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Database: PDB
Entry: 6OIK
LinkDB: 6OIK
Original site: 6OIK 
HEADER    SIGNALING PROTEIN                       09-APR-19   6OIK              
TITLE     MUSCARINIC ACETYLCHOLINE RECEPTOR 2-GO COMPLEX                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M2,MUSCARINIC            
COMPND   3 ACETYLCHOLINE RECEPTOR M2;                                           
COMPND   4 CHAIN: R;                                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA;     
COMPND   9 CHAIN: A;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT  
COMPND  14 BETA-1;                                                              
COMPND  15 CHAIN: B;                                                            
COMPND  16 SYNONYM: TRANSDUCIN BETA CHAIN 1;                                    
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT  
COMPND  20 GAMMA-2;                                                             
COMPND  21 CHAIN: G;                                                            
COMPND  22 SYNONYM: G GAMMA-I;                                                  
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: ANTIBODY FRAGMENT;                                         
COMPND  26 CHAIN: H;                                                            
COMPND  27 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: CHRM2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: GNAO1;                                                         
SOURCE  14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: GNB1;                                                          
SOURCE  22 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  23 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 GENE: GNG2;                                                          
SOURCE  30 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  31 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  35 ORGANISM_COMMON: MOUSE;                                              
SOURCE  36 ORGANISM_TAXID: 10090;                                               
SOURCE  37 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  38 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  39 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    G-PROTEIN COUPLED RECEPTOR-G-PROTEIN COMPLEX, NEUROTRANSMITTER        
KEYWDS   2 RECEPTOR, SIGNALING PROTEIN                                          
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.MAEDA,Q.QIANHUI,G.SKINIOTIS,B.KOBILKA                               
REVDAT   3   29-MAY-19 6OIK    1       JRNL                                     
REVDAT   2   22-MAY-19 6OIK    1       JRNL                                     
REVDAT   1   08-MAY-19 6OIK    0                                                
JRNL        AUTH   S.MAEDA,Q.QU,M.J.ROBERTSON,G.SKINIOTIS,B.K.KOBILKA           
JRNL        TITL   STRUCTURES OF THE M1 AND M2 MUSCARINIC ACETYLCHOLINE         
JRNL        TITL 2 RECEPTOR/G-PROTEIN COMPLEXES.                                
JRNL        REF    SCIENCE                       V. 364   552 2019              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   31073061                                                     
JRNL        DOI    10.1126/SCIENCE.AAW5188                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 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)  : 3.600                          
REMARK   3   NUMBER OF PARTICLES               : 261730                         
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 6OIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238783.                                   
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                 : MUSCARINIC ACETYLCHOLINE          
REMARK 245                                    RECEPTOR 2 IN COMPLEX WITH        
REMARK 245                                    HETEROTRIMERIC GOA PROTEIN;       
REMARK 245                                    MUSCARINIC ACETYLCHOLINE          
REMARK 245                                    RECEPTOR M2; GUANINE NUCLEOTIDE-  
REMARK 245                                    BINDING PROTEIN G(O) SUBUNIT      
REMARK 245                                    ALPHA, GUANINE NUCLEOTIDE-        
REMARK 245                                    BINDING PROTEIN G(I)/G(S)/G(T)    
REMARK 245                                    SUBUNIT BETA-1, GUANINE           
REMARK 245                                    NUCLEOTIDE-BINDING PROTEIN G(I)/  
REMARK 245                                    G(S)/G(O) SUBUNIT GAMMA-2,        
REMARK 245                                    ANTIBODY FRAGMENT                 
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : UNSPECIFIED                       
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 SUMMIT (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)  : 7.00                           
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, A, B, G, H                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP R    -4                                                      
REMARK 465     TYR R    -3                                                      
REMARK 465     LYS R    -2                                                      
REMARK 465     ASP R    -1                                                      
REMARK 465     ASP R     0                                                      
REMARK 465     ASP R     1                                                      
REMARK 465     ASP R     2                                                      
REMARK 465     ALA R     3                                                      
REMARK 465     SER R     4                                                      
REMARK 465     THR R     5                                                      
REMARK 465     ASP R     6                                                      
REMARK 465     SER R     7                                                      
REMARK 465     SER R     8                                                      
