HEADER SIGNALING PROTEIN 26-SEP-06 2IHB
TITLE CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF HUMAN RGS10 AND
TITLE 2 ACTIVATED GI ALPHA 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(K) SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GI, ALPHA-3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: REGULATOR OF G-PROTEIN SIGNALLING 10;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GNAI3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RGS10;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)R3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS G PROTEIN SIGNALLING, RGS, HETEROTRIMERIC G PROTEIN, SIGNALLING
KEYWDS 2 COMPLEX, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 3 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SOUNDARARAJAN,A.P.TURNBULL,E.PAPAGRIGORIOU,A.C.W.PIKE,G.BUNKOCZI,
AUTHOR 2 E.UGOCHUKWU,F.GORREC,F.VON DELFT,J.WEIGELT,A.EDWARDS,C.ARROWSMITH,
AUTHOR 3 M.SUNDSTROM,D.A.DOYLE,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 7 30-AUG-23 2IHB 1 REMARK SEQADV LINK
REVDAT 6 13-JUL-11 2IHB 1 VERSN
REVDAT 5 24-FEB-09 2IHB 1 VERSN
REVDAT 4 30-SEP-08 2IHB 1 JRNL
REVDAT 3 06-NOV-07 2IHB 1 REMARK
REVDAT 2 16-OCT-07 2IHB 1 REMARK
REVDAT 1 21-NOV-06 2IHB 0
JRNL AUTH M.SOUNDARARAJAN,F.S.WILLARD,A.J.KIMPLE,A.P.TURNBULL,
JRNL AUTH 2 L.J.BALL,G.A.SCHOCH,C.GILEADI,O.Y.FEDOROV,E.F.DOWLER,
JRNL AUTH 3 V.A.HIGMAN,S.Q.HUTSELL,M.SUNDSTROM,D.A.DOYLE,D.P.SIDEROVSKI
JRNL TITL STRUCTURAL DIVERSITY IN THE RGS DOMAIN AND ITS INTERACTION
JRNL TITL 2 WITH HETEROTRIMERIC G PROTEIN ALPHA-SUBUNITS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 6457 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18434541
JRNL DOI 10.1073/PNAS.0801508105
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 19430
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 + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1040
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1144
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3399
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.07000
REMARK 3 B22 (A**2) : 2.07000
REMARK 3 B33 (A**2) : -4.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.452
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.277
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.321
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3497 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2340 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4725 ; 1.057 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5697 ; 0.806 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 425 ; 5.349 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 165 ;36.469 ;24.485
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;15.248 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;21.765 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 526 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3864 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 737 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 763 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2332 ; 0.173 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1722 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1840 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 78 ; 0.141 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.102 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 3 ; 0.056 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 15 ; 0.178 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.027 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2186 ; 0.386 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 865 ; 0.053 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3420 ; 0.702 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1507 ; 0.895 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1305 ; 1.470 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 348
