  39           
SHEET    4 AA8 5 SER A 264  ASN A 270  1  O  PHE A 268   N  PHE A 224           
SHEET    5 AA8 5 ILE A 319  HIS A 322  1  O  HIS A 322   N  LEU A 269           
SSBOND   1 CYS S  122    CYS S  199                          1555   1555  2.03  
SITE     1 AC1 13 ASP S 129  ILE S 130  CYS S 133  THR S 134                    
SITE     2 AC1 13 VAL S 201  THR S 203  SER S 212  TRP S 327                    
SITE     3 AC1 13 PHE S 330  PHE S 331  SER S 334  MET S 337                    
SITE     4 AC1 13 PHE S 351                                                     
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      0.006289  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006289  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006289        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system