HEADER SIGNALING PROTEIN/HYDROLASE 03-JUN-14 4QJ5
TITLE STRUCTURE OF A FRAGMENT OF HUMAN PHOSPHOLIPASE C-BETA3 DELTA472-581,
TITLE 2 BOUND TO IP3 AND IN COMPLEX WITH GALPHAQ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 7-359;
COMPND 5 SYNONYM: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-Q;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE
COMPND 9 BETA-3;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 10-891;
COMPND 12 SYNONYM: PHOSPHOINOSITIDE PHOSPHOLIPASE C-BETA-3, PHOSPHOLIPASE C-
COMPND 13 BETA-3, PLC-BETA-3;
COMPND 14 EC: 3.1.4.11;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: GNAQ;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTA;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: PLCB3;
SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PFASTBACDUAL
KEYWDS GTP-BINDING PROTEIN ALPHA SUBUNITS, PHOSPHOLIPASE C BETA, PH DOMAIN,
KEYWDS 2 EF HAND, C2 DOMAIN, TIM BARREL DOMAIN, GTP HYDROLYSIS, G-PROTEIN
KEYWDS 3 SIGNALING, LIPASE, CALCIUM BINDING, GTP BINDING, PHOSPHOLIPIDS,
KEYWDS 4 MEMBRANE, SIGNALING PROTEIN-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.LYON,J.J.G.TESMER
REVDAT 5 20-SEP-23 4QJ5 1 REMARK SEQADV LINK
REVDAT 4 02-AUG-17 4QJ5 1 SOURCE REMARK
REVDAT 3 11-FEB-15 4QJ5 1 JRNL
REVDAT 2 24-DEC-14 4QJ5 1 JRNL
REVDAT 1 22-OCT-14 4QJ5 0
JRNL AUTH A.M.LYON,J.A.BEGLEY,T.D.MANETT,J.J.TESMER
JRNL TITL MOLECULAR MECHANISMS OF PHOSPHOLIPASE C BETA 3
JRNL TITL 2 AUTOINHIBITION.
JRNL REF STRUCTURE V. 22 1844 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 25435326
JRNL DOI 10.1016/J.STR.2014.10.008
REMARK 2
REMARK 2 RESOLUTION. 3.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 3.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 20962
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
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) : 3.41
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1438
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8621
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 2
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.37000
REMARK 3 B22 (A**2) : 1.69000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.626
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.602
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 88.636
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.865
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8875 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8479 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12007 ; 1.016 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19522 ; 0.703 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1060 ; 5.623 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 429 ;36.353 ;23.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1583 ;15.665 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 71 ;13.790 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1319 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9892 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2041 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4252 ; 0.821 ; 2.588
