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Database: PDB
Entry: 6DDF
LinkDB: 6DDF
Original site: 6DDF 
HEADER    MEMBRANE PROTEIN                        10-MAY-18   6DDF              
TITLE     MU OPIOID RECEPTOR-GI PROTEIN COMPLEX                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN;               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT  
COMPND   8 BETA-1;                                                              
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: TRANSDUCIN BETA CHAIN 1;                                    
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT  
COMPND  14 GAMMA-2;                                                             
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: G GAMMA-I;                                                  
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: MU-TYPE OPIOID RECEPTOR;                                   
COMPND  20 CHAIN: R;                                                            
COMPND  21 SYNONYM: MOR-1;                                                      
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: DAMGO;                                                     
COMPND  25 CHAIN: D;                                                            
COMPND  26 ENGINEERED: YES;                                                     
COMPND  27 OTHER_DETAILS: ANALOGUE OF ENKEPHALIN                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GNAI1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: GNB1;                                                          
SOURCE  17 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  18 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;                                 
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 GENE: GNG2;                                                          
SOURCE  28 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  29 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  31 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE;                                 
SOURCE  32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  33 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  34 MOL_ID: 4;                                                           
SOURCE  35 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  36 ORGANISM_COMMON: MOUSE;                                              
SOURCE  37 ORGANISM_TAXID: 10090;                                               
SOURCE  38 GENE: OPRM1, MOR, OPRM;                                              
SOURCE  39 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  40 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  41 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  42 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  44 EXPRESSION_SYSTEM_PLASMID: PVL 1392;                                 
SOURCE  45 MOL_ID: 5;                                                           
SOURCE  46 SYNTHETIC: YES;                                                      
SOURCE  47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  48 ORGANISM_COMMON: HUMAN;                                              
SOURCE  49 ORGANISM_TAXID: 9606                                                 
KEYWDS    COMPLEX, TRANSMEMBRANE, MEMBRANE PROTEIN                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.KOEHL,H.HU,S.MAEDA,A.MANGLIK,B.K.KOBILKA,G.SKINIOTIS,W.I.WEIS       
REVDAT   4   11-DEC-19 6DDF    1       REMARK                                   
REVDAT   3   04-JUL-18 6DDF    1       JRNL                                     
REVDAT   2   27-JUN-18 6DDF    1       JRNL                                     
REVDAT   1   13-JUN-18 6DDF    0                                                
JRNL        AUTH   A.KOEHL,H.HU,S.MAEDA,Y.ZHANG,Q.QU,J.M.PAGGI,N.R.LATORRACA,   
JRNL        AUTH 2 D.HILGER,R.DAWSON,H.MATILE,G.F.X.SCHERTLER,S.GRANIER,        
JRNL        AUTH 3 W.I.WEIS,R.O.DROR,A.MANGLIK,G.SKINIOTIS,B.K.KOBILKA          
JRNL        TITL   STRUCTURE OF THE MU-OPIOID RECEPTOR-GIPROTEIN COMPLEX.       
JRNL        REF    NATURE                        V. 558   547 2018              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   29899455                                                     
JRNL        DOI    10.1038/S41586-018-0219-7                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : GCTF, RELION, FREALIGN                    
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)  : 3.500                          
REMARK   3   NUMBER OF PARTICLES               : 359406                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING ONLY            
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6DDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234073.                                   
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                 : TERNARY COMPLEX OF DAMGO          
REMARK 245                                    -ACTIVATED MU-TYPE OPIOID         
REMARK 245                                    RECEPTOR WITH HETEROTRIMERIC GI   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 7.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT 1 SECOND BEFORE PLUNGING     
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : SIGNALING COMPLEX FORMED BY       
REMARK 245  INCUBATION OF DAMGO-BOUND MU-TYPE OPIOID RECEPTOR AND               
REMARK 245  HETEROTRIMERIC GI. EXCESS GDP REMOVED BY ADDITION OF APYRASE.       
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 2642                           
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)              : 800.00                         
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)  : 37.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : 48076                          
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: A, B, C, R, D                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE DAMGO IS PEPTIDE-LIKE, A MEMBER OF  CLASS.                       
