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PDBsum entry 2cjw

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Top Page protein ligands metals Protein-protein interface(s) links
G-protein PDB id
2cjw
Jmol
Contents
Protein chains
178 a.a.
173 a.a.
Ligands
GDP ×2
Metals
_MG ×2
Waters ×127
HEADER    G-PROTEIN                               09-APR-06   2CJW
TITLE     CRYSTAL STRUCTURE OF THE SMALL GTPASE GEM (GEMDNDCAM) IN
TITLE    2 COMPLEX TO MG.GDP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GTP-BINDING PROTEIN GEM;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: G DOMAIN, RESIDUES 74-261;
COMPND   5 SYNONYM: GEM, GTP-BINDING MITOGEN-INDUCED T-CELL PROTEIN,
COMPND   6  RAS-LIKE PROTEIN KIR;
COMPND   7 ENGINEERED: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: GTP-BINDING PROTEIN GEM;
COMPND  10 CHAIN: B;
COMPND  11 FRAGMENT: G DOMAIN, RESIDUES 74-261;
COMPND  12 SYNONYM: GEM, GTP-BINDING MITOGEN-INDUCED T-CELL PROTEIN,
COMPND  13  RAS-LIKE PROTEIN KIR;
COMPND  14 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 MOL_ID: 2;
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   9 ORGANISM_COMMON: HUMAN;
SOURCE  10 ORGANISM_TAXID: 9606;
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    G-PROTEIN, NUCLEOTIDE-BINDING, GTP-BINDING, SMALL GTPASE,
KEYWDS   2 CONFORMATIONAL CHANGE, CYSTEINE-MODIFIED, G-PROTEIN
KEYWDS   3 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.SPLINGARD,J.MENETREY,M.PERDERISET,J.CICOLARI,F.HAMOUDI,
AUTHOR   2 L.CABANIE,A.EL MARJOU,A.WELLS,A.HOUDUSSE,J.DE GUNZBURG
REVDAT   2   24-FEB-09 2CJW    1       VERSN
REVDAT   1   09-NOV-06 2CJW    0
JRNL        AUTH   A.SPLINGARD,J.MENETREY,M.PERDERISET,J.CICOLARI,
JRNL        AUTH 2 K.REGAZZONI,F.HAMOUDI,L.CABANIE,A.EL MARJOU,
JRNL        AUTH 3 A.WELLS,A.HOUDUSSE,J.DE GUNZBURG
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF THE
JRNL        TITL 2 GEM GTPASE.
JRNL        REF    J.BIOL.CHEM.                  V. 282  1905 2007
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   17107948
JRNL        DOI    10.1074/JBC.M604363200
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 33159
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) : 0.212
REMARK   3   R VALUE            (WORKING SET) : 0.209
REMARK   3   FREE R VALUE                     : 0.241
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3669
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2480
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250
REMARK   3   BIN FREE R VALUE SET COUNT          : 260
REMARK   3   BIN FREE R VALUE                    : 0.2440
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2795
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 113
REMARK   3   SOLVENT ATOMS            : 127
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.22
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.20000
REMARK   3    B22 (A**2) : 1.20000
REMARK   3    B33 (A**2) : -1.79000
REMARK   3    B12 (A**2) : 0.60000
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): 0.168
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.156
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.452
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2841 ; 0.010 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3827 ; 1.271 ; 1.991
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   345 ; 5.589 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   133 ;33.153 ;22.932
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   494 ;14.843 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;13.912 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   428 ; 0.089 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2086 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1219 ; 0.204 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1925 ; 0.299 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   137 ; 0.137 ; 0.200
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):    52 ; 0.210 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.226 ; 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):  1786 ; 1.199 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2741 ; 1.423 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1230 ; 1.886 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1086 ; 2.894 ; 4.500
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  : NULL
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
REMARK   3  RIDING POSITIONS. RESIDUES 102-105 AND 136-139 IN MOLECULE A
REMARK   3  AND RESIDUES 99-110 AND 136-142 IN MOLECULE B WERE DISORDERED
REMARK   3  AND NOT MODELED. SOME SIDE-CHAINS WERE MODELED WITH 0.0 OR
REMARK   3  PARTIAL OCCUPANCY RATE.
REMARK   4
REMARK   4 2CJW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-APR-06.
