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PDBsum entry 1zw6

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Oncoprotein PDB id
1zw6
Jmol
Contents
Protein chain
166 a.a.
Ligands
GNP
Metals
_MG ×3
_CA ×2
Waters ×167
HEADER    ONCOPROTEIN                             03-JUN-05   1ZW6
TITLE     CRYSTAL STRUCTURE OF THE GTP-BOUND FORM OF RASQ61G
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TRANSFORMING PROTEIN P21/H-RAS-1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: C-H-RAS;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HRAS, HRAS1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: CODONPLUS(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTB
KEYWDS    GTPASE, GTP, RAS, G-PROTEIN, ONCOPROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.FORD,V.HORNAK,H.KLEINMAN,N.NASSAR
REVDAT   2   24-FEB-09 1ZW6    1       VERSN
REVDAT   1   14-MAR-06 1ZW6    0
JRNL        AUTH   B.FORD,V.HORNAK,H.KLEINMAN,N.NASSAR
JRNL        TITL   STRUCTURE OF A TRANSIENT INTERMEDIATE FOR GTP
JRNL        TITL 2 HYDROLYSIS BY RAS.
JRNL        REF    STRUCTURE                     V.  14   427 2006
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   16531227
JRNL        DOI    10.1016/J.STR.2005.12.010
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.E.HALL,D.BAR-SAGI,N.NASSAR
REMARK   1  TITL   THE STRUCTURAL BASIS FOR THE TRANSITION FROM
REMARK   1  TITL 2 RAS-GTP TO RAS-GDP
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  99 12138 2002
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1  PMID   12213964
REMARK   1  DOI    10.1073/PNAS.192453199
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.79
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4
REMARK   3   NUMBER OF REFLECTIONS             : 30980
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) : 0.146
REMARK   3   R VALUE            (WORKING SET) : 0.144
REMARK   3   FREE R VALUE                     : 0.174
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1653
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) : 1.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2250
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.96
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1520
REMARK   3   BIN FREE R VALUE SET COUNT          : 127
REMARK   3   BIN FREE R VALUE                    : 0.1970
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1355
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 37
REMARK   3   SOLVENT ATOMS            : 167
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.24
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.07000
REMARK   3    B22 (A**2) : -0.07000
REMARK   3    B33 (A**2) : 0.10000
REMARK   3    B12 (A**2) : -0.03000
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): 0.067
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.060
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.032
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.834
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1408 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1248 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1903 ; 1.489 ; 1.987
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2909 ; 2.348 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   167 ; 9.712 ; 5.120
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    77 ;38.017 ;24.156
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   256 ;14.750 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;15.537 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   206 ; 0.083 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1549 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   285 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   279 ; 0.208 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1300 ; 0.197 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   687 ; 0.180 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):   818 ; 0.091 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   121 ; 0.188 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     8 ; 0.128 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    17 ; 0.397 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    43 ; 0.266 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.261 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     3 ; 0.334 ; 0.200
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):   855 ; 1.573 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   343 ; 0.495 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1331 ; 2.119 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   639 ; 2.913 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   572 ; 4.064 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2892 ; 1.529 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   172 ; 6.503 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  2635 ; 2.487 ; 3.000
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 : BABINET MODEL WITH 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
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 1ZW6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-05.
REMARK 100 THE RCSB ID CODE IS RCSB033193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X26C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI 111
REMARK 200  OPTICS                         : MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30980
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.800
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08600
REMARK 200   FOR THE DATA SET  : 24.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.46500
REMARK 200   FOR SHELL         : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG4000, 200MM CA ACETATE, 100
REMARK 280  MM TRIS-HCL, 10 MM MGCL2, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z
REMARK 290       6555   -X,-X+Y,-Z
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290      18555   -X+1/3,-X+Y+2/3,-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        0.00000
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        0.00000
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        0.00000
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        0.00000
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       44.38800
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       25.62742
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       44.79733
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       44.38800
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       25.62742
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       44.79733
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       44.38800
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       25.62742
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       44.79733
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       44.38800
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       25.62742
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       44.79733
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       44.38800
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       25.62742
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       44.79733
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       44.38800
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       25.62742
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       44.79733
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       51.25485
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       89.59467
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       51.25485
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       89.59467
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       51.25485
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       89.59467
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       51.25485
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       89.59467
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       51.25485
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       89.59467
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       51.25485
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       89.59467
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG    MG A 204  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 335  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 341  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 346  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 358  LIES ON A SPECIAL POSITION.