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: DAMGO                                                        
REMARK 400   CHAIN: D                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     CYS A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ILE A    56                                                      
REMARK 465     HIS A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     TYR A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     GLU A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     CYS A    66                                                      
REMARK 465     LYS A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     TYR A    69                                                      
REMARK 465     LYS A    70                                                      
REMARK 465     ALA 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     ILE A    81                                                      
REMARK 465     ILE A    82                                                      
REMARK 465     ALA A    83                                                      
REMARK 465     ILE A    84                                                      
REMARK 465     ILE A    85                                                      
REMARK 465     ARG A    86                                                      
REMARK 465     ALA A    87                                                      
REMARK 465     MET A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     ARG A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     LYS A    92                                                      
REMARK 465     ILE A    93                                                      
REMARK 465     ASP A    94                                                      
REMARK 465     PHE A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     ALA A    99                                                      
REMARK 465     ARG A   100                                                      
REMARK 465     ALA A   101                                                      
REMARK 465     ASP A   102                                                      
REMARK 465     ASP A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     ARG A   105                                                      
REMARK 465     GLN A   106                                                      
REMARK 465     LEU A   107                                                      
REMARK 465     PHE A   108                                                      
REMARK 465     VAL A   109                                                      
REMARK 465     LEU A   110                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     ALA A   114                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     GLY A   117                                                      
REMARK 465     PHE A   118                                                      
REMARK 465     MET A   119                                                      
REMARK 465     THR A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     GLU A   122                                                      
REMARK 465     LEU A   123                                                      
REMARK 465     ALA A   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     VAL A   126                                                      
REMARK 465     ILE A   127                                                      
REMARK 465     LYS A   128                                                      
REMARK 465     ARG A   129                                                      
REMARK 465     LEU A   130                                                      
REMARK 465     TRP A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     VAL A   136                                                      
REMARK 465     GLN A   137                                                      
REMARK 465     ALA A   138                                                      
REMARK 465     CYS A   139                                                      
REMARK 465     PHE A   140                                                      
REMARK 465     ASN A   141                                                      
REMARK 465     ARG A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     ARG A   144                                                      
REMARK 465     GLU A   145                                                      
REMARK 465     TYR A   146                                                      
REMARK 465     GLN A   147                                                      
REMARK 465     LEU A   148                                                      
REMARK 465     ASN A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     ALA A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     TYR A   154                                                      
REMARK 465     TYR A   155                                                      
REMARK 465     LEU A   156                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     ASP A   158                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     ARG A   161                                                      
REMARK 465     ILE A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     TYR A   167                                                      
REMARK 465     ILE A   168                                                      
REMARK 465     PRO A   169                                                      
REMARK 465     THR A   170                                                      
REMARK 465     GLN A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     ASP A   173                                                      