REMARK 100 THE PDBE ID CODE IS EBI-28441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96115
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36826
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 7.700
REMARK 200  R MERGE                    (I) : 0.08600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.34200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1KAO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 66.3
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NACACODYLATE PH6.5, 0.9M
REMARK 280  NAACETATE, 5MM MGCL2 AND 2MM DTT
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
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       27.13633
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       54.27267
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.70450
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       67.84083
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       13.56817
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 GENERATING THE BIOMOLECULE
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: PQS
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     GLU A    70
REMARK 465     PHE A    71
REMARK 465     GLY A    72
REMARK 465     MET A   102
REMARK 465     ASP A   103
REMARK 465     SER A   104
REMARK 465     ASP A   105
REMARK 465     LYS A   136
REMARK 465     GLY A   137
REMARK 465     GLU A   138
REMARK 465     ASN A   139
REMARK 465     LYS A   259
REMARK 465     GLU A   260
REMARK 465     SER A   261
REMARK 465     HIS B    99
REMARK 465     ASP B   100
REMARK 465     SER B   101
REMARK 465     MET B   102
REMARK 465     ASP B   103
REMARK 465     SER B   104
REMARK 465     ASP B   105
REMARK 465     CAS B   106
REMARK 465     GLU B   107
REMARK 465     VAL B   108
REMARK 465     LEU B   109
REMARK 465     GLY B   110
REMARK 465     LYS B   136
REMARK 465     GLY B   137
REMARK 465     GLU B   138
REMARK 465     ASN B   139
REMARK 465     GLU B   140
REMARK 465     TRP B   141
REMARK 465     LEU B   142
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480   M RES CSSEQI  ATOMS
REMARK 480     ASP A 100    CB   CG  OD1  OD2
REMARK 480     SER A 101    CB   OG
REMARK 480     GLU A 107    CB   CG   CD  OE1  OE2
REMARK 480     ASN A 135    CB   CG  OD1  ND2
REMARK 480     GLN A 180    CB   CG   CD  OE1  NE2
REMARK 480     ARG A 197    CG   CD   NE   CZ  NH1  NH2
REMARK 480     LYS A 246    CB   CG   CD   CE   NZ
REMARK 480     GLU A 247    CB   CG   CD  OE1  OE2
REMARK 480     GLU A 250    CB   CG   CD  OE1  OE2
REMARK 480     LYS A 257    CB   CG   CD   CE   NZ
REMARK 480     ARG A 258    CB   CG   CD   NE   CZ  NH1  NH2
REMARK 480     GLU B 134    CB   CG   CD  OE1  OE2
REMARK 480     ASN B 135    CB   CG  OD1  ND2
REMARK 480     HIS B 143    CB   CG  ND1  CD2  CE1  NE2
REMARK 480     GLU B 170    CB   CG   CD  OE1  OE2
REMARK 480     ARG B 177    CG   CD   NE   CZ  NH1  NH2
REMARK 480     ARG B 197    CG   CD   NE   CZ  NH1  NH2
REMARK 480     LYS B 248    CG   CD   CE   NZ
REMARK 480     ARG B 251    CG   CD   NE   CZ  NH1  NH2
REMARK 480     GLU B 260    CB   CG   CD  OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A  83   CB A  GLU A  83   CG A    0.116
REMARK 500    ASP A 100   CA    ASP A 100   CB      0.196
REMARK 500    GLN A 180   CA    GLN A 180   CB     -0.188
REMARK 500    LYS A 246   CA    LYS A 246   CB     -0.371
REMARK 500    LYS A 257   CA    LYS A 257   CB      0.136
REMARK 500    ARG A 258   CA    ARG A 258   CB     -0.323
REMARK 500    HIS B 143   CA    HIS B 143   CB     -0.255
REMARK 500    LYS B 248   CB    LYS B 248   CG     -0.198
