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Database: PDB
Entry: 3C7K
LinkDB: 3C7K
Original site: 3C7K 
HEADER    SIGNALING PROTEIN                       07-FEB-08   3C7K              
TITLE     MOLECULAR ARCHITECTURE OF GALPHAO AND THE STRUCTURAL BASIS FOR RGS16- 
TITLE    2 MEDIATED DEACTIVATION                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA;     
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 22-354;                                           
COMPND   5 SYNONYM: GUANINE NUCLEOTIDE-BINDING PROTEIN G(O) SUBUNIT ALPHA;      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: REGULATOR OF G-PROTEIN SIGNALING 16;                       
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: RESIDUES 53-180;                                           
COMPND  11 SYNONYM: RGS16, RETINALLY ABUNDANT REGULATOR OF G-PROTEIN SIGNALING, 
COMPND  12 RGS-R, A28-RGS14P;                                                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: GNAO1, GNA0, GNAO;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET;                                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: RGS16, RGSR;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    RGS, GALPHA, ALF4 HETEROTRIMERIC G-PROTEIN GAP, GTP-BINDING,          
KEYWDS   2 LIPOPROTEIN, MYRISTATE, NUCLEOTIDE-BINDING, PALMITATE, TRANSDUCER,   
KEYWDS   3 PHOSPHOPROTEIN, SIGNAL TRANSDUCTION INHIBITOR, SIGNALING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.C.SLEP,M.A.KERCHER,T.WIELAND,C.CHEN,M.I.SIMON,P.B.SIGLER            
REVDAT   3   25-OCT-17 3C7K    1       REMARK                                   
REVDAT   2   24-FEB-09 3C7K    1       VERSN                                    
REVDAT   1   06-MAY-08 3C7K    0                                                
JRNL        AUTH   K.C.SLEP,M.A.KERCHER,T.WIELAND,C.K.CHEN,M.I.SIMON,P.B.SIGLER 
JRNL        TITL   MOLECULAR ARCHITECTURE OF G{ALPHA}O AND THE STRUCTURAL BASIS 
JRNL        TITL 2 FOR RGS16-MEDIATED DEACTIVATION.                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  6243 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18434540                                                     
JRNL        DOI    10.1073/PNAS.0801569105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 24012                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.250                           
REMARK   3   FREE R VALUE                     : 0.311                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2365                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6815                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 93.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.61900                                            
REMARK   3    B22 (A**2) : -10.61900                                            
REMARK   3    B33 (A**2) : 21.23800                                             
REMARK   3    B12 (A**2) : -17.32200                                            
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 37.08                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  3  : GDP.PRM                                        
REMARK   3  PARAMETER FILE  4  : ALF4.PRM                                       
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3C7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046440.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.15                               
REMARK 200  MONOCHROMATOR                  : X25 MONOCHROMATOR                  
REMARK 200  OPTICS                         : X25 OPTICS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS - B4                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27489                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1AGR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 8000 200 MM TRIS PH 8.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      157.07333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       78.53667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       78.53667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      157.07333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     ASN A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     ILE A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     HIS A    57                                                      