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   NZ   LYS A    88     O    HOH A   337              2.14
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    ILE A  36      -66.50    -93.28
REMARK 500    GLU A  37      110.52   -164.85
REMARK 500    LYS A 117       35.93     70.00
REMARK 500    ARG A 149       -4.47     81.79
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                              CA A 201  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A  28   O
REMARK 620 2 ASP A  30   OD2  85.7
REMARK 620 3 HOH A 277   O    89.7  84.2
REMARK 620 4 HOH A 304   O   177.4  92.3  91.8
REMARK 620 5 GLU A  31   OE1  89.0  77.0 161.2  88.9
REMARK 620 6 ASP A  33   OD1 100.8 157.4  74.3  81.6 124.2
REMARK 620 7 ASP A  33   OD2  87.0 151.2 123.6  94.0  75.0  51.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 202  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 105   OD1
REMARK 620 2 ARG A 102   O    78.4
REMARK 620 3 ASP A 105   OD2  41.6  80.2
REMARK 620 4 HOH A 310   O    96.0  91.2 137.5
REMARK 620 5 HOH A 341   O    76.4  85.8  34.8 172.2
REMARK 620 6 ARG A 102   O    81.2 159.4  83.4  92.7  87.7
REMARK 620 7 HOH A 310   O    73.4  86.4 114.9  22.6 149.7  89.5
REMARK 620 8 HOH A 341   O    76.4  85.8  34.8 172.3   0.1  87.7 149.7
REMARK 620 9 ASP A 105   OD2 116.9  93.9  75.3 147.1  40.5  93.8 169.6  40.5
REMARK 620 10 ASP A 105   OD1 168.6  99.1 127.1  95.2  92.4 100.7 117.8
REMARK 620  92.3  51.9
REMARK 620 N                    1     2     3     4     5     6     7     8
REMARK 620     9
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 203  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 435   O
REMARK 620 2 HOH A 419   O    69.2
REMARK 620 3 HOH A 431   O    91.3  59.7
REMARK 620 4 HOH A 366   O   148.8 141.2 100.1
REMARK 620 5 HOH A 360   O   150.0  81.9  80.4  61.1
REMARK 620 6 GLN A 165   OE1  85.1  83.5 141.5 102.6  83.8
REMARK 620 7 GLY A 138   O    84.4 150.6 136.3  67.3 121.2  81.6
REMARK 620 8 HOH A 431   O   107.0  82.5  23.7  77.5  75.9 156.7 118.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 204  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 308   O
REMARK 620 2 HOH A 279   O    85.0
REMARK 620 3 HOH A 308   O    97.8  88.6
REMARK 620 4 HOH A 308   O    97.3 173.7  96.8
REMARK 620 5 HOH A 279   O   174.6  89.9  84.0  87.5
REMARK 620 6 HOH A 279   O    88.6  90.3 173.5  84.0  89.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 269  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GNP A 268   O2G
REMARK 620 2 GNP A 268   O2B  93.8
REMARK 620 3 HOH A 434   O    91.9  89.2
REMARK 620 4 THR A  35   OG1  90.1 175.3  87.9
REMARK 620 5 SER A  17   OG  173.4  92.6  90.1  83.6
REMARK 620 6 HOH A 272   O    91.3  91.9 176.5  90.7  86.5
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 A 269
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 201
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 203
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 204
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 268
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5P21   RELATED DB: PDB
REMARK 900 STRUCTURE OF WILD TYPE RAS BOUND TO GTP
REMARK 900 RELATED ID: 1LF0   RELATED DB: PDB
REMARK 900 STRUCTURE OF A59G MUTANT OF THE SAME PROTEIN BOUND TO GTP
REMARK 900 RELATED ID: 1ZVQ   RELATED DB: PDB
REMARK 900 STRUCTURE OF Q61G MUTANT OF THE SAME PROTEIN BOUND TO GDP