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4394 -25.4049 -31.3374
REMARK 3 T TENSOR
REMARK 3 T11: -0.1741 T22: -0.1096
REMARK 3 T33: -0.2642 T12: -0.0266
REMARK 3 T13: 0.0169 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 3.4671 L22: 1.9755
REMARK 3 L33: 3.1447 L12: 0.4301
REMARK 3 L13: 1.0510 L23: 0.5556
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: 0.0019 S13: -0.0201
REMARK 3 S21: -0.0515 S22: -0.0507 S23: 0.2177
REMARK 3 S31: 0.0105 S32: -0.1076 S33: 0.0899
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 24 B 102
REMARK 3 RESIDUE RANGE : B 114 B 145
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3296 -16.4536 -7.1103
REMARK 3 T TENSOR
REMARK 3 T11: -0.1290 T22: -0.0353
REMARK 3 T33: -0.2083 T12: 0.0503
REMARK 3 T13: 0.0443 T23: -0.0840
REMARK 3 L TENSOR
REMARK 3 L11: 5.7723 L22: 5.8487
REMARK 3 L33: 6.4491 L12: 0.4006
REMARK 3 L13: -1.4485 L23: -0.8734
REMARK 3 S TENSOR
REMARK 3 S11: -0.0457 S12: -0.3831 S13: 0.0060
REMARK 3 S21: 0.4323 S22: 0.0121 S23: 0.1024
REMARK 3 S31: -0.2032 S32: 0.1367 S33: 0.0335
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2IHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039570.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20470
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.2
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: PHASER
REMARK 200 STARTING MODEL: SWISSMODEL BASED ON THE COORDINATES OF PDB ENTRIES
REMARK 200 1AGR, 1EZT, 1EZY, 2BV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M BIS-TRIS, PH 5.5,
REMARK 280 25% PEG3350 , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.67950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 50.31400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 50.31400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 109.01925
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 50.31400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 50.31400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.33975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 50.31400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.31400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 109.01925
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 50.31400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.31400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.33975
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.67950
REMARK 290
REMARK 290 REMARK: NULL
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: 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 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 LYS A 32
REMARK 465 GLU A 350
REMARK 465 CYS A 351
REMARK 465 GLY A 352
REMARK 465 LEU A 353
REMARK 465 TYR A 354
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 LYS B 4
REMARK 465 ARG B 5
REMARK 465 PRO B 6
REMARK 465 PRO B 7
REMARK 465 SER B 8
REMARK 465 ASP B 9
REMARK 465 ILE B 10
REMARK 465 HIS B 11
REMARK 465 ASP B 12
REMARK 465 SER B 13
REMARK 465 ASP B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 SER B 17
REMARK 465 SER B 18
REMARK 465 SER B 19
REMARK 465 SER B 20
REMARK 465 HIS B 21
REMARK 465 GLN B 22
REMARK 465 SER B 23
REMARK 465 GLN B 103
REMARK 465 SER B 104
REMARK 465 ARG B 105
REMARK 465 LEU B 106