REMARK 465     GLU A    58                                                      
REMARK 465     ASP A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     LEU A   195                                                      
REMARK 465     HIS A   196                                                      
REMARK 465     PHE A   197                                                      
REMARK 465     ASN A   347                                                      
REMARK 465     LEU A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     GLY A   350                                                      
REMARK 465     CYS A   351                                                      
REMARK 465     GLY A   352                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     TYR A   354                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     PHE B    54                                                      
REMARK 465     SER B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     ASP B    57                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     ASP B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     ALA B   180                                                      
REMARK 465     ASN C    22                                                      
REMARK 465     LEU C    23                                                      
REMARK 465     LYS C    24                                                      
REMARK 465     GLU C    25                                                      
REMARK 465     ASP C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     ILE C    28                                                      
REMARK 465     SER C    29                                                      
REMARK 465     ALA C    30                                                      
REMARK 465     ALA C    31                                                      
REMARK 465     LYS C    32                                                      
REMARK 465     ASP C    33                                                      
REMARK 465     VAL C    34                                                      
REMARK 465     ASN C   346                                                      
REMARK 465     ASN C   347                                                      
REMARK 465     LEU C   348                                                      
REMARK 465     ARG C   349                                                      
REMARK 465     GLY C   350                                                      
REMARK 465     CYS C   351                                                      
REMARK 465     GLY C   352                                                      
REMARK 465     LEU C   353                                                      
REMARK 465     TYR C   354                                                      
REMARK 465     GLY D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     PHE D    54                                                      
REMARK 465     SER D    55                                                      
REMARK 465     GLU D    56                                                      
REMARK 465     ASP D    57                                                      
REMARK 465     VAL D    58                                                      
REMARK 465     LEU D    59                                                      
REMARK 465     GLY D    60                                                      
REMARK 465     TRP D    61                                                      
REMARK 465     ARG D    62                                                      
REMARK 465     GLU D    63                                                      