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    GLU A 107   N   -  CA  -  CB  ANGL. DEV. = -13.1 DEGREES
REMARK 500    ASN A 135   CB  -  CA  -  C   ANGL. DEV. =  15.6 DEGREES
REMARK 500    LYS A 246   CB  -  CA  -  C   ANGL. DEV. =  20.3 DEGREES
REMARK 500    LYS A 257   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES
REMARK 500    LYS A 257   CB  -  CA  -  C   ANGL. DEV. =  14.8 DEGREES
REMARK 500    ARG A 258   CA  -  CB  -  CG  ANGL. DEV. = -18.6 DEGREES
REMARK 500    ARG A 258   N   -  CA  -  CB  ANGL. DEV. = -15.2 DEGREES
REMARK 500    HIS B 143   N   -  CA  -  CB  ANGL. DEV. =  20.7 DEGREES
REMARK 500    LYS B 248   CA  -  CB  -  CG  ANGL. DEV. =  17.8 DEGREES
REMARK 500    GLU B 260   CB  -  CA  -  C   ANGL. DEV. = -18.0 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 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 192       32.57     72.49
REMARK 500    GLN B 225       84.88     52.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    SER A 101         0.9      L          D   EXPECTING SP3
REMARK 500    GLN A 180        13.7      L          L   OUTSIDE RANGE
REMARK 500    LYS A 257        24.9      L          L   OUTSIDE RANGE
REMARK 500    ASN B 135        22.1      L          L   OUTSIDE RANGE
REMARK 500    HIS B 143        10.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     CAS A  198
REMARK 610     CAS A  215
REMARK 610     CAS B  198
REMARK 610     CAS B  209
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 A1000  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2008   O
REMARK 620 2 HOH A2028   O    83.9
REMARK 620 3 HOH A2081   O    90.6  95.1
REMARK 620 4 SER A  89   OG   84.2 167.0  90.2
REMARK 620 5 GDP A 999   O2B 175.1  92.8  93.3  98.8
REMARK 620 6 HOH A2024   O    84.8  87.2 174.6  86.6  91.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B1000  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2045   O
REMARK 620 2 HOH B2007   O    97.1
REMARK 620 3 GDP B 999   O2B  89.5 170.8
REMARK 620 4 HOH B2046   O    99.8  90.8  94.4
REMARK 620 5 SER B  89   OG   89.8  86.8  86.9 170.3
REMARK 620 6 HOH B2024   O   173.7  83.8  88.9  86.4  84.0
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HT6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN GEM G-DOMAIN
REMARK 900  BOUND TO GDP
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 70-72 (EFG) IN MOLECULE B BELONG TO THE REMAINING
REMARK 999 PART OF THE TAG.
DBREF  2CJW A   70    73  PDB    2CJW     2CJW            70     73
DBREF  2CJW A   74   261  UNP    P55040   GEM_HUMAN       74    261
DBREF  2CJW B   70    73  PDB    2CJW     2CJW            70     73
DBREF  2CJW B   74   261  UNP    P55040   GEM_HUMAN       74    261
SEQRES   1 A  192  GLU PHE GLY MET THR TYR TYR ARG VAL VAL LEU ILE GLY
SEQRES   2 A  192  GLU GLN GLY VAL GLY LYS SER THR LEU ALA ASN ILE PHE
SEQRES   3 A  192  ALA GLY VAL HIS ASP SER MET ASP SER ASP CAS GLU VAL
SEQRES   4 A  192  LEU GLY GLU ASP THR TYR GLU ARG THR LEU MET VAL ASP
SEQRES   5 A  192  GLY GLU SER ALA THR ILE ILE LEU LEU ASP MET TRP GLU
SEQRES   6 A  192  ASN LYS GLY GLU ASN GLU TRP LEU HIS ASP HIS CYS MET
SEQRES   7 A  192  GLN VAL GLY ASP ALA TYR LEU ILE VAL TYR SER ILE THR
SEQRES   8 A  192  ASP ARG ALA SER PHE GLU LYS ALA SER GLU LEU ARG ILE
SEQRES   9 A  192  GLN LEU ARG ARG ALA ARG GLN THR GLU ASP ILE PRO ILE
SEQRES  10 A  192  ILE LEU VAL GLY ASN LYS SER ASP LEU VAL ARG CAS ARG
SEQRES  11 A  192  GLU VAL SER VAL SER GLU GLY ARG ALA CAS ALA VAL VAL
SEQRES  12 A  192  PHE ASP CAS LYS PHE ILE GLU THR SER ALA ALA VAL GLN
SEQRES  13 A  192  HIS ASN VAL LYS GLU LEU PHE GLU GLY ILE VAL ARG GLN