REMARK 465     ASP R     9                                                      
REMARK 465     ASN R    10                                                      
REMARK 465     SER R    11                                                      
REMARK 465     LEU R    12                                                      
REMARK 465     ALA R    13                                                      
REMARK 465     LEU R    14                                                      
REMARK 465     THR R    15                                                      
REMARK 465     SER R    16                                                      
REMARK 465     PRO R    17                                                      
REMARK 465     TYR R    18                                                      
REMARK 465     LYS R    19                                                      
REMARK 465     LYS R   346                                                      
REMARK 465     ASP R   347                                                      
REMARK 465     LYS R   348                                                      
REMARK 465     LYS R   349                                                      
REMARK 465     GLU R   350                                                      
REMARK 465     PRO R   351                                                      
REMARK 465     VAL R   352                                                      
REMARK 465     ALA R   353                                                      
REMARK 465     ASN R   354                                                      
REMARK 465     GLN R   355                                                      
REMARK 465     ASP R   356                                                      
REMARK 465     PRO R   357                                                      
REMARK 465     VAL R   358                                                      
REMARK 465     SER R   359                                                      
REMARK 465     ILE R   360                                                      
REMARK 465     VAL R   361                                                      
REMARK 465     ALA R   362                                                      
REMARK 465     ARG R   363                                                      
REMARK 465     LYS R   364                                                      
REMARK 465     ILE R   365                                                      
REMARK 465     VAL R   366                                                      
REMARK 465     LYS R   367                                                      
REMARK 465     MET R   368                                                      
REMARK 465     THR R   369                                                      
REMARK 465     LYS R   370                                                      
REMARK 465     GLN R   371                                                      
REMARK 465     PRO R   372                                                      
REMARK 465     ALA R   373                                                      
REMARK 465     LYS R   374                                                      
REMARK 465     LYS R   375                                                      
REMARK 465     LYS R   376                                                      
REMARK 465     PRO R   377                                                      
REMARK 465     PRO R   378                                                      
REMARK 465     HIS R   458                                                      
REMARK 465     TYR R   459                                                      
REMARK 465     LYS R   460                                                      
REMARK 465     ASN R   461                                                      
REMARK 465     ILE R   462                                                      
REMARK 465     GLY R   463                                                      
REMARK 465     ALA R   464                                                      
REMARK 465     THR R   465                                                      
REMARK 465     ARG R   466                                                      
REMARK 465     PRO R   467                                                      
REMARK 465     ALA R   468                                                      
REMARK 465     GLY R   469                                                      
REMARK 465     LEU R   470                                                      
REMARK 465     GLU R   471                                                      
REMARK 465     VAL R   472                                                      
REMARK 465     LEU R   473                                                      
REMARK 465     PHE R   474                                                      
REMARK 465     GLN R   475                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     CYS A     3                                                      
REMARK 465     ILE A    56                                                      
REMARK 465     HIS A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     ASP A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     VAL A    66                                                      
REMARK 465     LYS A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     TYR A    69                                                      
REMARK 465     LYS A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     VAL A    72                                                      
REMARK 465     VAL A    73                                                      
REMARK 465     TYR A    74                                                      
REMARK 465     SER A    75                                                      
REMARK 465     ASN A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     ILE A    78                                                      
REMARK 465     GLN A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     LEU A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     ALA A    83                                                      