REMARK 465     ARG D   177                                                      
REMARK 465     ASP D   178                                                      
REMARK 465     LEU D   179                                                      
REMARK 465     ALA D   180                                                      
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  AL    ALF A   365     O    HOH A   401              2.07            
REMARK 500   O2B  GDP A   361     O    HOH A   402              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO C 292   C   -  N   -  CA  ANGL. DEV. =   9.6 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    LEU A  38       68.60   -103.00                                   
REMARK 500    ILE A  55       48.23    -80.18                                   
REMARK 500    ASN A  76      -33.74    -39.40                                   
REMARK 500    GLU A  99        9.14    -56.82                                   
REMARK 500    THR A 102      -82.47    -67.15                                   
REMARK 500    SER A 104      -71.00    -59.03                                   
REMARK 500    ARG A 113       -5.29    -53.98                                   
REMARK 500    MET A 114       -7.21     68.29                                   
REMARK 500    GLU A 115       28.16    -70.00                                   
REMARK 500    PRO A 119      130.32    -35.93                                   
REMARK 500    TRP A 132       -9.91    -54.60                                   
REMARK 500    SER A 144       -0.29    -58.65                                   
REMARK 500    ASN A 150      140.94    -39.73                                   
REMARK 500    SER A 159       34.36   -151.12                                   
REMARK 500    TYR A 168      135.13    -37.64                                   
REMARK 500    ARG A 177        1.07    -59.60                                   
REMARK 500    PHE A 190      148.09    168.93                                   
REMARK 500    PHE A 192      -90.96   -100.87                                   
REMARK 500    ILE A 213      -20.21    -37.36                                   
REMARK 500    HIS A 214      -71.67    -71.73                                   
REMARK 500    CYS A 215       24.93    -66.43                                   
REMARK 500    ASP A 218       82.64     38.41                                   
REMARK 500    THR A 220      -73.30    -51.13                                   
REMARK 500    GLU A 239       30.52    -65.57                                   
REMARK 500    ASN A 256       42.63    -88.17                                   
REMARK 500    PHE A 259      -18.88    -46.38                                   
REMARK 500    ASP A 262       44.64   -104.51                                   
REMARK 500    ASN A 270      174.41    -49.64                                   
REMARK 500    TYR A 291      105.87    -33.74                                   
REMARK 500    ARG A 313      -81.42    -90.37                                   
REMARK 500    HIS A 322      112.83   -167.82                                   
REMARK 500    CYS A 325       78.09   -163.22                                   
REMARK 500    ALA A 326      -27.48    -34.12                                   
REMARK 500    ALA A 345       32.91    -73.48                                   
REMARK 500    PHE B  86       52.25     70.20                                   
REMARK 500    SER B  87       34.11   -159.93                                   
REMARK 500    ARG B 122      134.41    -31.93                                   
REMARK 500    GLU B 124       19.59     57.08                                   
REMARK 500    ALA B 145       64.90   -166.62                                   
REMARK 500    ALA B 146      105.15    -29.60                                   
REMARK 500    CYS B 150      -74.10    -42.24                                   
REMARK 500    ASP B 165      -72.88   -124.34                                   
REMARK 500    LEU B 171      -79.06    -52.33                                   