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4251 ; 0.821 ; 2.588
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5308 ; 1.528 ; 3.878
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5309 ; 1.528 ; 3.878
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4623 ; 0.447 ; 2.622
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4619 ; 0.445 ; 2.620
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6694 ; 0.898 ; 3.913
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9840 ; 2.640 ;19.728
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9841 ; 2.640 ;19.732
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 37 A 352
REMARK 3 RESIDUE RANGE : A 400 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2408 -4.3559 47.5130
REMARK 3 T TENSOR
REMARK 3 T11: 1.2630 T22: 0.6795
REMARK 3 T33: 0.0470 T12: 0.1311
REMARK 3 T13: -0.0577 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 1.3164 L22: 0.5474
REMARK 3 L33: 1.3506 L12: 0.3761
REMARK 3 L13: 0.5052 L23: 0.1504
REMARK 3 S TENSOR
REMARK 3 S11: -0.0634 S12: 0.0372 S13: 0.1428
REMARK 3 S21: 0.1014 S22: 0.0779 S23: 0.1378
REMARK 3 S31: 0.1646 S32: 0.2476 S33: -0.0144
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 12 B 881
REMARK 3 RESIDUE RANGE : B 901 B 901
REMARK 3 RESIDUE RANGE : B 902 B 902
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4864 10.0429 12.7198
REMARK 3 T TENSOR
REMARK 3 T11: 1.3232 T22: 0.6266
REMARK 3 T33: 0.0553 T12: -0.1094
REMARK 3 T13: -0.1474 T23: -0.0284
REMARK 3 L TENSOR
REMARK 3 L11: 0.3321 L22: 0.0956
REMARK 3 L33: 1.2077 L12: -0.0123
REMARK 3 L13: 0.0773 L23: -0.0053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0258 S12: 0.0292 S13: 0.0800
REMARK 3 S21: -0.0445 S22: -0.0679 S23: 0.0398
REMARK 3 S31: -0.1162 S32: 0.3058 S33: 0.0936
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 4QJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086120.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : KOHZU MONOCHROMATOR, CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22003
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6950
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049
REMARK 200 STARTING MODEL: PDB ENTRY 3OHM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 200 MM NACL, 5% (V/V) PEG
REMARK 280 3350, PH 6.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 102.95900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.93450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 102.95900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.93450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
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 MET A -19
REMARK 465 SER A -18
REMARK 465 TYR A -17
REMARK 465 TYR A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 ASP A -9
REMARK 465 TYR A -8
REMARK 465 ASP A -7
REMARK 465 ILE A -6
REMARK 465 PRO A -5
REMARK 465 THR A -4
REMARK 465 THR A -3
REMARK 465 GLU A -2