DBREF  1ZW6 A    1   166  UNP    P01112   RASH_HUMAN       1    166
SEQADV 1ZW6 CSO A   51  UNP  P01112    CYS    51 MODIFIED RESIDUE
SEQADV 1ZW6 GLY A   61  UNP  P01112    GLN    61 ENGINEERED
SEQRES   1 A  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES   2 A  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES   3 A  166  HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES   4 A  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CSO LEU
SEQRES   5 A  166  LEU ASP ILE LEU ASP THR ALA GLY GLY GLU GLU TYR SER
SEQRES   6 A  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES   7 A  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES   8 A  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES   9 A  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES  10 A  166  CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES  11 A  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES  12 A  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES  13 A  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
MODRES 1ZW6 CSO A   51  CYS  S-HYDROXYCYSTEINE
HET    CSO  A  51       7
HET     MG  A 269       1
HET     CA  A 201       1
HET     CA  A 202       1
HET     MG  A 203       1
HET     MG  A 204       1
HET    GNP  A 268      32
HETNAM     CSO S-HYDROXYCYSTEINE
HETNAM      MG MAGNESIUM ION
HETNAM      CA CALCIUM ION
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
FORMUL   1  CSO    C3 H7 N O3 S
FORMUL   2   MG    3(MG 2+)
FORMUL   3   CA    2(CA 2+)
FORMUL   7  GNP    C10 H17 N6 O13 P3
FORMUL   8  HOH   *167(H2 O)
HELIX    1   1 GLY A   15  ASN A   26  1                                  12
HELIX    2   2 GLY A   61  GLU A   63  5                                   3
HELIX    3   3 TYR A   64  MET A   72  1                                   9
HELIX    4   4 ASN A   86  ASP A   92  1                                   7
HELIX    5   5 ASP A   92  ASP A  105  1                                  14
HELIX    6   6 GLU A  126  GLY A  138  1                                  13
HELIX    7   7 GLY A  151  HIS A  166  1                                  16
SHEET    1   A 6 GLU A  37  ILE A  46  0
SHEET    2   A 6 GLU A  49  THR A  58 -1  O  ILE A  55   N  TYR A  40
SHEET    3   A 6 THR A   2  GLY A  10  1  N  LEU A   6   O  LEU A  56
SHEET    4   A 6 GLY A  77  ALA A  83  1  O  VAL A  81   N  VAL A   9
SHEET    5   A 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82
SHEET    6   A 6 TYR A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113
LINK         C   THR A  50                 N   CSO A  51     1555   1555  1.33
LINK         C   CSO A  51                 N   LEU A  52     1555   1555  1.33
LINK        CA    CA A 201                 O   PHE A  28     1555   1555  2.34
LINK        CA    CA A 201                 OD2 ASP A  30     1555   1555  2.40
LINK        CA    CA A 201                 O   HOH A 277     1555   1555  2.39
LINK        CA    CA A 201                 O   HOH A 304     1555   1555  2.34
LINK        CA    CA A 202                 OD1 ASP A 105     1555   1555  2.68
LINK        CA    CA A 202                 O   ARG A 102     1555   1555  2.34
LINK        CA    CA A 202                 OD2 ASP A 105     1555   1555  3.24
LINK        CA    CA A 202                 O   HOH A 310     1555   1555  2.22
LINK        CA    CA A 202                 O   HOH A 341     1555   1555  2.59