REMARK 500    LYS B 172       78.68    -52.93                                   
REMARK 500    ALA B 175      -36.93    -39.69                                   
REMARK 500    GLU C  43       37.72     26.56                                   
REMARK 500    HIS C  57       57.92   -160.64                                   
REMARK 500    GLU C  58      -24.16   -141.29                                   
REMARK 500    ASP C  59      -74.15    157.84                                   
REMARK 500    SER C  75      -71.69    -53.05                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      86 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 362  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 182   OG1                                                    
REMARK 620 2 GDP A 361   O2B 141.4                                              
REMARK 620 3 HOH A 403   O    94.4 121.3                                        
REMARK 620 4 SER A  47   OG   76.2 103.3  66.9                                  
REMARK 620 5 HOH A 402   O    93.9  50.2 138.8  76.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 362  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 182   OG1                                                    
REMARK 620 2 GDP C 361   O2B 157.8                                              
REMARK 620 3 HOH C 402   O    77.4  81.1                                        
REMARK 620 4 SER C  47   OG   82.5 103.5  91.4                                  
REMARK 620 5 HOH C 403   O    89.2 112.0 166.4  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 362                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 362                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF C 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 361                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C7L   RELATED DB: PDB                                   
DBREF  3C7K A   22   354  UNP    P18872   GNAO_MOUSE      22    354             
DBREF  3C7K B   53   180  UNP    P97428   RGS16_MOUSE     53    180             
DBREF  3C7K C   22   354  UNP    P18872   GNAO_MOUSE      22    354             
DBREF  3C7K D   53   180  UNP    P97428   RGS16_MOUSE     53    180             
SEQADV 3C7K GLY B   52  UNP  P97428              EXPRESSION TAG                 
SEQADV 3C7K GLY D   52  UNP  P97428              EXPRESSION TAG                 
SEQRES   1 A  333  ASN LEU LYS GLU ASP GLY ILE SER ALA ALA LYS ASP VAL          
SEQRES   2 A  333  LYS LEU LEU LEU LEU GLY ALA GLY GLU SER GLY LYS SER          
SEQRES   3 A  333  THR ILE VAL LYS GLN MET LYS ILE ILE HIS GLU ASP GLY          
SEQRES   4 A  333  PHE SER GLY GLU ASP VAL LYS GLN TYR LYS PRO VAL VAL          
SEQRES   5 A  333  TYR SER ASN THR ILE GLN SER LEU ALA ALA ILE VAL ARG          
SEQRES   6 A  333  ALA MET ASP THR LEU GLY VAL GLU TYR GLY ASP LYS GLU          
SEQRES   7 A  333  ARG LYS THR ASP SER LYS MET VAL CYS ASP VAL VAL SER          
SEQRES   8 A  333  ARG MET GLU ASP THR GLU PRO PHE SER ALA GLU LEU LEU          
SEQRES   9 A  333  SER ALA MET MET ARG LEU TRP GLY ASP SER GLY ILE GLN          
SEQRES  10 A  333  GLU CYS PHE ASN ARG SER ARG GLU TYR GLN LEU ASN ASP          
SEQRES  11 A  333  SER ALA LYS TYR TYR LEU ASP SER LEU ASP ARG ILE GLY          
SEQRES  12 A  333  ALA GLY ASP TYR GLN PRO THR GLU GLN ASP ILE LEU ARG          
SEQRES  13 A  333  THR ARG VAL LYS THR THR GLY ILE VAL GLU THR HIS PHE          
SEQRES  14 A  333  THR PHE LYS ASN LEU HIS PHE ARG LEU PHE ASP VAL GLY          
SEQRES  15 A  333  GLY GLN ARG SER GLU ARG LYS LYS TRP ILE HIS CYS PHE          
SEQRES  16 A  333  GLU ASP VAL THR ALA ILE ILE PHE CYS VAL ALA LEU SER          
SEQRES  17 A  333  GLY TYR ASP GLN VAL LEU HIS GLU ASP GLU THR THR ASN          
SEQRES  18 A  333  ARG MET HIS GLU SER LEU MET LEU PHE ASP SER ILE CYS          
SEQRES  19 A  333  ASN ASN LYS PHE PHE ILE ASP THR SER ILE ILE LEU PHE          
SEQRES  20 A  333  LEU ASN LYS LYS ASP LEU PHE GLY GLU LYS ILE LYS LYS          
SEQRES  21 A  333  SER PRO LEU THR ILE CYS PHE PRO GLU TYR PRO GLY SER          
