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Chemical substance (3) PDB-CCD (3) Protein sequence (8) UniProt (2) SWISS-PROT (2) PDBSTR (4) Protein domain (9) InterPro (7) Pfam (2) Literature (1) PubMed (1) All databases (21)
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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