REMARK 465     ILE A    84                                                      
REMARK 465     VAL A    85                                                      
REMARK 465     ARG A    86                                                      
REMARK 465     ALA A    87                                                      
REMARK 465     MET A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     THR A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     ILE A    93                                                      
REMARK 465     GLU A    94                                                      
REMARK 465     TYR A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     LYS A    98                                                      
REMARK 465     GLU A    99                                                      
REMARK 465     ARG A   100                                                      
REMARK 465     LYS A   101                                                      
REMARK 465     ALA A   102                                                      
REMARK 465     ASP A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     LYS A   105                                                      
REMARK 465     MET A   106                                                      
REMARK 465     VAL A   107                                                      
REMARK 465     CYS A   108                                                      
REMARK 465     ASP A   109                                                      
REMARK 465     VAL A   110                                                      
REMARK 465     VAL A   111                                                      
REMARK 465     SER A   112                                                      
REMARK 465     ARG A   113                                                      
REMARK 465     MET A   114                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     ASP A   116                                                      
REMARK 465     THR A   117                                                      
REMARK 465     GLU A   118                                                      
REMARK 465     PRO A   119                                                      
REMARK 465     PHE A   120                                                      
REMARK 465     SER A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     GLU A   123                                                      
REMARK 465     LEU A   124                                                      
REMARK 465     LEU A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     ALA A   127                                                      
REMARK 465     MET A   128                                                      
REMARK 465     MET A   129                                                      
REMARK 465     ARG A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     TRP A   132                                                      
REMARK 465     GLY A   133                                                      
REMARK 465     ASP A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     ILE A   137                                                      
REMARK 465     GLN A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     CYS A   140                                                      
REMARK 465     PHE A   141                                                      
REMARK 465     ASN A   142                                                      
REMARK 465     ARG A   143                                                      
REMARK 465     SER A   144                                                      
REMARK 465     ARG A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     TYR A   147                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     ASN A   150                                                      
REMARK 465     ASP A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     LYS A   154                                                      
REMARK 465     TYR A   155                                                      
REMARK 465     TYR A   156                                                      
REMARK 465     LEU A   157                                                      
REMARK 465     ASP A   158                                                      
REMARK 465     SER A   159                                                      
REMARK 465     LEU A   160                                                      
REMARK 465     ASP A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     ILE A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     ALA A   166                                                      
REMARK 465     ASP A   167                                                      
REMARK 465     TYR A   168                                                      
REMARK 465     GLN A   169                                                      
REMARK 465     PRO A   170                                                      
REMARK 465     THR A   171                                                      
REMARK 465     GLU A   172                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     ASP A   174                                                      
REMARK 465     ILE A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     ARG A   177                                                      
REMARK 465     THR A   178                                                      
REMARK 465     ARG A   179                                                      
REMARK 465     VAL A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     VAL A   234                                                      
REMARK 465     LEU A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     ASP A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     THR A   240                                                      
REMARK 465     THR A   241                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