REMARK 465     VAL A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     ARG A   176                                                      
REMARK 465     THR A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     VAL A   179                                                      
REMARK 465     LYS A   180                                                      
REMARK 465     THR A   181                                                      
REMARK 465     LEU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     ASP A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     MET A   240                                                      
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     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     ASN C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     ARG C    62                                                      
REMARK 465     GLU C    63                                                      
REMARK 465     LYS C    64                                                      
REMARK 465     LYS C    65                                                      
REMARK 465     PHE C    66                                                      
REMARK 465     PHE C    67                                                      
REMARK 465     CYS C    68                                                      
REMARK 465     ALA C    69                                                      
REMARK 465     ILE C    70                                                      
REMARK 465     LEU C    71                                                      
REMARK 465     ASN R     3                                                      
REMARK 465     ILE R     4                                                      
REMARK 465     SER R     5                                                      
REMARK 465     ASP R     6                                                      
REMARK 465     CYS R     7                                                      
REMARK 465     SER R     8                                                      
REMARK 465     ASP R     9                                                      
REMARK 465     PRO R    10                                                      
REMARK 465     LEU R    11                                                      
REMARK 465     ALA R    12                                                      
REMARK 465     PRO R    13                                                      
REMARK 465     ALA R    14                                                      
REMARK 465     SER R    15                                                      
REMARK 465     CYS R    16                                                      
REMARK 465     SER R    17                                                      
REMARK 465     PRO R    18                                                      
REMARK 465     ALA R    19                                                      
REMARK 465     PRO R    20                                                      
REMARK 465     GLY R    21                                                      
REMARK 465     SER R    22                                                      
REMARK 465     TRP R    23                                                      
REMARK 465     LEU R    24                                                      
REMARK 465     ASN R    25                                                      
REMARK 465     LEU R    26                                                      
REMARK 465     SER R    27                                                      
REMARK 465     HIS R    28                                                      
REMARK 465     VAL R    29                                                      
REMARK 465     ASP R    30                                                      
REMARK 465     GLY R    31                                                      
REMARK 465     ASN R    32                                                      
REMARK 465     GLN R    33                                                      
REMARK 465     SER R    34                                                      
REMARK 465     ASP R    35                                                      
REMARK 465     PRO R    36                                                      
REMARK 465     CYS R    37                                                      
REMARK 465     GLY R    38                                                      
REMARK 465     PRO R    39                                                      
REMARK 465     ASN R    40                                                      
REMARK 465     ARG R    41                                                      
REMARK 465     THR R    42                                                      
REMARK 465     GLY R    43                                                      
REMARK 465     LEU R    44                                                      
REMARK 465     GLY R    45                                                      
REMARK 465     GLU R    46                                                      
REMARK 465     ASN R    47                                                      
REMARK 465     LEU R    48                                                      
REMARK 465     TYR R    49                                                      
REMARK 465     PHE R    50                                                      
REMARK 465     GLN R    51                                                      
REMARK 465     GLY R    52                                                      
REMARK 465     SER R    53                                                      
REMARK 465     HIS R    54                                                      
REMARK 465     SER R    55                                                      