REMARK 465 ASN A -1
REMARK 465 LEU A 0
REMARK 465 TYR A 1
REMARK 465 PHE A 2
REMARK 465 GLN A 3
REMARK 465 GLY A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 MET A 7
REMARK 465 ALA A 8
REMARK 465 CYS A 9
REMARK 465 CYS A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 ALA A 15
REMARK 465 LYS A 16
REMARK 465 GLU A 17
REMARK 465 ALA A 18
REMARK 465 ARG A 19
REMARK 465 ARG A 20
REMARK 465 ILE A 21
REMARK 465 ASN A 22
REMARK 465 ASP A 23
REMARK 465 GLU A 24
REMARK 465 ILE A 25
REMARK 465 GLU A 26
REMARK 465 ARG A 27
REMARK 465 GLN A 28
REMARK 465 LEU A 29
REMARK 465 ARG A 30
REMARK 465 ARG A 31
REMARK 465 ASP A 32
REMARK 465 LYS A 33
REMARK 465 ARG A 34
REMARK 465 ASP A 35
REMARK 465 LEU A 353
REMARK 465 LYS A 354
REMARK 465 GLU A 355
REMARK 465 TYR A 356
REMARK 465 ASN A 357
REMARK 465 LEU A 358
REMARK 465 VAL A 359
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 GLY B 8
REMARK 465 THR B 9
REMARK 465 ALA B 10
REMARK 465 LEU B 11
REMARK 465 PHE B 92
REMARK 465 GLY B 93
REMARK 465 GLY B 94
REMARK 465 PRO B 95
REMARK 465 ASP B 96
REMARK 465 PRO B 570
REMARK 465 LYS B 571
REMARK 465 LYS B 572
REMARK 465 PRO B 573
REMARK 465 THR B 574
REMARK 465 THR B 575
REMARK 465 ASP B 576
REMARK 465 GLU B 577
REMARK 465 GLY B 578
REMARK 465 THR B 579
REMARK 465 ALA B 580
REMARK 465 SER B 581
REMARK 465 SER B 582
REMARK 465 GLU B 583
REMARK 465 VAL B 584
REMARK 465 ASN B 585
REMARK 465 ALA B 586
REMARK 465 THR B 587
REMARK 465 GLU B 588
REMARK 465 GLU B 882
REMARK 465 SER B 883
REMARK 465 GLU B 884
REMARK 465 ALA B 885
REMARK 465 GLN B 886
REMARK 465 ALA B 887
REMARK 465 GLY B 888
REMARK 465 GLN B 889
REMARK 465 GLU B 890
REMARK 465 THR B 891
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 401 O HOH A 501 1.83
REMARK 500 O3B GDP A 400 AL ALF A 401 1.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 98 53.97 71.37
REMARK 500 TYR A 151 -157.77 -119.99
REMARK 500 SER A 154 154.57 -46.33
REMARK 500 SER A 171 31.78 -141.94
REMARK 500 GLU A 234 33.03 -88.80
REMARK 500 LYS A 252 -71.46 -53.96
REMARK 500 HIS A 327 124.30 -174.57
REMARK 500 GLU B 34 -76.62 -83.17
REMARK 500 SER B 36 80.49 57.84
REMARK 500 PRO B 57 90.09 -58.73
REMARK 500 ASP B 126 8.27 53.70
REMARK 500 ASN B 141 122.48 -32.66
REMARK 500 PHE B 179 60.58 -106.81
REMARK 500 SER B 180 41.56 -85.03
REMARK 500 ASP B 182 70.12 -173.93
REMARK 500 PHE B 208 68.57 -103.72
REMARK 500 ARG B 223 75.25 -116.86
REMARK 500 ALA B 235 80.48 -163.68
REMARK 500 LYS B 253 -40.83 -152.80
REMARK 500 GLN B 290 -164.37 -122.28
REMARK 500 ASN B 305 40.50 -87.65
REMARK 500 LEU B 315 77.96 -100.18
REMARK 500 ASN B 333 63.51 35.13
REMARK 500 ALA B 338 -79.77 -171.79
REMARK 500 GLU B 372 -157.83 -92.12
REMARK 500 GLU B 373 39.94 -166.03
REMARK 500 PHE B 381 74.42 33.37
REMARK 500 THR B 382 -120.10 -115.68
REMARK 500 SER B 404 121.98 -175.80
REMARK 500 SER B 418 116.38 -162.70
REMARK 500 ASN B 595 -84.73 -142.23
REMARK 500 LYS B 603 -62.03 -101.94
REMARK 500 ASN B 612 73.07 53.97
REMARK 500 LEU B 679 66.39 -110.95