SEQRES  22 A  333  ASN THR TYR GLU ASP ALA ALA ALA TYR ILE GLN THR GLN          
SEQRES  23 A  333  PHE GLU SER LYS ASN ARG SER PRO ASN LYS GLU ILE TYR          
SEQRES  24 A  333  CYS HIS MET THR CYS ALA THR ASP THR ASN ASN ILE GLN          
SEQRES  25 A  333  VAL VAL PHE ASP ALA VAL THR ASP ILE ILE ILE ALA ASN          
SEQRES  26 A  333  ASN LEU ARG GLY CYS GLY LEU TYR                              
SEQRES   1 B  129  GLY SER PHE SER GLU ASP VAL LEU GLY TRP ARG GLU SER          
SEQRES   2 B  129  PHE ASP LEU LEU LEU ASN SER LYS ASN GLY VAL ALA ALA          
SEQRES   3 B  129  PHE HIS ALA PHE LEU LYS THR GLU PHE SER GLU GLU ASN          
SEQRES   4 B  129  LEU GLU PHE TRP LEU ALA CYS GLU GLU PHE LYS LYS ILE          
SEQRES   5 B  129  ARG SER ALA THR LYS LEU ALA SER ARG ALA HIS HIS ILE          
SEQRES   6 B  129  PHE ASP GLU TYR ILE ARG SER GLU ALA PRO LYS GLU VAL          
SEQRES   7 B  129  ASN ILE ASP HIS GLU THR ARG GLU LEU THR LYS THR ASN          
SEQRES   8 B  129  LEU GLN ALA ALA THR THR SER CYS PHE ASP VAL ALA GLN          
SEQRES   9 B  129  GLY LYS THR ARG THR LEU MET GLU LYS ASP SER TYR PRO          
SEQRES  10 B  129  ARG PHE LEU LYS SER PRO ALA TYR ARG ASP LEU ALA              
SEQRES   1 C  333  ASN LEU LYS GLU ASP GLY ILE SER ALA ALA LYS ASP VAL          
SEQRES   2 C  333  LYS LEU LEU LEU LEU GLY ALA GLY GLU SER GLY LYS SER          
SEQRES   3 C  333  THR ILE VAL LYS GLN MET LYS ILE ILE HIS GLU ASP GLY          
SEQRES   4 C  333  PHE SER GLY GLU ASP VAL LYS GLN TYR LYS PRO VAL VAL          
SEQRES   5 C  333  TYR SER ASN THR ILE GLN SER LEU ALA ALA ILE VAL ARG          
SEQRES   6 C  333  ALA MET ASP THR LEU GLY VAL GLU TYR GLY ASP LYS GLU          
SEQRES   7 C  333  ARG LYS THR ASP SER LYS MET VAL CYS ASP VAL VAL SER          
SEQRES   8 C  333  ARG MET GLU ASP THR GLU PRO PHE SER ALA GLU LEU LEU          
SEQRES   9 C  333  SER ALA MET MET ARG LEU TRP GLY ASP SER GLY ILE GLN          
SEQRES  10 C  333  GLU CYS PHE ASN ARG SER ARG GLU TYR GLN LEU ASN ASP          
SEQRES  11 C  333  SER ALA LYS TYR TYR LEU ASP SER LEU ASP ARG ILE GLY          
SEQRES  12 C  333  ALA GLY ASP TYR GLN PRO THR GLU GLN ASP ILE LEU ARG          
SEQRES  13 C  333  THR ARG VAL LYS THR THR GLY ILE VAL GLU THR HIS PHE          
SEQRES  14 C  333  THR PHE LYS ASN LEU HIS PHE ARG LEU PHE ASP VAL GLY          
SEQRES  15 C  333  GLY GLN ARG SER GLU ARG LYS LYS TRP ILE HIS CYS PHE          
SEQRES  16 C  333  GLU ASP VAL THR ALA ILE ILE PHE CYS VAL ALA LEU SER          
SEQRES  17 C  333  GLY TYR ASP GLN VAL LEU HIS GLU ASP GLU THR THR ASN          
SEQRES  18 C  333  ARG MET HIS GLU SER LEU MET LEU PHE ASP SER ILE CYS          
SEQRES  19 C  333  ASN ASN LYS PHE PHE ILE ASP THR SER ILE ILE LEU PHE          
SEQRES  20 C  333  LEU ASN LYS LYS ASP LEU PHE GLY GLU LYS ILE LYS LYS          
SEQRES  21 C  333  SER PRO LEU THR ILE CYS PHE PRO GLU TYR PRO GLY SER          
SEQRES  22 C  333  ASN THR TYR GLU ASP ALA ALA ALA TYR ILE GLN THR GLN          
SEQRES  23 C  333  PHE GLU SER LYS ASN ARG SER PRO ASN LYS GLU ILE TYR          
SEQRES  24 C  333  CYS HIS MET THR CYS ALA THR ASP THR ASN ASN ILE GLN          
SEQRES  25 C  333  VAL VAL PHE ASP ALA VAL THR ASP ILE ILE ILE ALA ASN          
SEQRES  26 C  333  ASN LEU ARG GLY CYS GLY LEU TYR                              
SEQRES   1 D  129  GLY SER PHE SER GLU ASP VAL LEU GLY TRP ARG GLU SER          
SEQRES   2 D  129  PHE ASP LEU LEU LEU ASN SER LYS ASN GLY VAL ALA ALA          
SEQRES   3 D  129  PHE HIS ALA PHE LEU LYS THR GLU PHE SER GLU GLU ASN          
SEQRES   4 D  129  LEU GLU PHE TRP LEU ALA CYS GLU GLU PHE LYS LYS ILE          
SEQRES   5 D  129  ARG SER ALA THR LYS LEU ALA SER ARG ALA HIS HIS ILE          
SEQRES   6 D  129  PHE ASP GLU TYR ILE ARG SER GLU ALA PRO LYS GLU VAL          
SEQRES   7 D  129  ASN ILE ASP HIS GLU THR ARG GLU LEU THR LYS THR ASN          
SEQRES   8 D  129  LEU GLN ALA ALA THR THR SER CYS PHE ASP VAL ALA GLN          
SEQRES   9 D  129  GLY LYS THR ARG THR LEU MET GLU LYS ASP SER TYR PRO          
SEQRES  10 D  129  ARG PHE LEU LYS SER PRO ALA TYR ARG ASP LEU ALA              