REMARK 465     LEU R    56                                                      
REMARK 465     CYS R    57                                                      
REMARK 465     PRO R    58                                                      
REMARK 465     GLN R    59                                                      
REMARK 465     THR R    60                                                      
REMARK 465     GLY R    61                                                      
REMARK 465     SER R    62                                                      
REMARK 465     PRO R    63                                                      
REMARK 465     SER R    64                                                      
REMARK 465     CYS R   346                                                      
REMARK 465     PHE R   347                                                      
REMARK 465     ARG R   348                                                      
REMARK 465     GLU R   349                                                      
REMARK 465     PHE R   350                                                      
REMARK 465     CYS R   351                                                      
REMARK 465     ILE R   352                                                      
REMARK 465     PRO R   353                                                      
REMARK 465     THR R   354                                                      
REMARK 465     SER R   355                                                      
REMARK 465     SER R   356                                                      
REMARK 465     THR R   357                                                      
REMARK 465     ILE R   358                                                      
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     LEU A   5    CG   CD1  CD2                                       
REMARK 470     GLU A  28    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  43    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  55    CG1  CG2  CD1                                       
REMARK 470     GLU A 207    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 241    CG   OD1  ND2                                       
REMARK 470     LYS A 270    CG   CD   CE   NZ                                   
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 279    CG   CD   CE   NZ                                   
REMARK 470     LYS A 280    CG   CD   CE   NZ                                   
REMARK 470     ILE A 285    CG1  CG2  CD1                                       
REMARK 470     CYS A 305    SG                                                  
REMARK 470     GLU A 308    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 318    CG   CD   OE1  OE2                                  
REMARK 470     THR A 327    OG1  CG2                                            
REMARK 470     ASP A 337    CG   OD1  OD2                                       
REMARK 470     ASP A 350    CG   OD1  OD2                                       
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     CYS B  25    SG                                                  
REMARK 470     SER B  31    OG                                                  
REMARK 470     ARG B  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 130    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 214    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 217    CG   SD   CE                                        
REMARK 470     ASN B 237    CG   OD1  ND2                                       
REMARK 470     CYS B 271    SG                                                  
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     ASP B 312    CG   OD1  OD2                                       
REMARK 470     CYS B 317    SG                                                  
REMARK 470     ASP C  26    CG   OD1  OD2                                       
REMARK 470     ASP C  48    CG   OD1  OD2                                       
REMARK 470     SER C  57    OG                                                  
REMARK 470     GLU C  58    CG   CD   OE1  OE2                                  
REMARK 470     MET R  65    CG   SD   CE                                        
REMARK 470     VAL R  66    CG1  CG2                                            
REMARK 470     THR R  67    OG1  CG2                                            
REMARK 470     ILE R  69    CG1  CG2  CD1                                       
REMARK 470     MET R  72    CG   SD   CE                                        
REMARK 470     LEU R  74    CG   CD1  CD2                                       
REMARK 470     SER R  76    OG                                                  
REMARK 470     ILE R  77    CG1  CG2  CD1                                       
REMARK 470     VAL R  80    CG1  CG2                                            
REMARK 470     VAL R  81    CG1  CG2                                            
REMARK 470     VAL R  94    CG1  CG2                                            
REMARK 470     ARG R  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS R 100    CG   CD   CE   NZ                                   
REMARK 470     ASP R 114    CG   OD1  OD2                                       
REMARK 470     SER R 119    OG                                                  
REMARK 470     SER R 125    OG                                                  
REMARK 470     LEU R 129    CG   CD1  CD2                                       
REMARK 470     THR R 132    OG1  CG2                                            
REMARK 470     ASN R 137    CG   OD1  ND2                                       
REMARK 470     ILE R 138    CG1  CG2  CD1                                       
REMARK 470     LYS R 185    CG   CD   CE   NZ                                   