REMARK 465 ASN B 107
REMARK 465 GLU B 108
REMARK 465 LYS B 109
REMARK 465 ILE B 110
REMARK 465 LEU B 111
REMARK 465 GLU B 112
REMARK 465 GLU B 113
REMARK 465 LYS B 146
REMARK 465 HIS B 147
REMARK 465 LYS B 148
REMARK 465 ARG B 149
REMARK 465 THR B 150
REMARK 465 GLU B 151
REMARK 465 GLU B 152
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 33 CG CD OE1 OE2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 GLU A 116 CD OE1 OE2
REMARK 470 LYS A 128 NZ
REMARK 470 ARG A 132 CD NE CZ NH1 NH2
REMARK 470 ASP A 193 CG OD1 OD2
REMARK 470 LYS A 197 CD CE NZ
REMARK 470 GLU A 238 CD OE1 OE2
REMARK 470 LYS A 248 NZ
REMARK 470 LYS A 257 CD CE NZ
REMARK 470 GLU A 276 CG CD OE1 OE2
REMARK 470 ARG A 280 CD NE CZ NH1 NH2
REMARK 470 ASP A 315 CG OD1 OD2
REMARK 470 LYS A 330 CD CE NZ
REMARK 470 LYS A 345 CD CE NZ
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 LEU B 24 CG CD1 CD2
REMARK 470 LYS B 25 CE NZ
REMARK 470 SER B 26 OG
REMARK 470 LYS B 29 CD CE NZ
REMARK 470 LYS B 53 CD CE NZ
REMARK 470 LYS B 71 CE NZ
REMARK 470 LYS B 75 CD CE NZ
REMARK 470 GLN B 77 CG CD OE1 NE2
REMARK 470 GLU B 80 CD OE1 OE2
REMARK 470 LYS B 83 CD CE NZ
REMARK 470 LYS B 93 CE NZ
REMARK 470 LYS B 121 CE NZ
REMARK 470 LYS B 140 CD CE NZ
REMARK 470 ASP B 142 CG OD1 OD2
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 354 O2B GDP A 356 1.97
REMARK 500 AL ALF A 354 O HOH A 358 1.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 58 -115.93 -109.34
REMARK 500 SER B 96 50.40 -104.96
REMARK 500 ASP B 133 -79.77 -116.42
REMARK 500 LEU B 143 -37.03 -39.72
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 355 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 47 OG
REMARK 620 2 THR A 181 OG1 82.6
REMARK 620 3 GDP A 356 O1B 95.1 174.1
REMARK 620 4 HOH A 359 O 77.4 88.9 95.9
REMARK 620 5 HOH A 360 O 84.5 80.8 93.6 160.2
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 ALF A 354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 356
DBREF 2IHB A 32 354 UNP P08754 GNAI3_HUMAN 32 354
DBREF 2IHB B 2 152 UNP Q96GN0 Q96GN0_HUMAN 10 160
SEQADV 2IHB SER B 0 UNP Q96GN0 EXPRESSION TAG
SEQADV 2IHB MET B 1 UNP Q96GN0 EXPRESSION TAG
SEQRES 1 A 323 LYS GLU VAL LYS LEU LEU LEU LEU GLY ALA GLY GLU SER
SEQRES 2 A 323 GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE ILE HIS
SEQRES 3 A 323 GLU ASP GLY TYR SER GLU ASP GLU CYS LYS GLN TYR LYS
SEQRES 4 A 323 VAL VAL VAL TYR SER ASN THR ILE GLN SER ILE ILE ALA
SEQRES 5 A 323 ILE ILE ARG ALA MET GLY ARG LEU LYS ILE ASP PHE GLY
SEQRES 6 A 323 GLU ALA ALA ARG ALA ASP ASP ALA ARG GLN LEU PHE VAL
SEQRES 7 A 323 LEU ALA GLY SER ALA GLU GLU GLY VAL MET THR PRO GLU
SEQRES 8 A 323 LEU ALA GLY VAL ILE LYS ARG LEU TRP ARG ASP GLY GLY
SEQRES 9 A 323 VAL GLN ALA CYS PHE SER ARG SER ARG GLU TYR GLN LEU
SEQRES 10 A 323 ASN ASP SER ALA SER TYR TYR LEU ASN ASP LEU ASP ARG
SEQRES 11 A 323 ILE SER GLN SER ASN TYR ILE PRO THR GLN GLN ASP VAL
SEQRES 12 A 323 LEU ARG THR ARG VAL LYS THR THR GLY ILE VAL GLU THR
SEQRES 13 A 323 HIS PHE THR PHE LYS ASP LEU TYR PHE LYS MET PHE ASP
SEQRES 14 A 323 VAL GLY GLY GLN ARG SER GLU ARG LYS LYS TRP ILE HIS
SEQRES 15 A 323 CYS PHE GLU GLY VAL THR ALA ILE ILE PHE CYS VAL ALA
SEQRES 16 A 323 LEU SER ASP TYR ASP LEU VAL LEU ALA GLU ASP GLU GLU
SEQRES 17 A 323 MET ASN ARG MET HIS GLU SER MET LYS LEU PHE ASP SER
SEQRES 18 A 323 ILE CYS ASN ASN LYS TRP PHE THR GLU THR SER ILE ILE
SEQRES 19 A 323 LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU GLU LYS ILE
SEQRES 20 A 323 LYS ARG SER PRO LEU THR ILE CYS TYR PRO GLU TYR THR
SEQRES 21 A 323 GLY SER ASN THR TYR GLU GLU ALA ALA ALA TYR ILE GLN