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     CYS G    68                                                      
REMARK 465     ALA G    69                                                      
REMARK 465     ILE G    70                                                      
REMARK 465     LEU G    71                                                      
REMARK 465     GLY H   123                                                      
REMARK 465     GLY H   124                                                      
REMARK 465     GLY H   125                                                      
REMARK 465     SER H   126                                                      
REMARK 465     GLY H   127                                                      
REMARK 465     GLY H   128                                                      
REMARK 465     GLY H   129                                                      
REMARK 465     GLY H   130                                                      
REMARK 465     SER H   131                                                      
REMARK 465     GLY H   132                                                      
REMARK 465     GLY H   133                                                      
REMARK 465     GLY H   134                                                      
REMARK 465     GLY H   249                                                      
REMARK 465     SER H   250                                                      
REMARK 465     LEU H   251                                                      
REMARK 465     GLU H   252                                                      
REMARK 465     VAL H   253                                                      
REMARK 465     LEU H   254                                                      
REMARK 465     PHE H   255                                                      
REMARK 465     GLN H   256                                                      
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     THR R  20    OG1  CG2                                            
REMARK 470     PHE R  21    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU R  22    CG   CD   OE1  OE2                                  
REMARK 470     VAL R  23    CG1  CG2                                            
REMARK 470     ILE R  26    CG1  CG2  CD1                                       
REMARK 470     LEU R  28    CG   CD1  CD2                                       
REMARK 470     SER R  32    OG                                                  
REMARK 470     ILE R  42    CG1  CG2  CD1                                       
REMARK 470     LYS R  49    CG   CD   CE   NZ                                   
REMARK 470     VAL R  50    CG1  CG2                                            
REMARK 470     ARG R  52    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN R  55    CG   CD   OE1  NE2                                  
REMARK 470     CYS R  67    SG                                                  
REMARK 470     LEU R  70    CG   CD1  CD2                                       
REMARK 470     VAL R  74    CG1  CG2                                            
REMARK 470     LEU R  91    CG   CD1  CD2                                       
REMARK 470     ASP R  97    CG   OD1  OD2                                       
REMARK 470     LEU R  98    CG   CD1  CD2                                       
REMARK 470     LYS R 127    CG   CD   CE   NZ                                   
REMARK 470     THR R 136    OG1  CG2                                            
REMARK 470     LYS R 138    CG   CD   CE   NZ                                   
REMARK 470     VAL R 149    CG1  CG2                                            
REMARK 470     VAL R 168    CG1  CG2                                            
REMARK 470     ASP R 173    CG   OD1  OD2                                       
REMARK 470     GLU R 175    CG   CD   OE1  OE2                                  
REMARK 470     PHE R 181    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE R 192    CG1  CG2  CD1                                       
REMARK 470     LEU R 197    CG   CD1  CD2                                       
REMARK 470     ARG R 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER R 380    OG                                                  
REMARK 470     GLU R 382    CG   CD   OE1  OE2                                  
REMARK 470     THR R 420    OG1  CG2                                            
REMARK 470     VAL R 421    CG1  CG2                                            
REMARK 470     ILE R 424    CG1  CG2  CD1                                       
REMARK 470     LYS R 448    CG   CD   CE   NZ                                   
REMARK 470     LYS R 449    CG   CD   CE   NZ                                   
REMARK 470     LYS R 452    CG   CD   CE   NZ                                   
REMARK 470     LEU R 455    CG   CD1  CD2                                       
REMARK 470     MET R 456    CG   SD   CE                                        
REMARK 470     CYS R 457    SG                                                  
REMARK 470     GLU A  20    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  25    CG   CD   OE1  OE2                                  
REMARK 470     SER A  29    OG                                                  
REMARK 470     THR A 182    OG1  CG2                                            
REMARK 470     HIS A 196    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 229    OG                                                  
REMARK 470     MET A 249    CG   SD   CE                                        
REMARK 470     ASP A 262    CG   OD1  OD2                                       
REMARK 470     LYS A 280    CG   CD   CE   NZ                                   
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 328    CG   OD1  OD2                                       
REMARK 470     THR A 329    OG1  CG2                                            
REMARK 470     GLU B   3    CG   CD   OE1  OE2                                  