REMARK 500 SER B 711 136.60 -172.10
REMARK 500 THR B 716 105.41 -57.10
REMARK 500 GLN B 768 -52.00 -28.81
REMARK 500 ASN B 773 53.74 -147.44
REMARK 500 ASP B 777 66.82 -113.26
REMARK 500 GLU B 801 103.60 -54.02
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 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 53 OG
REMARK 620 2 THR A 186 OG1 84.6
REMARK 620 3 GDP A 400 O2B 88.7 152.8
REMARK 620 4 GDP A 400 O2A 116.7 130.2 76.1
REMARK 620 5 HOH A 502 O 59.3 78.2 75.7 151.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 333 OD1
REMARK 620 2 GLU B 362 OE2 94.7
REMARK 620 3 ASP B 364 OD2 90.4 148.7
REMARK 620 4 ASP B 364 OD1 106.4 92.9 56.2
REMARK 620 5 GLU B 413 OE1 165.7 80.7 100.6 87.5
REMARK 620 6 I3P B 902 O11 76.0 100.5 110.8 166.3 91.4
REMARK 620 7 I3P B 902 O2 109.1 61.2 144.5 137.1 56.7 50.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3P B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QJ3 RELATED DB: PDB
REMARK 900 RELATED ID: 4QJ4 RELATED DB: PDB
DBREF 4QJ5 A 7 359 UNP P21279 GNAQ_MOUSE 7 359
DBREF 4QJ5 B 10 470 UNP Q01970 PLCB3_HUMAN 10 470
DBREF 4QJ5 B 570 891 UNP Q01970 PLCB3_HUMAN 570 891
SEQADV 4QJ5 MET A -19 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 SER A -18 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 TYR A -17 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 TYR A -16 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 HIS A -15 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 HIS A -14 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 HIS A -13 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 HIS A -12 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 HIS A -11 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 HIS A -10 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 ASP A -9 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 TYR A -8 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 ASP A -7 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 ILE A -6 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 PRO A -5 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 THR A -4 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 THR A -3 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 GLU A -2 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 ASN A -1 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 LEU A 0 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 TYR A 1 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 PHE A 2 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 GLN A 3 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 GLY A 4 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 ALA A 5 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 ALA A 6 UNP P21279 EXPRESSION TAG