REMARK 470     ILE R 186    CG1  CG2  CD1                                       
REMARK 470     ILE R 193    CG1  CG2  CD1                                       
REMARK 470     MET R 203    CG   SD   CE                                        
REMARK 470     LYS R 209    CG   CD   CE   NZ                                   
REMARK 470     GLN R 212    CG   CD   OE1  NE2                                  
REMARK 470     ILE R 215    CG1  CG2  CD1                                       
REMARK 470     PHE R 221    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN R 230    CG   OD1  ND2                                       
REMARK 470     LEU R 246    CG   CD1  CD2                                       
REMARK 470     VAL R 291    CG1  CG2                                            
REMARK 470     THR R 294    OG1  CG2                                            
REMARK 470     LYS R 303    CG   CD   CE   NZ                                   
REMARK 470     THR R 307    OG1  CG2                                            
REMARK 470     PHE R 313    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER R 317    OG                                                  
REMARK 470     PHE R 343    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS R 344    CG   CD   CE   NZ                                   
REMARK 470     ARG R 345    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ETA D   5   C   -  N   -  CA  ANGL. DEV. = -15.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 229       37.70    -97.99                                   
REMARK 500    ASN A 294       51.78    -95.82                                   
REMARK 500    THR A 295     -167.16   -127.74                                   
REMARK 500    THR B  87       -2.47     67.33                                   
REMARK 500    CYS B 114     -168.88   -118.29                                   
REMARK 500    THR B 143      -31.76   -130.56                                   
REMARK 500    ASP B 163       50.20    -93.24                                   
REMARK 500    THR B 164       -8.74     72.05                                   
REMARK 500    LEU B 308       64.01   -101.37                                   
REMARK 500    GLU C  47       54.27    -91.55                                   
REMARK 500    THR R 132     -169.99   -103.41                                   
REMARK 500    PRO R 134       44.84    -82.67                                   
REMARK 500    THR R 207     -165.94    -79.81                                   
REMARK 500    SER R 214     -177.80   -179.92                                   
REMARK 500    PHE R 241      -35.52   -131.53                                   
REMARK 500    SER R 268       76.39     59.57                                   
REMARK 500    LEU R 339       55.61    -95.81                                   
REMARK 500    MEA D   4       84.02     58.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-7868   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 6DDE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EMD-7869   RELATED DB: EMDB                              
DBREF  6DDF A    1   354  UNP    P63096   GNAI1_HUMAN      1    354             
DBREF  6DDF B    2   340  UNP    P62873   GBB1_HUMAN       2    340             
DBREF  6DDF C    1    71  UNP    P59768   GBG2_HUMAN       1     71             
DBREF  6DDF R    3   358  UNP    P42866   OPRM_MOUSE       9    358             
DBREF  6DDF D    1     5  PDB    6DDF     6DDF             1      5             
SEQADV 6DDF PRO B   -3  UNP  P62873              EXPRESSION TAG                 
SEQADV 6DDF GLY B   -2  UNP  P62873              EXPRESSION TAG                 
SEQADV 6DDF SER B   -1  UNP  P62873              EXPRESSION TAG                 
SEQADV 6DDF SER B    0  UNP  P62873              EXPRESSION TAG                 
SEQADV 6DDF GLY B    1  UNP  P62873              EXPRESSION TAG                 
SEQADV 6DDF GLU R   46  UNP  P42866              INSERTION                      
SEQADV 6DDF ASN R   47  UNP  P42866              INSERTION                      
SEQADV 6DDF LEU R   48  UNP  P42866              INSERTION                      
SEQADV 6DDF TYR R   49  UNP  P42866              INSERTION                      
SEQADV 6DDF PHE R   50  UNP  P42866              INSERTION                      
SEQADV 6DDF GLN R   51  UNP  P42866              INSERTION                      
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 ASP ARG ASN LEU ARG GLU ASP          
SEQRES   3 A  354  GLY GLU LYS ALA ALA ARG GLU 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 ALA GLY TYR SER GLU GLU GLU          
SEQRES   6 A  354  CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE          
SEQRES   7 A  354  GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU          
SEQRES   8 A  354  LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA          
SEQRES   9 A  354  ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY          
SEQRES  10 A  354  PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU          
SEQRES  11 A  354  TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER          
SEQRES  12 A  354  ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU          
SEQRES  13 A  354  ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO          
SEQRES  14 A  354  THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR          
SEQRES  15 A  354  GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS          
SEQRES  16 A  354  PHE LYS MET PHE ASP VAL GLY GLY GLN ARG SER GLU ARG          
SEQRES  17 A  354  LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE          
SEQRES  18 A  354  ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU          
SEQRES  19 A  354  ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET          
SEQRES  20 A  354  LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR          