REMARK 470     GLN B   6    CG   CD   OE1  NE2                                  
REMARK 470     ARG B   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B   9    CG   CD   OE1  NE2                                  
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     ASP B  20    CG   OD1  OD2                                       
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     CYS B  25    SG                                                  
REMARK 470     ASN B  36    CG   OD1  ND2                                       
REMARK 470     ARG B  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 130    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 172    CG   CD   OE1  OE2                                  
REMARK 470     MET B 217    CG   SD   CE                                        
REMARK 470     ASP B 228    CG   OD1  OD2                                       
REMARK 470     ASP B 312    CG   OD1  OD2                                       
REMARK 470     ILE G   9    CG1  CG2  CD1                                       
REMARK 470     ARG G  13    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G  14    CG   CD   CE   NZ                                   
REMARK 470     GLU G  17    CG   CD   OE1  OE2                                  
REMARK 470     ILE G  25    CG1  CG2  CD1                                       
REMARK 470     ARG G  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN H  13    CG   CD   OE1  NE2                                  
REMARK 470     GLU H  42    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  43    CG   CD   CE   NZ                                   
REMARK 470     GLU H  46    CG   CD   OE1  OE2                                  
REMARK 470     ASP H  62    CG   OD1  OD2                                       
REMARK 470     LYS H  65    CG   CD   CE   NZ                                   
REMARK 470     LYS H  76    CG   CD   CE   NZ                                   
REMARK 470     GLU H  89    CG   CD   OE1  OE2                                  
REMARK 470     SER H 121    OG                                                  
REMARK 470     SER H 136    OG                                                  
REMARK 470     GLU H 153    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 160    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 218    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 234    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 244    CG   CD   CE   NZ                                   
REMARK 470     LYS H 248    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR R   104     OH   TYR R   426              1.99            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS R 127       76.66   -111.42                                   
REMARK 500    PHE R 180       30.33    -97.96                                   
REMARK 500    ARG R 216       -5.54     69.97                                   
REMARK 500    ILE R 217      -64.36   -105.07                                   
REMARK 500    GLU A   8       -0.24   -141.04                                   
REMARK 500    LEU A 284       31.41    -92.93                                   
REMARK 500    CYS A 325       -9.13     80.22                                   
REMARK 500    THR B  87       34.76     37.72                                   
REMARK 500    LYS B 127       39.83    -98.40                                   
REMARK 500    ASP B 153     -159.29   -149.02                                   
REMARK 500    ASP B 163       42.09   -103.19                                   
REMARK 500    LEU B 190      142.12   -170.26                                   
REMARK 500    ALA B 248       -1.36     67.41                                   
REMARK 500    SER B 265      116.40   -162.21                                   
REMARK 500    ASP B 291       32.88    -92.60                                   
REMARK 500    SER B 334       -0.31     69.60                                   
REMARK 500    ASN H  77       61.74     37.25                                   
REMARK 500    SER H  99       56.74   -141.54                                   
REMARK 500    SER H 136       37.95    -99.54                                   
REMARK 500    LEU H 188      -60.31    -99.82                                   
REMARK 500    MET H 192      -18.89     73.66                                   
REMARK 500    SER H 193      -16.42   -142.88                                   
REMARK 500    HIS H 232       27.60   -141.50                                   
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 IXO R 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2CU R 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-20079   RELATED DB: EMDB                             
REMARK 900 GPCR COMPLEX 2                                                       
DBREF  6OIK R    3   359  UNP    P08172   ACM2_HUMAN       3    232             
DBREF  6OIK R  360   466  UNP    P08172   ACM2_HUMAN     360    466             
DBREF  6OIK A    1   354  UNP    P09471   GNAO_HUMAN       1    354             
DBREF  6OIK B    2   340  UNP    P62873   GBB1_HUMAN       2    340             
DBREF  6OIK G    1    71  UNP    P59768   GBG2_HUMAN       1     71             
DBREF  6OIK H    1   256  PDB    6OIK     6OIK             1    256             
SEQADV 6OIK ASP R   -4  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK TYR R   -3  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK LYS R   -2  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ASP R   -1  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ASP R    0  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ASP R    1  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ASP R    2  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ALA R    3  UNP  P08172    ASN     3 ENGINEERED MUTATION            
SEQADV 6OIK ASP R    6  UNP  P08172    ASN     6 ENGINEERED MUTATION            
SEQADV 6OIK ASP R    9  UNP  P08172    ASN     9 ENGINEERED MUTATION            