SEQADV 4QJ5 MET B 0 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 ALA B 1 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 HIS B 2 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 HIS B 3 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 HIS B 4 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 HIS B 5 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 HIS B 6 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 HIS B 7 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 GLY B 8 UNP Q01970 EXPRESSION TAG
SEQADV 4QJ5 THR B 9 UNP Q01970 EXPRESSION TAG
SEQRES 1 A 379 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 379 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ALA
SEQRES 3 A 379 MET ALA CYS CYS LEU SER GLU GLU ALA LYS GLU ALA ARG
SEQRES 4 A 379 ARG ILE ASN ASP GLU ILE GLU ARG GLN LEU ARG ARG ASP
SEQRES 5 A 379 LYS ARG ASP ALA ARG ARG GLU LEU LYS LEU LEU LEU LEU
SEQRES 6 A 379 GLY THR GLY GLU SER GLY LYS SER THR PHE ILE LYS GLN
SEQRES 7 A 379 MET ARG ILE ILE HIS GLY SER GLY TYR SER ASP GLU ASP
SEQRES 8 A 379 LYS ARG GLY PHE THR LYS LEU VAL TYR GLN ASN ILE PHE
SEQRES 9 A 379 THR ALA MET GLN ALA MET ILE ARG ALA MET ASP THR LEU
SEQRES 10 A 379 LYS ILE PRO TYR LYS TYR GLU HIS ASN LYS ALA HIS ALA
SEQRES 11 A 379 GLN LEU VAL ARG GLU VAL ASP VAL GLU LYS VAL SER ALA
SEQRES 12 A 379 PHE GLU ASN PRO TYR VAL ASP ALA ILE LYS SER LEU TRP
SEQRES 13 A 379 ASN ASP PRO GLY ILE GLN GLU CYS TYR ASP ARG ARG ARG
SEQRES 14 A 379 GLU TYR GLN LEU SER ASP SER THR LYS TYR TYR LEU ASN
SEQRES 15 A 379 ASP LEU ASP ARG VAL ALA ASP PRO SER TYR LEU PRO THR
SEQRES 16 A 379 GLN GLN ASP VAL LEU ARG VAL ARG VAL PRO THR THR GLY
SEQRES 17 A 379 ILE ILE GLU TYR PRO PHE ASP LEU GLN SER VAL ILE PHE
SEQRES 18 A 379 ARG MET VAL ASP VAL GLY GLY GLN ARG SER GLU ARG ARG
SEQRES 19 A 379 LYS TRP ILE HIS CYS PHE GLU ASN VAL THR SER ILE MET
SEQRES 20 A 379 PHE LEU VAL ALA LEU SER GLU TYR ASP GLN VAL LEU VAL
SEQRES 21 A 379 GLU SER ASP ASN GLU ASN ARG MET GLU GLU SER LYS ALA
SEQRES 22 A 379 LEU PHE ARG THR ILE ILE THR TYR PRO TRP PHE GLN ASN
SEQRES 23 A 379 SER SER VAL ILE LEU PHE LEU ASN LYS LYS ASP LEU LEU
SEQRES 24 A 379 GLU GLU LYS ILE MET TYR SER HIS LEU VAL ASP TYR PHE
SEQRES 25 A 379 PRO GLU TYR ASP GLY PRO GLN ARG ASP ALA GLN ALA ALA
SEQRES 26 A 379 ARG GLU PHE ILE LEU LYS MET PHE VAL ASP LEU ASN PRO
SEQRES 27 A 379 ASP SER ASP LYS ILE ILE TYR SER HIS PHE THR CYS ALA
SEQRES 28 A 379 THR ASP THR GLU ASN ILE ARG PHE VAL PHE ALA ALA VAL
SEQRES 29 A 379 LYS ASP THR ILE LEU GLN LEU ASN LEU LYS GLU TYR ASN
SEQRES 30 A 379 LEU VAL
SEQRES 1 B 793 MET ALA HIS HIS HIS HIS HIS HIS GLY THR ALA LEU GLN
SEQRES 2 B 793 LEU GLU PRO PRO THR VAL VAL GLU THR LEU ARG ARG GLY
SEQRES 3 B 793 SER LYS PHE ILE LYS TRP ASP GLU GLU THR SER SER ARG
SEQRES 4 B 793 ASN LEU VAL THR LEU ARG VAL ASP PRO ASN GLY PHE PHE
SEQRES 5 B 793 LEU TYR TRP THR GLY PRO ASN MET GLU VAL ASP THR LEU
SEQRES 6 B 793 ASP ILE SER SER ILE ARG ASP THR ARG THR GLY ARG TYR
SEQRES 7 B 793 ALA ARG LEU PRO LYS ASP PRO LYS ILE ARG GLU VAL LEU
SEQRES 8 B 793 GLY PHE GLY GLY PRO ASP ALA ARG LEU GLU GLU LYS LEU
SEQRES 9 B 793 MET THR VAL VAL SER GLY PRO ASP PRO VAL ASN THR VAL
SEQRES 10 B 793 PHE LEU ASN PHE MET ALA VAL GLN ASP ASP THR ALA LYS