SEQRES  21 A  354  ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU          
SEQRES  22 A  354  PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS          
SEQRES  23 A  354  TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA          
SEQRES  24 A  354  ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS          
SEQRES  25 A  354  ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS          
SEQRES  26 A  354  ALA THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA          
SEQRES  27 A  354  VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS          
SEQRES  28 A  354  GLY LEU PHE                                                  
SEQRES   1 B  344  PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG GLN          
SEQRES   2 B  344  GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG          
SEQRES   3 B  344  LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN          
SEQRES   4 B  344  ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG          
SEQRES   5 B  344  ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET          
SEQRES   6 B  344  HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER          
SEQRES   7 B  344  GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR          
SEQRES   8 B  344  ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL          
SEQRES   9 B  344  MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA          
SEQRES  10 B  344  CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU          
SEQRES  11 B  344  LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU          
SEQRES  12 B  344  ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU          
SEQRES  13 B  344  ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR          
SEQRES  14 B  344  CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR          
SEQRES  15 B  344  THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER          
SEQRES  16 B  344  LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS          
SEQRES  17 B  344  ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET          
SEQRES  18 B  344  CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN          
SEQRES  19 B  344  ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR          
SEQRES  20 B  344  GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG          
SEQRES  21 B  344  ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE          
SEQRES  22 B  344  ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY          
SEQRES  23 B  344  ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN          
SEQRES  24 B  344  VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU          
SEQRES  25 B  344  ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR          
SEQRES  26 B  344  ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER          
SEQRES  27 B  344  PHE LEU LYS ILE TRP ASN                                      
SEQRES   1 C   71  MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG          
SEQRES   2 C   71  LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP          
SEQRES   3 C   71  ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA          
SEQRES   4 C   71  TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR          
SEQRES   5 C   71  PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS          
SEQRES   6 C   71  PHE PHE CYS ALA ILE LEU                                      
SEQRES   1 R  356  ASN ILE SER ASP CYS SER ASP PRO LEU ALA PRO ALA SER          
SEQRES   2 R  356  CYS SER PRO ALA PRO GLY SER TRP LEU ASN LEU SER HIS          
SEQRES   3 R  356  VAL ASP GLY ASN GLN SER ASP PRO CYS GLY PRO ASN ARG          
SEQRES   4 R  356  THR GLY LEU GLY GLU ASN LEU TYR PHE GLN GLY SER HIS          
SEQRES   5 R  356  SER LEU CYS PRO GLN THR GLY SER PRO SER MET VAL THR          
SEQRES   6 R  356  ALA ILE THR ILE MET ALA LEU TYR SER ILE VAL CYS VAL          
SEQRES   7 R  356  VAL GLY LEU PHE GLY ASN PHE LEU VAL MET TYR VAL ILE          
SEQRES   8 R  356  VAL ARG TYR THR LYS MET LYS THR ALA THR ASN ILE TYR          
SEQRES   9 R  356  ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU ALA THR SER          
SEQRES  10 R  356  THR LEU PRO PHE GLN SER VAL ASN TYR LEU MET GLY THR          
SEQRES  11 R  356  TRP PRO PHE GLY ASN ILE LEU CYS LYS ILE VAL ILE SER          
SEQRES  12 R  356  ILE ASP TYR TYR ASN MET PHE THR SER ILE PHE THR LEU          
SEQRES  13 R  356  CYS THR MET SER VAL ASP ARG TYR ILE ALA VAL CYS HIS          
SEQRES  14 R  356  PRO VAL LYS ALA LEU ASP PHE ARG THR PRO ARG ASN ALA          
SEQRES  15 R  356  LYS ILE VAL ASN VAL CYS ASN TRP ILE LEU SER SER ALA          
SEQRES  16 R  356  ILE GLY LEU PRO VAL MET PHE MET ALA THR THR LYS TYR          
SEQRES  17 R  356  ARG GLN GLY SER ILE ASP CYS THR LEU THR PHE SER HIS          
SEQRES  18 R  356  PRO THR TRP TYR TRP GLU ASN LEU LEU LYS ILE CYS VAL          
SEQRES  19 R  356  PHE ILE PHE ALA PHE ILE MET PRO VAL LEU ILE ILE THR          
SEQRES  20 R  356  VAL CYS TYR GLY LEU MET ILE LEU ARG LEU LYS SER VAL          
SEQRES  21 R  356  ARG MET LEU SER GLY SER LYS GLU LYS ASP ARG ASN LEU          
SEQRES  22 R  356  ARG ARG ILE THR ARG MET VAL LEU VAL VAL VAL ALA VAL          
SEQRES  23 R  356  PHE ILE VAL CYS TRP THR PRO ILE HIS ILE TYR VAL ILE          
SEQRES  24 R  356  ILE LYS ALA LEU ILE THR ILE PRO GLU THR THR PHE GLN          
SEQRES  25 R  356  THR VAL SER TRP HIS PHE CYS ILE ALA LEU GLY TYR THR          
SEQRES  26 R  356  ASN SER CYS LEU ASN PRO VAL LEU TYR ALA PHE LEU ASP          
SEQRES  27 R  356  GLU ASN PHE LYS ARG CYS PHE ARG GLU PHE CYS ILE PRO          
SEQRES  28 R  356  THR SER SER THR ILE                                          
SEQRES   1 D    5  TYR DAL GLY MEA ETA                                          