SEQADV 6OIK PRO R  467  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ALA R  468  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK GLY R  469  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK LEU R  470  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK GLU R  471  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK VAL R  472  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK LEU R  473  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK PHE R  474  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK GLN R  475  UNP  P08172              EXPRESSION TAG                 
SEQADV 6OIK ASP A    9  UNP  P09471    GLU     9 ENGINEERED MUTATION            
SEQADV 6OIK LYS A   10  UNP  P09471    ARG    10 ENGINEERED MUTATION            
SEQADV 6OIK VAL A   13  UNP  P09471    LEU    13 ENGINEERED MUTATION            
SEQADV 6OIK MET A   18  UNP  P09471    ALA    18 ENGINEERED MUTATION            
SEQADV 6OIK GLY B   -4  UNP  P62873              EXPRESSION TAG                 
SEQADV 6OIK PRO B   -3  UNP  P62873              EXPRESSION TAG                 
SEQADV 6OIK GLY B   -2  UNP  P62873              EXPRESSION TAG                 
SEQADV 6OIK SER B   -1  UNP  P62873              EXPRESSION TAG                 
SEQADV 6OIK SER B    0  UNP  P62873              EXPRESSION TAG                 
SEQADV 6OIK GLY B    1  UNP  P62873              EXPRESSION TAG                 
SEQRES   1 R  353  ASP TYR LYS ASP ASP ASP ASP ALA SER THR ASP SER SER          
SEQRES   2 R  353  ASP ASN SER LEU ALA LEU THR SER PRO TYR LYS THR PHE          
SEQRES   3 R  353  GLU VAL VAL PHE ILE VAL LEU VAL ALA GLY SER LEU SER          
SEQRES   4 R  353  LEU VAL THR ILE ILE GLY ASN ILE LEU VAL MET VAL SER          
SEQRES   5 R  353  ILE LYS VAL ASN ARG HIS LEU GLN THR VAL ASN ASN TYR          
SEQRES   6 R  353  PHE LEU PHE SER LEU ALA CYS ALA ASP LEU ILE ILE GLY          
SEQRES   7 R  353  VAL PHE SER MET ASN LEU TYR THR LEU TYR THR VAL ILE          
SEQRES   8 R  353  GLY TYR TRP PRO LEU GLY PRO VAL VAL CYS ASP LEU TRP          
SEQRES   9 R  353  LEU ALA LEU ASP TYR VAL VAL SER ASN ALA SER VAL MET          
SEQRES  10 R  353  ASN LEU LEU ILE ILE SER PHE ASP ARG TYR PHE CYS VAL          
SEQRES  11 R  353  THR LYS PRO LEU THR TYR PRO VAL LYS ARG THR THR LYS          
SEQRES  12 R  353  MET ALA GLY MET MET ILE ALA ALA ALA TRP VAL LEU SER          
SEQRES  13 R  353  PHE ILE LEU TRP ALA PRO ALA ILE LEU PHE TRP GLN PHE          
SEQRES  14 R  353  ILE VAL GLY VAL ARG THR VAL GLU ASP GLY GLU CYS TYR          
SEQRES  15 R  353  ILE GLN PHE PHE SER ASN ALA ALA VAL THR PHE GLY THR          
SEQRES  16 R  353  ALA ILE ALA ALA PHE TYR LEU PRO VAL ILE ILE MET THR          
SEQRES  17 R  353  VAL LEU TYR TRP HIS ILE SER ARG ALA SER LYS SER ARG          
SEQRES  18 R  353  ILE LYS LYS ASP LYS LYS GLU PRO VAL ALA ASN GLN ASP          
SEQRES  19 R  353  PRO VAL SER ILE VAL ALA ARG LYS ILE VAL LYS MET THR          
SEQRES  20 R  353  LYS GLN PRO ALA LYS LYS LYS PRO PRO PRO SER ARG GLU          
SEQRES  21 R  353  LYS LYS VAL THR ARG THR ILE LEU ALA ILE LEU LEU ALA          
SEQRES  22 R  353  PHE ILE ILE THR TRP ALA PRO TYR ASN VAL MET VAL LEU          
SEQRES  23 R  353  ILE ASN THR PHE CYS ALA PRO CYS ILE PRO ASN THR VAL          
SEQRES  24 R  353  TRP THR ILE GLY TYR TRP LEU CYS TYR ILE ASN SER THR          
SEQRES  25 R  353  ILE ASN PRO ALA CYS TYR ALA LEU CYS ASN ALA THR PHE          
SEQRES  26 R  353  LYS LYS THR PHE LYS HIS LEU LEU MET CYS HIS TYR LYS          
SEQRES  27 R  353  ASN ILE GLY ALA THR ARG PRO ALA GLY LEU GLU VAL LEU          
SEQRES  28 R  353  PHE GLN                                                      
SEQRES   1 A  354  MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL          
SEQRES   2 A  354  GLU ARG SER LYS MET ILE GLU LYS ASN LEU LYS GLU ASP          
SEQRES   3 A  354  GLY ILE SER ALA ALA LYS ASP VAL LYS LEU LEU LEU LEU          
SEQRES   4 A  354  GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN          
SEQRES   5 A  354  MET LYS ILE ILE HIS GLU ASP GLY PHE SER GLY GLU ASP          
SEQRES   6 A  354  VAL LYS GLN TYR LYS PRO VAL VAL TYR SER ASN THR ILE          
SEQRES   7 A  354  GLN SER LEU ALA ALA ILE VAL ARG ALA MET ASP THR LEU          
SEQRES   8 A  354  GLY ILE GLU TYR GLY ASP LYS GLU ARG LYS ALA ASP ALA          
SEQRES   9 A  354  LYS MET VAL CYS ASP VAL VAL SER ARG MET GLU ASP THR          
SEQRES  10 A  354  GLU PRO PHE SER ALA GLU LEU LEU SER ALA MET MET ARG          
SEQRES  11 A  354  LEU TRP GLY ASP SER GLY ILE GLN GLU CYS PHE ASN ARG          
SEQRES  12 A  354  SER ARG GLU TYR GLN LEU ASN ASP SER ALA LYS TYR TYR          
SEQRES  13 A  354  LEU ASP SER LEU ASP ARG ILE GLY ALA ALA ASP TYR GLN          
SEQRES  14 A  354  PRO THR GLU GLN ASP ILE LEU ARG THR ARG VAL LYS THR          
SEQRES  15 A  354  THR GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASN LEU          
SEQRES  16 A  354  HIS PHE ARG LEU PHE ASP VAL GLY GLY GLN ARG SER GLU          
SEQRES  17 A  354  ARG LYS LYS TRP ILE HIS CYS PHE GLU ASP VAL THR ALA          
SEQRES  18 A  354  ILE ILE PHE CYS VAL ALA LEU SER GLY TYR ASP GLN VAL          
SEQRES  19 A  354  LEU HIS GLU ASP GLU THR THR ASN ARG MET HIS GLU SER          
SEQRES  20 A  354  LEU MET LEU PHE ASP SER ILE CYS ASN ASN LYS PHE PHE          
SEQRES  21 A  354  ILE ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP          
SEQRES  22 A  354  LEU PHE GLY GLU LYS ILE LYS LYS SER PRO LEU THR ILE          
SEQRES  23 A  354  CYS PHE PRO GLU TYR THR GLY PRO ASN THR TYR GLU ASP          
SEQRES  24 A  354  ALA ALA ALA TYR ILE GLN ALA GLN PHE GLU SER LYS ASN          
SEQRES  25 A  354  ARG SER PRO ASN LYS GLU ILE TYR CYS HIS MET THR CYS          
SEQRES  26 A  354  ALA THR ASP THR ASN ASN ILE GLN VAL VAL PHE ASP ALA          
SEQRES  27 A  354  VAL THR ASP ILE ILE ILE ALA ASN ASN LEU ARG GLY CYS          
SEQRES  28 A  354  GLY LEU TYR                                                  
SEQRES   1 B  345  GLY PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG          
SEQRES   2 B  345  GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA          
SEQRES   3 B  345  ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR          