SEQRES 11 B 793 VAL TRP SER GLU GLU LEU PHE LYS LEU ALA MET ASN ILE
SEQRES 12 B 793 LEU ALA GLN ASN ALA SER ARG ASN THR PHE LEU ARG LYS
SEQRES 13 B 793 ALA TYR THR LYS LEU LYS LEU GLN VAL ASN GLN ASP GLY
SEQRES 14 B 793 ARG ILE PRO VAL LYS ASN ILE LEU LYS MET PHE SER ALA
SEQRES 15 B 793 ASP LYS LYS ARG VAL GLU THR ALA LEU GLU SER CYS GLY
SEQRES 16 B 793 LEU LYS PHE ASN ARG SER GLU SER ILE ARG PRO ASP GLU
SEQRES 17 B 793 PHE SER LEU GLU ILE PHE GLU ARG PHE LEU ASN LYS LEU
SEQRES 18 B 793 CYS LEU ARG PRO ASP ILE ASP LYS ILE LEU LEU GLU ILE
SEQRES 19 B 793 GLY ALA LYS GLY LYS PRO TYR LEU THR LEU GLU GLN LEU
SEQRES 20 B 793 MET ASP PHE ILE ASN GLN LYS GLN ARG ASP PRO ARG LEU
SEQRES 21 B 793 ASN GLU VAL LEU TYR PRO PRO LEU ARG PRO SER GLN ALA
SEQRES 22 B 793 ARG LEU LEU ILE GLU LYS TYR GLU PRO ASN GLN GLN PHE
SEQRES 23 B 793 LEU GLU ARG ASP GLN MET SER MET GLU GLY PHE SER ARG
SEQRES 24 B 793 TYR LEU GLY GLY GLU GLU ASN GLY ILE LEU PRO LEU GLU
SEQRES 25 B 793 ALA LEU ASP LEU SER THR ASP MET THR GLN PRO LEU SER
SEQRES 26 B 793 ALA TYR PHE ILE ASN SER SER HIS ASN THR TYR LEU THR
SEQRES 27 B 793 ALA GLY GLN LEU ALA GLY THR SER SER VAL GLU MET TYR
SEQRES 28 B 793 ARG GLN ALA LEU LEU TRP GLY CYS ARG CYS VAL GLU LEU
SEQRES 29 B 793 ASP VAL TRP LYS GLY ARG PRO PRO GLU GLU GLU PRO PHE
SEQRES 30 B 793 ILE THR HIS GLY PHE THR MET THR THR GLU VAL PRO LEU
SEQRES 31 B 793 ARG ASP VAL LEU GLU ALA ILE ALA GLU THR ALA PHE LYS
SEQRES 32 B 793 THR SER PRO TYR PRO VAL ILE LEU SER PHE GLU ASN HIS
SEQRES 33 B 793 VAL ASP SER ALA LYS GLN GLN ALA LYS MET ALA GLU TYR
SEQRES 34 B 793 CYS ARG SER ILE PHE GLY ASP ALA LEU LEU ILE GLU PRO
SEQRES 35 B 793 LEU ASP LYS TYR PRO LEU ALA PRO GLY VAL PRO LEU PRO
SEQRES 36 B 793 SER PRO GLN ASP LEU MET GLY ARG ILE LEU VAL LYS ASN
SEQRES 37 B 793 LYS LYS ARG PRO LYS LYS PRO THR THR ASP GLU GLY THR
SEQRES 38 B 793 ALA SER SER GLU VAL ASN ALA THR GLU GLU MET SER THR
SEQRES 39 B 793 LEU VAL ASN TYR ILE GLU PRO VAL LYS PHE LYS SER PHE
SEQRES 40 B 793 GLU ALA ALA ARG LYS ARG ASN LYS CYS PHE GLU MET SER
SEQRES 41 B 793 SER PHE VAL GLU THR LYS ALA MET GLU GLN LEU THR LYS
SEQRES 42 B 793 SER PRO MET GLU PHE VAL GLU TYR ASN LYS GLN GLN LEU
SEQRES 43 B 793 SER ARG ILE TYR PRO LYS GLY THR ARG VAL ASP SER SER
SEQRES 44 B 793 ASN TYR MET PRO GLN LEU PHE TRP ASN VAL GLY CYS GLN
SEQRES 45 B 793 LEU VAL ALA LEU ASN PHE GLN THR LEU ASP VAL ALA MET
SEQRES 46 B 793 GLN LEU ASN ALA GLY VAL PHE GLU TYR ASN GLY ARG SER
SEQRES 47 B 793 GLY TYR LEU LEU LYS PRO GLU PHE MET ARG ARG PRO ASP
SEQRES 48 B 793 LYS SER PHE ASP PRO PHE THR GLU VAL ILE VAL ASP GLY
SEQRES 49 B 793 ILE VAL ALA ASN ALA LEU ARG VAL LYS VAL ILE SER GLY
SEQRES 50 B 793 GLN PHE LEU SER ASP ARG LYS VAL GLY ILE TYR VAL GLU
SEQRES 51 B 793 VAL ASP MET PHE GLY LEU PRO VAL ASP THR ARG ARG LYS
SEQRES 52 B 793 TYR ARG THR ARG THR SER GLN GLY ASN SER PHE ASN PRO
SEQRES 53 B 793 VAL TRP ASP GLU GLU PRO PHE ASP PHE PRO LYS VAL VAL
SEQRES 54 B 793 LEU PRO THR LEU ALA SER LEU ARG ILE ALA ALA PHE GLU
SEQRES 55 B 793 GLU GLY GLY LYS PHE VAL GLY HIS ARG ILE LEU PRO VAL