HET    DAL  D   2       5                                                       
HET    MEA  D   4      12                                                       
HET    ETA  D   5       4                                                       
HETNAM     DAL D-ALANINE                                                        
HETNAM     MEA N-METHYLPHENYLALANINE                                            
HETNAM     ETA ETHANOLAMINE                                                     
FORMUL   5  DAL    C3 H7 N O2                                                   
FORMUL   5  MEA    C10 H13 N O2                                                 
FORMUL   5  ETA    C2 H7 N O                                                    
HELIX    1 AA1 GLU A    8  ARG A   32  1                                  25    
HELIX    2 AA2 SER A   47  LYS A   51  5                                   5    
HELIX    3 AA3 GLU A  207  GLU A  216  5                                  10    
HELIX    4 AA4 ARG A  242  ASN A  255  1                                  14    
HELIX    5 AA5 LYS A  270  ILE A  278  1                                   9    
HELIX    6 AA6 GLU A  298  ASP A  309  1                                  12    
HELIX    7 AA7 LYS A  330  CYS A  351  1                                  22    
HELIX    8 AA8 GLN B    6  CYS B   25  1                                  20    
HELIX    9 AA9 GLN C   11  ASN C   24  1                                  14    
HELIX   10 AB1 ALA C   34  ALA C   43  1                                  10    
HELIX   11 AB2 THR R   70  THR R   97  1                                  28    
HELIX   12 AB3 THR R  101  LEU R  121  1                                  21    
HELIX   13 AB4 LEU R  121  MET R  130  1                                  10    
HELIX   14 AB5 GLY R  136  HIS R  171  1                                  36    
HELIX   15 AB6 LYS R  174  ARG R  179  1                                   6    
HELIX   16 AB7 ARG R  182  PHE R  204  1                                  23    
HELIX   17 AB8 GLU R  229  PHE R  241  1                                  13    
HELIX   18 AB9 PHE R  241  THR R  249  1                                   9    
HELIX   19 AC1 THR R  249  LYS R  260  1                                  12    
HELIX   20 AC2 SER R  268  THR R  294  1                                  27    
HELIX   21 AC3 THR R  294  ILE R  306  1                                  13    
HELIX   22 AC4 PHE R  313  TYR R  326  1                                  14    
HELIX   23 AC5 TYR R  326  TYR R  336  1                                  11    
SHEET    1 AA1 4 GLU A 186  THR A 190  0                                        
SHEET    2 AA1 4 HIS A 195  ASP A 200 -1  O  MET A 198   N  THR A 187           
SHEET    3 AA1 4 VAL A  34  GLY A  40  1  N  LEU A  36   O  LYS A 197           
SHEET    4 AA1 4 ALA A 220  CYS A 224  1  O  ILE A 222   N  LEU A  37           
SHEET    1 AA2 2 LEU A 266  PHE A 267  0                                        
SHEET    2 AA2 2 THR A 321  HIS A 322  1  O  HIS A 322   N  LEU A 266           
SHEET    1 AA3 2 THR B  47  LEU B  51  0                                        
SHEET    2 AA3 2 LEU B 336  TRP B 339 -1  O  LEU B 336   N  LEU B  51           
SHEET    1 AA4 4 HIS B  62  TRP B  63  0                                        
SHEET    2 AA4 4 LEU B  70  SER B  72 -1  O  VAL B  71   N  HIS B  62           
SHEET    3 AA4 4 LYS B  78  TRP B  82 -1  O  ILE B  80   N  SER B  72           
SHEET    4 AA4 4 LYS B  89  PRO B  94 -1  O  HIS B  91   N  ILE B  81           
SHEET    1 AA5 4 ALA B 104  TYR B 105  0                                        
SHEET    2 AA5 4 TYR B 111  ALA B 113 -1  O  ALA B 113   N  ALA B 104           
SHEET    3 AA5 4 CYS B 121  ASN B 125 -1  O  TYR B 124   N  VAL B 112           
SHEET    4 AA5 4 ARG B 134  LEU B 139 -1  O  ARG B 134   N  ASN B 125           
SHEET    1 AA6 4 LEU B 146  PHE B 151  0                                        
SHEET    2 AA6 4 GLN B 156  SER B 161 -1  O  VAL B 158   N  ARG B 150           
SHEET    3 AA6 4 THR B 165  ASP B 170 -1  O  TRP B 169   N  ILE B 157           
SHEET    4 AA6 4 GLN B 176  THR B 181 -1  O  THR B 178   N  LEU B 168           
SHEET    1 AA7 4 VAL B 187  SER B 191  0                                        
SHEET    2 AA7 4 LEU B 198  ALA B 203 -1  O  GLY B 202   N  MET B 188           
SHEET    3 AA7 4 SER B 207  ASP B 212 -1  O  LYS B 209   N  SER B 201           
SHEET    4 AA7 4 GLN B 220  THR B 223 -1  O  PHE B 222   N  ALA B 208           
SHEET    1 AA8 4 ILE B 229  PHE B 234  0                                        
SHEET    2 AA8 4 ALA B 240  SER B 245 -1  O  GLY B 244   N  ASN B 230           
SHEET    3 AA8 4 CYS B 250  ASP B 254 -1  O  ARG B 251   N  THR B 243           
SHEET    4 AA8 4 GLU B 260  MET B 262 -1  O  MET B 262   N  LEU B 252           
SHEET    1 AA9 4 ILE B 273  PHE B 278  0                                        
SHEET    2 AA9 4 LEU B 284  TYR B 289 -1  O  LEU B 286   N  SER B 277           
SHEET    3 AA9 4 ASN B 295  ASP B 298 -1  O  TRP B 297   N  LEU B 285           
SHEET    4 AA9 4 ARG B 304  VAL B 307 -1  O  ALA B 305   N  VAL B 296           
SHEET    1 AB1 2 VAL B 315  VAL B 320  0                                        
SHEET    2 AB1 2 VAL B 327  SER B 331 -1  O  GLY B 330   N  CYS B 317           
SSBOND   1 CYS R  140    CYS R  217                          1555   1555  2.03  
LINK         C   TYR D   1                 N   DAL D   2     1555   1555  1.33  
LINK         C   DAL D   2                 N   GLY D   3     1555   1555  1.33  
LINK         C   GLY D   3                 N   MEA D   4     1555   1555  1.34  
LINK         C   MEA D   4                 N   ETA D   5     1555   1555  1.43  
CISPEP   1 HIS R  223    PRO R  224          0         2.35                     
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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