SEQRES   4 B  345  ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR          
SEQRES   5 B  345  ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA          
SEQRES   6 B  345  MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA          
SEQRES   7 B  345  SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR          
SEQRES   8 B  345  THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP          
SEQRES   9 B  345  VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL          
SEQRES  10 B  345  ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN          
SEQRES  11 B  345  LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU          
SEQRES  12 B  345  LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE          
SEQRES  13 B  345  LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR          
SEQRES  14 B  345  THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR          
SEQRES  15 B  345  THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU          
SEQRES  16 B  345  SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA          
SEQRES  17 B  345  CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY          
SEQRES  18 B  345  MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE          
SEQRES  19 B  345  ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA          
SEQRES  20 B  345  THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU          
SEQRES  21 B  345  ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN          
SEQRES  22 B  345  ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER          
SEQRES  23 B  345  GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS          
SEQRES  24 B  345  ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL          
SEQRES  25 B  345  LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL          
SEQRES  26 B  345  THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP          
SEQRES  27 B  345  SER PHE LEU LYS ILE TRP 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 CYS ALA ILE LEU                                      
SEQRES   1 H  256  ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  256  PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY          
SEQRES   3 H  256  PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN          
SEQRES   4 H  256  ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER          
SEQRES   5 H  256  SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS          
SEQRES   6 H  256  GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR          
SEQRES   7 H  256  LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  256  ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY          
SEQRES   9 H  256  SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU          
SEQRES  10 H  256  THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  11 H  256  SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA          
SEQRES  12 H  256  THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER          
SEQRES  13 H  256  ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN          
SEQRES  14 H  256  GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY          
SEQRES  15 H  256  GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU          
SEQRES  16 H  256  ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER          
SEQRES  17 H  256  GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA          
SEQRES  18 H  256  GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU          
SEQRES  19 H  256  TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU          
SEQRES  20 H  256  LYS GLY SER LEU GLU VAL LEU PHE GLN                          
HET    IXO  R 501      14                                                       
HET    2CU  R 502      29                                                       
HETNAM     IXO 4-(4,5-DIHYDRO-1,2-OXAZOL-3-YLOXY)-N,N,N-TRIMETHYLBUT-           
HETNAM   2 IXO  2-YN-1-AMINIUM                                                  
HETNAM     2CU 3-AMINO-5-CHLORO-N-CYCLOPROPYL-4-METHYL-6-[2-(4-                 
HETNAM   2 2CU  METHYLPIPERAZIN-1-YL)-2-OXOETHOXY]THIENO[2,3-                   
HETNAM   3 2CU  B]PYRIDINE-2-CARBOXAMIDE                                        
HETSYN     IXO IPEROXO                                                          
HETSYN     2CU LY2119620 POSITIVE ALLOSTERIC MODULATOR OF M2/M4                 
HETSYN   2 2CU  RECEPTOR                                                        
FORMUL   6  IXO    C10 H17 N2 O2 1+                                             
FORMUL   7  2CU    C19 H24 CL N5 O3 S                                           
HELIX    1 AA1 THR R   20  VAL R   50  1                                  31    
HELIX    2 AA2 THR R   56  GLY R   87  1                                  32    
HELIX    3 AA3 VAL R   94  LYS R  127  1                                  34    
HELIX    4 AA4 THR R  136  PHE R  161  1                                  26    
HELIX    5 AA5 PHE R  161  GLY R  167  1                                   7    
HELIX    6 AA6 ALA R  184  PHE R  195  1                                  12    
HELIX    7 AA7 PHE R  195  SER R  213  1                                  19    
HELIX    8 AA8 SER R  380  ASN R  410  1                                  31    
HELIX    9 AA9 ASN R  419  ILE R  431  1                                  13    
HELIX   10 AB1 ILE R  431  ASN R  436  1                                   6    
HELIX   11 AB2 ASN R  436  ALA R  441  1                                   6    
HELIX   12 AB3 ASN R  444  LEU R  454  1                                  11    
HELIX   13 AB4 ASP A    9  LYS A   32  1                                  24    
HELIX   14 AB5 GLY A   45  LYS A   51  1                                   7    
HELIX   15 AB6 GLU A  208  TRP A  212  5                                   5    
HELIX   16 AB7 ARG A  243  CYS A  255  1                                  13    
HELIX   17 AB8 LYS A  271  SER A  282  1                                  12    
HELIX   18 AB9 THR A  296  SER A  310  1                                  15    