SEQRES 56 B 793 SER ALA ILE ARG SER GLY TYR HIS TYR VAL CYS LEU ARG
SEQRES 57 B 793 ASN GLU ALA ASN GLN PRO LEU CYS LEU PRO ALA LEU LEU
SEQRES 58 B 793 ILE TYR THR GLU ALA SER ASP TYR ILE PRO ASP ASP HIS
SEQRES 59 B 793 GLN ASP TYR ALA GLU ALA LEU ILE ASN PRO ILE LYS HIS
SEQRES 60 B 793 VAL SER LEU MET ASP GLN ARG ALA ARG GLN LEU ALA ALA
SEQRES 61 B 793 LEU ILE GLY GLU SER GLU ALA GLN ALA GLY GLN GLU THR
HET GDP A 400 28
HET ALF A 401 5
HET MG A 402 1
HET CA B 901 1
HET I3P B 902 24
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM ALF TETRAFLUOROALUMINATE ION
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
HETNAM I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 ALF AL F4 1-
FORMUL 5 MG MG 2+
FORMUL 6 CA CA 2+
FORMUL 7 I3P C6 H15 O15 P3
FORMUL 8 HOH *2(H2 O)
HELIX 1 1 GLY A 51 HIS A 63 1 13
HELIX 2 2 SER A 68 LYS A 98 1 31
HELIX 3 3 GLU A 104 GLU A 115 1 12
HELIX 4 4 ASP A 117 VAL A 121 5 5
HELIX 5 5 PRO A 127 ASN A 137 1 11
HELIX 6 6 ASP A 138 ARG A 147 1 10
HELIX 7 7 ARG A 148 TYR A 151 5 4
HELIX 8 8 SER A 156 ASN A 162 1 7
HELIX 9 9 ASP A 163 ASP A 169 1 7
HELIX 10 10 THR A 175 VAL A 182 1 8
HELIX 11 11 ARG A 210 PHE A 220 5 11
HELIX 12 12 SER A 233 GLN A 237 5 5
HELIX 13 13 ASN A 246 ILE A 259 1 14
HELIX 14 14 THR A 260 GLN A 265 5 6
HELIX 15 15 LYS A 275 ILE A 283 1 9
HELIX 16 16 HIS A 287 TYR A 291 5 5
HELIX 17 17 ASP A 301 ASP A 315 1 15
HELIX 18 18 ASP A 333 GLN A 350 1 18
HELIX 19 19 GLU B 20 GLY B 25 1 6
HELIX 20 20 PRO B 57 MET B 59 5 3
HELIX 21 21 ARG B 76 ALA B 78 5 3
HELIX 22 22 ASP B 83 GLY B 91 1 9
HELIX 23 23 LEU B 99 GLU B 101 5 3
HELIX 24 24 ASP B 126 ASN B 141 1 16
HELIX 25 25 ASN B 141 ASN B 146 1 6
HELIX 26 26 SER B 148 GLN B 163 1 16
HELIX 27 27 VAL B 172 PHE B 179 1 8
HELIX 28 28 ASP B 182 CYS B 193 1 12
HELIX 29 29 ARG B 204 PHE B 208 5 5
HELIX 30 30 SER B 209 CYS B 221 1 13
HELIX 31 31 ARG B 223 GLY B 234 1 12
HELIX 32 32 THR B 242 LYS B 253 1 12
HELIX 33 33 ARG B 268 TYR B 279 1 12
HELIX 34 34 ASN B 282 ARG B 288 1 7
HELIX 35 35 SER B 292 GLY B 301 1 10
HELIX 36 36 PRO B 309 ASP B 314 1 6
HELIX 37 37 PRO B 322 SER B 324 5 3
HELIX 38 38 VAL B 347 LEU B 355 1 9
HELIX 39 39 LEU B 389 ALA B 400 1 12
HELIX 40 40 SER B 418 PHE B 433 1 16
HELIX 41 41 PRO B 456 MET B 460 5 5
HELIX 42 42 GLU B 589 LEU B 593 5 5
HELIX 43 43 SER B 604 ASN B 612 1 9
HELIX 44 44 GLU B 622 SER B 632 1 11
HELIX 45 45 SER B 632 LYS B 641 1 10
HELIX 46 46 PRO B 661 ASN B 666 1 6
HELIX 47 47 ASP B 680 PHE B 690 1 11
HELIX 48 48 PRO B 849 ASP B 851 5 3
HELIX 49 49 HIS B 852 ASN B 861 1 10
HELIX 50 50 ASN B 861 GLY B 881 1 21
SHEET 1 A 6 ILE A 189 ASP A 195 0
SHEET 2 A 6 ILE A 200 VAL A 206 -1 O ASP A 205 N ILE A 190
SHEET 3 A 6 GLU A 39 GLY A 46 1 N LEU A 42 O VAL A 204
SHEET 4 A 6 SER A 225 ALA A 231 1 O SER A 225 N LEU A 43
SHEET 5 A 6 SER A 268 ASN A 274 1 O ASN A 274 N VAL A 230
SHEET 6 A 6 ILE A 324 PHE A 328 1 O HIS A 327 N LEU A 273
SHEET 1 B 7 VAL B 61 ASP B 65 0
SHEET 2 B 7 PHE B 51 THR B 55 -1 N LEU B 52 O LEU B 64