HET     MG  A 362       1                                                       
HET    ALF  A 365       5                                                       
HET    GDP  A 361      28                                                       
HET     MG  C 362       1                                                       
HET    ALF  C 365       5                                                       
HET    GDP  C 361      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  ALF    2(AL F4 1-)                                                  
FORMUL   7  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL  11  HOH   *6(H2 O)                                                      
HELIX    1   1 ILE A   49  MET A   53  5                                   5    
HELIX    2   2 SER A   62  GLY A   92  1                                  31    
HELIX    3   3 GLU A   99  MET A  114  1                                  16    
HELIX    4   4 SER A  121  TRP A  132  1                                  12    
HELIX    5   5 ASP A  134  ASN A  142  1                                   9    
HELIX    6   6 SER A  152  ASP A  158  1                                   7    
HELIX    7   7 SER A  159  GLY A  164  1                                   6    
HELIX    8   8 GLU A  208  ILE A  213  1                                   6    
HELIX    9   9 HIS A  214  GLU A  217  5                                   4    
HELIX   10  10 ALA A  227  GLN A  233  5                                   7    
HELIX   11  11 ASN A  242  ASN A  256  1                                  15    
HELIX   12  12 ASN A  257  ILE A  261  5                                   5    
HELIX   13  13 LYS A  271  LYS A  280  1                                  10    
HELIX   14  14 PRO A  283  CYS A  287  5                                   5    
HELIX   15  15 THR A  296  LYS A  311  1                                  16    
HELIX   16  16 ASP A  328  ALA A  345  1                                  18    
HELIX   17  17 SER B   64  ASN B   70  1                                   7    
HELIX   18  18 SER B   71  PHE B   86  1                                  16    
HELIX   19  19 GLU B   88  LYS B  101  1                                  14    
HELIX   20  20 SER B  105  TYR B  120  1                                  16    
HELIX   21  21 ASP B  132  LEU B  143  1                                  12    
HELIX   22  22 GLN B  144  ALA B  146  5                                   3    
HELIX   23  23 PHE B  151  ASP B  165  1                                  15    
HELIX   24  24 TYR B  167  LYS B  172  1                                   6    
HELIX   25  25 SER B  173  ARG B  177  5                                   5    
HELIX   26  26 GLY C   45  GLU C   58  1                                  14    
HELIX   27  27 ASP C   65  GLY C   92  1                                  28    
HELIX   28  28 GLU C   99  ARG C  113  1                                  15    
HELIX   29  29 SER C  121  GLY C  133  1                                  13    
HELIX   30  30 ASP C  134  ASN C  142  1                                   9    
HELIX   31  31 SER C  152  ASP C  158  1                                   7    
HELIX   32  32 SER C  159  ALA C  165  1                                   7    
HELIX   33  33 THR C  171  ARG C  177  1                                   7    
HELIX   34  34 GLU C  208  ILE C  213  1                                   6    
HELIX   35  35 HIS C  214  GLU C  217  5                                   4    
HELIX   36  36 ALA C  227  GLN C  233  5                                   7    
HELIX   37  37 ASN C  242  ASN C  256  1                                  15    
HELIX   38  38 ASN C  257  ILE C  261  5                                   5    
HELIX   39  39 LYS C  271  GLU C  277  1                                   7    
HELIX   40  40 PRO C  283  CYS C  287  5                                   5    
HELIX   41  41 THR C  296  LYS C  311  1                                  16    
HELIX   42  42 ASP C  328  ALA C  345  1                                  18    