SEQRES  14 A  192  VAL ARG LEU ARG ARG ASP SER LYS GLU LYS ASN GLU ARG
SEQRES  15 A  192  ARG LEU ALA TYR GLN LYS ARG LYS GLU SER
SEQRES   1 B  192  GLU PHE GLY MET THR TYR TYR ARG VAL VAL LEU ILE GLY
SEQRES   2 B  192  GLU GLN GLY VAL GLY LYS SER THR LEU ALA ASN ILE PHE
SEQRES   3 B  192  ALA GLY VAL HIS ASP SER MET ASP SER ASP CAS GLU VAL
SEQRES   4 B  192  LEU GLY GLU ASP THR TYR GLU ARG THR LEU MET VAL ASP
SEQRES   5 B  192  GLY GLU SER ALA THR ILE ILE LEU LEU ASP MET TRP GLU
SEQRES   6 B  192  ASN LYS GLY GLU ASN GLU TRP LEU HIS ASP HIS CAS MET
SEQRES   7 B  192  GLN VAL GLY ASP ALA TYR LEU ILE VAL TYR SER ILE THR
SEQRES   8 B  192  ASP ARG ALA SER PHE GLU LYS ALA SER GLU LEU ARG ILE
SEQRES   9 B  192  GLN LEU ARG ARG ALA ARG GLN THR GLU ASP ILE PRO ILE
SEQRES  10 B  192  ILE LEU VAL GLY ASN LYS SER ASP LEU VAL ARG CAS ARG
SEQRES  11 B  192  GLU VAL SER VAL SER GLU GLY ARG ALA CAS ALA VAL VAL
SEQRES  12 B  192  PHE ASP CYS LYS PHE ILE GLU THR SER ALA ALA VAL GLN
SEQRES  13 B  192  HIS ASN VAL LYS GLU LEU PHE GLU GLY ILE VAL ARG GLN
SEQRES  14 B  192  VAL ARG LEU ARG ARG ASP SER LYS GLU LYS ASN GLU ARG
SEQRES  15 B  192  ARG LEU ALA TYR GLN LYS ARG LYS GLU SER
MODRES 2CJW CAS A  106  CYS  S-(DIMETHYLARSENIC)CYSTEINE
MODRES 2CJW CAS A  198  CYS  S-(DIMETHYLARSENIC)CYSTEINE
MODRES 2CJW CAS A  209  CYS  S-(DIMETHYLARSENIC)CYSTEINE
MODRES 2CJW CAS A  215  CYS  S-(DIMETHYLARSENIC)CYSTEINE
MODRES 2CJW CAS B  146  CYS  S-(DIMETHYLARSENIC)CYSTEINE
MODRES 2CJW CAS B  198  CYS  S-(DIMETHYLARSENIC)CYSTEINE
MODRES 2CJW CAS B  209  CYS  S-(DIMETHYLARSENIC)CYSTEINE
HET    CAS  A 106       7
HET    CAS  A 198       9
HET    CAS  A 209       9
HET    CAS  A 215       7
HET    CAS  B 146       9
HET    CAS  B 198       7
HET    CAS  B 209       7
HET     MG  A1000       1
HET     MG  B1000       1
HET    GDP  A 999      28
HET    GDP  B 999      28
HETNAM     CAS S-(DIMETHYLARSENIC)CYSTEINE
HETNAM      MG MAGNESIUM ION
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL   1  CAS    7(C5 H12 AS N O2 S)
FORMUL   3   MG    2(MG 2+)
FORMUL   5  GDP    2(C10 H15 N5 O11 P2)
FORMUL   7  HOH   *127(H2 O1)
HELIX    1   1 GLY A   87  HIS A   99  1                                  13
HELIX    2   2 CAS A  106  GLY A  110  5                                   5
HELIX    3   3 LEU A  142  ASP A  144  5                                   3
HELIX    4   4 HIS A  145  GLY A  150  1                                   6
HELIX    5   5 ASP A  161  ARG A  179  1                                  19
HELIX    6   6 LEU A  195  ARG A  199  5                                   5
HELIX    7   7 SER A  202  PHE A  213  1                                  12
HELIX    8   8 ASN A  227  ASP A  244  1                                  18
HELIX    9   9 SER A  245  ARG A  258  1                                  14
HELIX   10  10 GLY B   87  GLY B   97  1                                  11
HELIX   11  11 HIS B  145  GLY B  150  1                                   6
HELIX   12  12 ASP B  161  ARG B  179  1                                  19
HELIX   13  13 LEU B  195  ARG B  199  5                                   5
HELIX   14  14 SER B  202  ASP B  214  1                                  13
HELIX   15  15 ASN B  227  ASP B  244  1                                  18
HELIX   16  16 SER B  245  SER B  261  1                                  17
SHEET    1  AA 6 THR A 113  VAL A 120  0
SHEET    2  AA 6 GLU A 123  LEU A 130 -1  O  GLU A 123   N  VAL A 120
SHEET    3  AA 6 TYR A  75  ILE A  81  1  O  TYR A  76   N  ILE A 128
SHEET    4  AA 6 ALA A 152  SER A 158  1  O  ALA A 152   N  VAL A  79
SHEET    5  AA 6 ILE A 186  ASN A 191  1  O  ILE A 187   N  ILE A 155