SHEET 3 B 7 ARG B 38 VAL B 45 -1 N ARG B 44 O TYR B 53
SHEET 4 B 7 SER B 26 TRP B 31 -1 N PHE B 28 O VAL B 41
SHEET 5 B 7 VAL B 116 ALA B 122 -1 O MET B 121 N ILE B 29
SHEET 6 B 7 LEU B 103 SER B 108 -1 N VAL B 106 O LEU B 118
SHEET 7 B 7 ILE B 69 THR B 74 -1 N ARG B 70 O VAL B 107
SHEET 1 C 2 ILE B 170 PRO B 171 0
SHEET 2 C 2 SER B 202 ILE B 203 -1 O ILE B 203 N ILE B 170
SHEET 1 D 6 GLU B 598 PRO B 599 0
SHEET 2 D 6 GLU B 616 VAL B 621 1 O MET B 617 N GLU B 598
SHEET 3 D 6 SER B 645 TYR B 648 1 O ARG B 646 N PHE B 620
SHEET 4 D 6 LEU B 671 LEU B 674 1 O ALA B 673 N ILE B 647
SHEET 5 D 6 TYR B 326 SER B 331 1 N SER B 330 O LEU B 674
SHEET 6 D 6 TYR B 698 LEU B 700 -1 O LEU B 699 N PHE B 327
SHEET 1 E 2 ALA B 342 GLY B 343 0
SHEET 2 E 2 MET B 383 THR B 384 1 O MET B 383 N GLY B 343
SHEET 1 F 5 VAL B 387 PRO B 388 0
SHEET 2 F 5 PHE B 376 ILE B 377 -1 N ILE B 377 O VAL B 387
SHEET 3 F 5 CYS B 360 TRP B 366 -1 N TRP B 366 O PHE B 376
SHEET 4 F 5 VAL B 408 ASN B 414 1 O SER B 411 N VAL B 361
SHEET 5 F 5 ILE B 463 LYS B 466 1 O LEU B 464 N VAL B 408
SHEET 1 G 4 PHE B 781 VAL B 786 0
SHEET 2 G 4 ASN B 726 GLN B 736 -1 N LEU B 728 O PHE B 783
SHEET 3 G 4 PRO B 832 ASP B 846 -1 O SER B 845 N ALA B 727
SHEET 4 G 4 GLY B 819 ARG B 826 -1 N GLY B 819 O THR B 842
SHEET 1 H 4 TYR B 762 ARG B 763 0
SHEET 2 H 4 ILE B 745 PHE B 752 -1 N VAL B 749 O TYR B 762
SHEET 3 H 4 SER B 793 GLU B 800 -1 O PHE B 799 N TYR B 746
SHEET 4 H 4 PHE B 805 PRO B 812 -1 O LEU B 811 N LEU B 794
LINK OG SER A 53 MG MG A 402 1555 1555 2.19
LINK OG1 THR A 186 MG MG A 402 1555 1555 2.18
LINK O2B GDP A 400 MG MG A 402 1555 1555 2.18
LINK O2A GDP A 400 MG MG A 402 1555 1555 2.88
LINK MG MG A 402 O HOH A 502 1555 1555 2.42
LINK OD1 ASN B 333 CA CA B 901 1555 1555 2.32
LINK OE2 GLU B 362 CA CA B 901 1555 1555 2.32
LINK OD2 ASP B 364 CA CA B 901 1555 1555 2.32
LINK OD1 ASP B 364 CA CA B 901 1555 1555 2.33
LINK OE1 GLU B 413 CA CA B 901 1555 1555 2.32
LINK CA CA B 901 O11 I3P B 902 1555 1555 2.46
LINK CA CA B 901 O2 I3P B 902 1555 1555 3.07
CISPEP 1 ASN A 126 PRO A 127 0 3.94
SITE 1 AC1 20 GLU A 49 SER A 50 GLY A 51 LYS A 52
SITE 2 AC1 20 SER A 53 THR A 54 LEU A 180 ARG A 181
SITE 3 AC1 20 VAL A 182 ARG A 183 ASN A 274 LYS A 275
SITE 4 AC1 20 ASP A 277 LEU A 278 CYS A 330 ALA A 331
SITE 5 AC1 20 THR A 332 ALF A 401 MG A 402 HOH A 502
SITE 1 AC2 13 GLY A 48 GLU A 49 LYS A 52 ARG A 183
SITE 2 AC2 13 PRO A 185 THR A 186 VAL A 206 GLY A 208
SITE 3 AC2 13 GLN A 209 GDP A 400 MG A 402 HOH A 501
SITE 4 AC2 13 HOH A 502
SITE 1 AC3 5 SER A 53 THR A 186 GDP A 400 ALF A 401
SITE 2 AC3 5 HOH A 502
SITE 1 AC4 5 ASN B 333 GLU B 362 ASP B 364 GLU B 413
SITE 2 AC4 5 I3P B 902
SITE 1 AC5 9 HIS B 332 ASN B 333 GLU B 362 HIS B 379
SITE 2 AC5 9 GLU B 413 SER B 619 ARG B 646 TYR B 648
SITE 3 AC5 9 CA B 901
CRYST1 205.918 89.869 93.261 90.00 101.80 90.00 C 1 2 1 4
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 0.004856 0.000000 0.001015 0.00000
SCALE2 0.000000 0.011127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