HELIX   43  43 PHE D   65  LEU D   69  5                                   5    
HELIX   44  44 ASN D   73  LYS D   83  1                                  11    
HELIX   45  45 GLU D   88  LYS D  101  1                                  14    
HELIX   46  46 SER D  105  ILE D  121  1                                  17    
HELIX   47  47 ASP D  132  LEU D  143  1                                  12    
HELIX   48  48 PHE D  151  GLU D  163  1                                  13    
HELIX   49  49 TYR D  167  LYS D  172  1                                   6    
SHEET    1   A 6 VAL A 186  THR A 188  0                                        
SHEET    2   A 6 LEU A 199  ASP A 201 -1  O  LEU A 199   N  THR A 188           
SHEET    3   A 6 LEU A  36  GLY A  40  1  N  LEU A  38   O  PHE A 200           
SHEET    4   A 6 ALA A 221  CYS A 225  1  O  ILE A 223   N  LEU A  37           
SHEET    5   A 6 SER A 264  PHE A 268  1  O  ILE A 266   N  ILE A 222           
SHEET    6   A 6 ILE A 319  TYR A 320  1  O  TYR A 320   N  LEU A 267           
SHEET    1   B 6 VAL C 186  THR C 191  0                                        
SHEET    2   B 6 HIS C 196  ASP C 201 -1  O  LEU C 199   N  THR C 188           
SHEET    3   B 6 LEU C  36  GLY C  40  1  N  LEU C  36   O  ARG C 198           
SHEET    4   B 6 ALA C 221  CYS C 225  1  O  ALA C 221   N  LEU C  37           
SHEET    5   B 6 SER C 264  PHE C 268  1  O  SER C 264   N  ILE C 222           
SHEET    6   B 6 ILE C 319  HIS C 322  1  O  TYR C 320   N  LEU C 267           
LINK         OG1 THR A 182                MG    MG A 362     1555   1555  2.18  
LINK         OG1 THR C 182                MG    MG C 362     1555   1555  2.42  
LINK        MG    MG A 362                 O2B GDP A 361     1555   1555  2.07  
LINK        MG    MG C 362                 O2B GDP C 361     1555   1555  2.20  
LINK        MG    MG A 362                 O   HOH A 403     1555   1555  2.48  
LINK        MG    MG C 362                 O   HOH C 402     1555   1555  2.26  
LINK         OG  SER A  47                MG    MG A 362     1555   1555  2.52  
LINK         OG  SER C  47                MG    MG C 362     1555   1555  2.53  
LINK        MG    MG C 362                 O   HOH C 403     1555   1555  2.67  
LINK        MG    MG A 362                 O   HOH A 402     1555   1555  2.70  
SITE     1 AC1  2 SER A  47  THR A 182                                          
SITE     1 AC2  9 ALA A  41  GLY A  42  GLU A  43  LYS A  46                    
SITE     2 AC2  9 ARG A 179  LYS A 181  THR A 182  GLY A 204                    
SITE     3 AC2  9 GLN A 205                                                     
SITE     1 AC3  2 SER C  47  THR C 182                                          
SITE     1 AC4  8 GLY C  42  GLU C  43  LYS C  46  ARG C 179                    
SITE     2 AC4  8 LYS C 181  THR C 182  GLY C 204  GLN C 205                    
SITE     1 AC5 19 GLU A  43  SER A  44  GLY A  45  LYS A  46                    
SITE     2 AC5 19 SER A  47  THR A  48  ASP A 151  SER A 152                    
SITE     3 AC5 19 LEU A 176  ARG A 177  THR A 178  ARG A 179                    
SITE     4 AC5 19 ASN A 270  LYS A 271  ASP A 273  LEU A 274                    
SITE     5 AC5 19 CYS A 325  ALA A 326  THR A 327                               
SITE     1 AC6 18 GLU C  43  SER C  44  GLY C  45  LYS C  46                    
SITE     2 AC6 18 SER C  47  THR C  48  ASP C 151  SER C 152                    
SITE     3 AC6 18 LEU C 176  ARG C 177  THR C 178  ARG C 179                    
SITE     4 AC6 18 ASN C 270  LYS C 271  ASP C 273  LEU C 274                    
SITE     5 AC6 18 CYS C 325  ALA C 326                                          
CRYST1   96.357   96.357  235.610  90.00  90.00 120.00 P 32 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010378  0.005992  0.000000        0.00000                         
SCALE2      0.000000  0.011984  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004244        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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