HELIX   19 AC1 ASN A  330  CYS A  351  1                                  22    
HELIX   20 AC2 LEU B    4  CYS B   25  1                                  22    
HELIX   21 AC3 SER G    8  ALA G   23  1                                  16    
HELIX   22 AC4 LYS G   29  ALA G   45  1                                  17    
HELIX   23 AC5 LYS G   46  ASP G   48  5                                   3    
HELIX   24 AC6 ALA H   28  PHE H   32  5                                   5    
HELIX   25 AC7 SER H   53  GLY H   56  5                                   4    
HELIX   26 AC8 GLU H  220  VAL H  224  5                                   5    
SHEET    1 AA1 6 VAL A 186  THR A 191  0                                        
SHEET    2 AA1 6 HIS A 196  ASP A 201 -1  O  ASP A 201   N  VAL A 186           
SHEET    3 AA1 6 VAL A  34  GLY A  40  1  N  VAL A  34   O  ARG A 198           
SHEET    4 AA1 6 ALA A 221  ALA A 227  1  O  ILE A 223   N  LEU A  39           
SHEET    5 AA1 6 ILE A 265  ASN A 270  1  O  PHE A 268   N  PHE A 224           
SHEET    6 AA1 6 ILE A 319  MET A 323  1  O  TYR A 320   N  LEU A 267           
SHEET    1 AA2 4 THR B  47  ARG B  52  0                                        
SHEET    2 AA2 4 PHE B 335  TRP B 339 -1  O  ILE B 338   N  ARG B  48           
SHEET    3 AA2 4 VAL B 327  SER B 331 -1  N  THR B 329   O  LYS B 337           
SHEET    4 AA2 4 VAL B 315  VAL B 320 -1  N  GLY B 319   O  ALA B 328           
SHEET    1 AA3 4 ILE B  58  TRP B  63  0                                        
SHEET    2 AA3 4 LEU B  70  SER B  74 -1  O  VAL B  71   N  HIS B  62           
SHEET    3 AA3 4 LYS B  78  TRP B  82 -1  O  LYS B  78   N  SER B  74           
SHEET    4 AA3 4 LYS B  89  PRO B  94 -1  O  ILE B  93   N  LEU B  79           
SHEET    1 AA4 4 VAL B 100  TYR B 105  0                                        
SHEET    2 AA4 4 TYR B 111  GLY B 116 -1  O  GLY B 115   N  MET B 101           
SHEET    3 AA4 4 CYS B 121  ASN B 125 -1  O  TYR B 124   N  VAL B 112           
SHEET    4 AA4 4 ARG B 134  LEU B 139 -1  O  ARG B 137   N  ILE B 123           
SHEET    1 AA5 4 LEU B 146  PHE B 151  0                                        
SHEET    2 AA5 4 GLN B 156  SER B 161 -1  O  SER B 160   N  SER B 147           
SHEET    3 AA5 4 CYS B 166  ASP B 170 -1  O  TRP B 169   N  ILE B 157           
SHEET    4 AA5 4 GLN B 175  PHE B 180 -1  O  PHE B 180   N  CYS B 166           
SHEET    1 AA6 4 SER B 191  LEU B 192  0                                        
SHEET    2 AA6 4 LEU B 198  SER B 201 -1  O  VAL B 200   N  SER B 191           
SHEET    3 AA6 4 SER B 207  ASP B 212 -1  O  TRP B 211   N  PHE B 199           
SHEET    4 AA6 4 CYS B 218  THR B 223 -1  O  GLN B 220   N  LEU B 210           
SHEET    1 AA7 4 ILE B 229  PHE B 234  0                                        
SHEET    2 AA7 4 ALA B 240  SER B 245 -1  O  GLY B 244   N  ALA B 231           
SHEET    3 AA7 4 CYS B 250  ASP B 254 -1  O  PHE B 253   N  PHE B 241           
SHEET    4 AA7 4 GLU B 260  TYR B 264 -1  O  LEU B 261   N  LEU B 252           
SHEET    1 AA8 4 VAL B 276  PHE B 278  0                                        
SHEET    2 AA8 4 LEU B 284  ALA B 287 -1  O  LEU B 286   N  SER B 277           
SHEET    3 AA8 4 CYS B 294  ASP B 298 -1  O  TRP B 297   N  LEU B 285           
SHEET    4 AA8 4 ARG B 304  LEU B 308 -1  O  LEU B 308   N  CYS B 294           
SHEET    1 AA9 4 GLN H   3  SER H   7  0                                        
SHEET    2 AA9 4 SER H  17  SER H  25 -1  O  SER H  23   N  VAL H   5           
SHEET    3 AA9 4 THR H  78  THR H  84 -1  O  LEU H  79   N  CYS H  22           
SHEET    4 AA9 4 PHE H  68  ASP H  73 -1  N  SER H  71   O  PHE H  80           
SHEET    1 AB1 6 GLY H  10  VAL H  12  0                                        
SHEET    2 AB1 6 THR H 115  VAL H 119  1  N  THR H 118   O  GLY H  10           
SHEET    3 AB1 6 ALA H  92  ARG H  98 -1  N  ALA H  92   O  LEU H 117           
SHEET    4 AB1 6 MET H  34  GLN H  39 -1  N  HIS H  35   O  VAL H  97           
SHEET    5 AB1 6 LEU H  45  ILE H  51 -1  O  ILE H  51   N  MET H  34           
SHEET    6 AB1 6 ILE H  58  TYR H  60 -1  O  TYR H  59   N  TYR H  50           
SHEET    1 AB2 4 GLY H  10  VAL H  12  0                                        
SHEET    2 AB2 4 THR H 115  VAL H 119  1  N  THR H 118   O  GLY H  10           
SHEET    3 AB2 4 ALA H  92  ARG H  98 -1  N  ALA H  92   O  LEU H 117           
SHEET    4 AB2 4 PHE H 110  TRP H 111 -1  O  PHE H 110   N  ARG H  98           
SHEET    1 AB3 6 SER H 146  VAL H 149  0                                        
SHEET    2 AB3 6 THR H 243  LEU H 247  1  O  GLU H 246   N  VAL H 149           
SHEET    3 AB3 6 VAL H 226  GLN H 231 -1  N  TYR H 227   O  THR H 243           
SHEET    4 AB3 6 LEU H 174  GLN H 179 -1  N  PHE H 177   O  TYR H 228           
SHEET    5 AB3 6 PRO H 185  TYR H 190 -1  O  GLN H 186   N  LEU H 178           
SHEET    6 AB3 6 ASN H 194  LEU H 195 -1  O  ASN H 194   N  TYR H 190           
SHEET    1 AB4 3 VAL H 155  ARG H 160  0                                        
SHEET    2 AB4 3 ALA H 211  ILE H 216 -1  O  ILE H 216   N  VAL H 155           
SHEET    3 AB4 3 PHE H 203  SER H 208 -1  N  SER H 206   O  THR H 213           
SSBOND   1 CYS R   96    CYS R  176                          1555   1555  2.37  
SSBOND   2 CYS R  413    CYS R  416                          1555   1555  2.03  
SSBOND   3 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND   4 CYS H  159    CYS H  229                          1555   1555  2.04  
CISPEP   1 TYR H  235    PRO H  236          0         6.90                     
SITE     1 AC1 11 TYR R 104  ASN R 108  VAL R 111  ALA R 194                    
SITE     2 AC1 11 PHE R 195  TRP R 400  TYR R 403  ASN R 404                    
SITE     3 AC1 11 TYR R 426  CYS R 429  TYR R 430                               
SITE     1 AC2  7 TYR R  80  THR R  84  TYR R 177  PHE R 181                    
SITE     2 AC2  7 ASN R 419  TRP R 422  THR R 423                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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