LINK        MG    MG A 203                 O   HOH A 435     1555   1555  2.23
LINK        MG    MG A 203                 O   HOH A 419     1555   1555  2.71
LINK        MG    MG A 203                 O   HOH A 431     1555   1555  1.68
LINK        MG    MG A 203                 O   HOH A 366     1555   1555  1.88
LINK        MG    MG A 203                 O   HOH A 360     1555   1555  2.59
LINK        MG    MG A 203                 OE1 GLN A 165     1555   1555  2.29
LINK        MG    MG A 204                 O   HOH A 308     1555   1555  2.06
LINK        MG    MG A 204                 O   HOH A 279     1555   1555  2.20
LINK         O2G GNP A 268                MG    MG A 269     1555   1555  1.98
LINK         O2B GNP A 268                MG    MG A 269     1555   1555  2.05
LINK        MG    MG A 269                 O   HOH A 434     1555   1555  2.13
LINK        MG    MG A 269                 OG1 THR A  35     1555   1555  2.09
LINK        MG    MG A 269                 OG  SER A  17     1555   1555  2.06
LINK        MG    MG A 269                 O   HOH A 272     1555   1555  2.06
LINK        CA    CA A 201                 OE1 GLU A  31     1555   5556  2.33
LINK        CA    CA A 201                 OD1 ASP A  33     1555   5556  2.54
LINK        CA    CA A 201                 OD2 ASP A  33     1555   5556  2.48
LINK        CA    CA A 202                 O   ARG A 102     1555   6556  2.25
LINK        CA    CA A 202                 O   HOH A 310     1555   6556  2.38
LINK        CA    CA A 202                 O   HOH A 341     1555   6556  2.59
LINK        CA    CA A 202                 OD2 ASP A 105     1555   6556  2.74
LINK        CA    CA A 202                 OD1 ASP A 105     1555   6556  1.88
LINK        MG    MG A 203                 O   GLY A 138     1555  16545  2.82
LINK        MG    MG A 203                 O   HOH A 431     1555  16545  2.28
LINK        MG    MG A 204                 O   HOH A 308     1555   3655  2.07
LINK        MG    MG A 204                 O   HOH A 308     1555   2545  2.08
LINK        MG    MG A 204                 O   HOH A 279     1555   3655  2.22
LINK        MG    MG A 204                 O   HOH A 279     1555   2545  2.21
SITE     1 AC1  5 SER A  17  THR A  35  GNP A 268  HOH A 272
SITE     2 AC1  5 HOH A 434
SITE     1 AC2  6 PHE A  28  ASP A  30  GLU A  31  ASP A  33
SITE     2 AC2  6 HOH A 277  HOH A 304
SITE     1 AC3  4 ARG A 102  ASP A 105  HOH A 310  HOH A 341
SITE     1 AC4  7 GLY A 138  GLN A 165  HOH A 360  HOH A 366
SITE     2 AC4  7 HOH A 419  HOH A 431  HOH A 435
SITE     1 AC5  2 HOH A 279  HOH A 308
SITE     1 AC6 31 GLY A  12  GLY A  13  VAL A  14  GLY A  15
SITE     2 AC6 31 LYS A  16  SER A  17  ALA A  18  PHE A  28
SITE     3 AC6 31 VAL A  29  ASP A  30  GLU A  31  TYR A  32
SITE     4 AC6 31 PRO A  34  THR A  35  GLY A  60  ASN A 116
SITE     5 AC6 31 LYS A 117  ASP A 119  LEU A 120  SER A 145
SITE     6 AC6 31 ALA A 146  LYS A 147   MG A 269  HOH A 272
SITE     7 AC6 31 HOH A 276  HOH A 290  HOH A 309  HOH A 321
SITE     8 AC6 31 HOH A 353  HOH A 357  HOH A 434
CRYST1   88.776   88.776  134.392  90.00  90.00 120.00 H 3 2        18
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      0.011264  0.006503  0.000000        0.00000
SCALE2      0.000000  0.013007  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007441        0.00000
      
PROCHECK
Go to PROCHECK summary
 References