SEQRES 22 A 323 CYS GLN PHE GLU ASP LEU ASN ARG ARG LYS ASP THR LYS
SEQRES 23 A 323 GLU ILE TYR THR HIS PHE THR CYS ALA THR ASP THR LYS
SEQRES 24 A 323 ASN VAL GLN PHE VAL PHE ASP ALA VAL THR ASP VAL ILE
SEQRES 25 A 323 ILE LYS ASN ASN LEU LYS GLU CYS GLY LEU TYR
SEQRES 1 B 153 SER MET SER ARG LYS ARG PRO PRO SER ASP ILE HIS ASP
SEQRES 2 B 153 SER ASP GLY SER SER SER SER SER HIS GLN SER LEU LYS
SEQRES 3 B 153 SER THR ALA LYS TRP ALA ALA SER LEU GLU ASN LEU LEU
SEQRES 4 B 153 GLU ASP PRO GLU GLY VAL LYS ARG PHE ARG GLU PHE LEU
SEQRES 5 B 153 LYS LYS GLU PHE SER GLU GLU ASN VAL LEU PHE TRP LEU
SEQRES 6 B 153 ALA CYS GLU ASP PHE LYS LYS MET GLN ASP LYS THR GLN
SEQRES 7 B 153 MET GLN GLU LYS ALA LYS GLU ILE TYR MET THR PHE LEU
SEQRES 8 B 153 SER SER LYS ALA SER SER GLN VAL ASN VAL GLU GLY GLN
SEQRES 9 B 153 SER ARG LEU ASN GLU LYS ILE LEU GLU GLU PRO HIS PRO
SEQRES 10 B 153 LEU MET PHE GLN LYS LEU GLN ASP GLN ILE PHE ASN LEU
SEQRES 11 B 153 MET LYS TYR ASP SER TYR SER ARG PHE LEU LYS SER ASP
SEQRES 12 B 153 LEU PHE LEU LYS HIS LYS ARG THR GLU GLU
HET ALF A 354 5
HET MG A 355 1
HET GDP A 356 28
HETNAM ALF TETRAFLUOROALUMINATE ION
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 ALF AL F4 1-
FORMUL 4 MG MG 2+
FORMUL 5 GDP C10 H15 N5 O11 P2
FORMUL 6 HOH *18(H2 O)
HELIX 1 1 GLY A 45 GLU A 58 1 14
HELIX 2 2 SER A 62 GLN A 68 1 7
HELIX 3 3 TYR A 69 LYS A 92 1 24
HELIX 4 4 ALA A 99 LEU A 110 1 12
HELIX 5 5 ALA A 111 GLU A 115 5 5
HELIX 6 6 THR A 120 ASP A 133 1 14
HELIX 7 7 ASP A 133 ARG A 142 1 10
HELIX 8 8 SER A 143 TYR A 146 5 4
HELIX 9 9 SER A 151 ASN A 157 1 7
HELIX 10 10 ASP A 158 GLN A 164 1 7
HELIX 11 11 THR A 170 ARG A 176 1 7
HELIX 12 12 GLN A 204 LYS A 209 1 6
HELIX 13 13 LYS A 210 PHE A 215 5 6
HELIX 14 14 SER A 228 LEU A 232 5 5
HELIX 15 15 ASN A 241 ASN A 255 1 15
HELIX 16 16 ASN A 256 THR A 260 5 5
HELIX 17 17 LYS A 270 SER A 281 1 12
HELIX 18 18 PRO A 282 CYS A 286 5 5
HELIX 19 19 THR A 295 ASP A 309 1 15
HELIX 20 20 ASP A 328 ASN A 346 1 19
HELIX 21 21 LEU B 24 SER B 33 1 10
HELIX 22 22 SER B 33 ASP B 40 1 8
HELIX 23 23 ASP B 40 GLU B 54 1 15
HELIX 24 24 GLU B 57 MET B 72 1 16
HELIX 25 25 ASP B 74 LEU B 90 1 17
HELIX 26 26 PHE B 119 ASP B 133 1 15
HELIX 27 27 ASP B 133 LEU B 139 1 7
SHEET 1 A 6 ILE A 184 PHE A 191 0
SHEET 2 A 6 LEU A 194 VAL A 201 -1 O PHE A 196 N PHE A 189
SHEET 3 A 6 VAL A 34 LEU A 39 1 N LEU A 36 O LYS A 197
SHEET 4 A 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37
SHEET 5 A 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221
SHEET 6 A 6 ILE A 319 PHE A 323 1 O TYR A 320 N LEU A 266
LINK OG SER A 47 MG MG A 355 1555 1555 2.24
LINK OG1 THR A 181 MG MG A 355 1555 1555 1.97
LINK MG MG A 355 O1B GDP A 356 1555 1555 2.07
LINK MG MG A 355 O HOH A 359 1555 1555 1.85
LINK MG MG A 355 O HOH A 360 1555 1555 1.88
SITE 1 AC1 14 GLY A 42 GLU A 43 LYS A 46 ARG A 178
SITE 2 AC1 14 LYS A 180 THR A 181 VAL A 201 GLY A 203
SITE 3 AC1 14 GLN A 204 MG A 355 GDP A 356 HOH A 358
SITE 4 AC1 14 HOH A 359 HOH A 360
SITE 1 AC2 6 SER A 47 THR A 181 ALF A 354 GDP A 356
SITE 2 AC2 6 HOH A 359 HOH A 360
SITE 1 AC3 22 GLU A 43 SER A 44 GLY A 45 LYS A 46
SITE 2 AC3 22 SER A 47 THR A 48 SER A 151 LEU A 175
SITE 3 AC3 22 ARG A 176 THR A 177 ARG A 178 ASN A 269
SITE 4 AC3 22 LYS A 270 ASP A 272 LEU A 273 CYS A 325
SITE 5 AC3 22 ALA A 326 THR A 327 ALF A 354 MG A 355
SITE 6 AC3 22 HOH A 359 HOH A 360
CRYST1 100.628 100.628 145.359 90.00 90.00 90.00 P 43 21 2 8
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 0.009938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006880 0.00000
(ATOM LINES ARE NOT SHOWN.)
END