SHEET    6  AA 6 LYS A 216  GLU A 219  1  O  LYS A 216   N  LEU A 188
SHEET    1  BA 6 THR B 113  VAL B 120  0
SHEET    2  BA 6 GLU B 123  LEU B 130 -1  O  GLU B 123   N  VAL B 120
SHEET    3  BA 6 TYR B  75  GLY B  82  1  O  TYR B  76   N  ILE B 128
SHEET    4  BA 6 ALA B 152  SER B 158  1  O  ALA B 152   N  VAL B  79
SHEET    5  BA 6 ILE B 186  ASN B 191  1  O  ILE B 187   N  ILE B 155
SHEET    6  BA 6 LYS B 216  THR B 220  1  O  LYS B 216   N  LEU B 188
LINK         C   CAS A 106                 N   GLU A 107     1555   1555  1.34
LINK         C   ARG A 197                 N   CAS A 198     1555   1555  1.33
LINK         C   CAS A 198                 N   ARG A 199     1555   1555  1.33
LINK         C   ALA A 208                 N   CAS A 209     1555   1555  1.34
LINK         C   CAS A 209                 N   ALA A 210     1555   1555  1.34
LINK         C   ASP A 214                 N   CAS A 215     1555   1555  1.33
LINK         C   CAS A 215                 N   LYS A 216     1555   1555  1.33
LINK         O2B GDP A 999                MG    MG A1000     1555   1555  1.99
LINK        MG    MG A1000                 O   HOH A2024     1555   1555  2.03
LINK        MG    MG A1000                 OG  SER A  89     1555   1555  2.21
LINK        MG    MG A1000                 O   HOH A2081     1555   1555  2.11
LINK        MG    MG A1000                 O   HOH A2028     1555   1555  2.15
LINK        MG    MG A1000                 O   HOH A2008     1555   1555  2.27
LINK         C   HIS B 145                 N   CAS B 146     1555   1555  1.33
LINK         C   CAS B 146                 N   MET B 147     1555   1555  1.33
LINK         C   ARG B 197                 N   CAS B 198     1555   1555  1.33
LINK         C   CAS B 198                 N   ARG B 199     1555   1555  1.33
LINK         C   ALA B 208                 N   CAS B 209     1555   1555  1.33
LINK         C   CAS B 209                 N   ALA B 210     1555   1555  1.33
LINK        MG    MG B1000                 O2B GDP B 999     1555   1555  2.18
LINK        MG    MG B1000                 O   HOH B2046     1555   1555  2.18
LINK        MG    MG B1000                 OG  SER B  89     1555   1555  2.26
LINK        MG    MG B1000                 O   HOH B2024     1555   1555  2.16
LINK        MG    MG B1000                 O   HOH B2007     1555   1555  1.93
LINK        MG    MG B1000                 O   HOH B2045     1555   1555  2.15
SITE     1 AC1  6 SER A  89  GDP A 999  HOH A2008  HOH A2024
SITE     2 AC1  6 HOH A2028  HOH A2081
SITE     1 AC2  6 SER B  89  GDP B 999  HOH B2007  HOH B2024
SITE     2 AC2  6 HOH B2045  HOH B2046
SITE     1 AC3 24 GLN A  84  GLY A  85  VAL A  86  GLY A  87
SITE     2 AC3 24 LYS A  88  SER A  89  THR A  90  ASN A 191
SITE     3 AC3 24 LYS A 192  ASP A 194  LEU A 195  PHE A 213
SITE     4 AC3 24 SER A 221  ALA A 222  ALA A 223   MG A1000
SITE     5 AC3 24 HOH A2024  HOH A2028  HOH A2045  HOH A2076
SITE     6 AC3 24 HOH A2077  HOH A2079  HOH A2080  HOH A2081
SITE     1 AC4 18 GLU B  83  GLY B  85  VAL B  86  GLY B  87
SITE     2 AC4 18 LYS B  88  SER B  89  THR B  90  ASN B 191
SITE     3 AC4 18 LYS B 192  ASP B 194  LEU B 195  SER B 221
SITE     4 AC4 18 ALA B 222  ALA B 223   MG B1000  HOH B2024
SITE     5 AC4 18 HOH B2045  HOH B2046
CRYST1  116.617  116.617   81.409  90.00  90.00 120.00 P 61         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      0.008575  0.004951  0.000000        0.00000
SCALE2      0.000000  0.009902  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012284        0.00000
      
PROCHECK
Go to PROCHECK summary
 References