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PDBsum entry 2ce2

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Signaling protein PDB id
2ce2
Jmol
Contents
Protein chain
166 a.a.
Ligands
GDP
XY2
Metals
_MG
HEADER    SIGNALING PROTEIN                       02-FEB-06   2CE2
TITLE     CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS
TITLE    2 P21 IN COMPLEX WITH GDP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GTPASE HRAS;
COMPND   3 CHAIN: X;
COMPND   4 FRAGMENT: RESIDUES 1-166;
COMPND   5 SYNONYM: H-RAS P21, TRANSFORMING PROTEIN P21, C-H-RAS-1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES;
COMPND   8 OTHER_DETAILS: AN IANBD FLUOROPHORE WAS ATTACHED TO CYS-32
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 EXPRESSION_SYSTEM_STRAIN: CK600K;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTAC RAS
KEYWDS    SIGNALING PROTEIN, GUANINE NUCLEOTIDE BINDING PROTEIN, FLUORESCENCE,
KEYWDS   2 MEMBRANE, LIPOPROTEIN, PALMITATE, PRENYLATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.U.KLINK,R.S.GOODY,A.J.SCHEIDIG
REVDAT   3   13-JUL-11 2CE2    1       VERSN
REVDAT   2   24-FEB-09 2CE2    1       VERSN
REVDAT   1   23-AUG-06 2CE2    0
JRNL        AUTH   B.U.KLINK,R.S.GOODY,A.J.SCHEIDIG
JRNL        TITL   A NEWLY DESIGNED MICROSPECTROFLUOROMETER FOR KINETIC
JRNL        TITL 2 STUDIES ON PROTEIN CRYSTALS IN COMBINATION WITH X-RAY
JRNL        TITL 3 DIFFRACTION
JRNL        REF    BIOPHYS.J.                    V.  91   981 2006
JRNL        REFN                   ISSN 0006-3495
JRNL        PMID   16698776
JRNL        DOI    10.1529/BIOPHYSJ.105.078931
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.U.KLINK,A.J.SCHEIDIG
REMARK   1  TITL   NOT YET DEFINED
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    1.0  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) : 1.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0
REMARK   3   NUMBER OF REFLECTIONS             : 76394
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) : 0.145
REMARK   3   R VALUE            (WORKING SET) : 0.144
REMARK   3   FREE R VALUE                     : 0.163
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4021
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) : 1.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.03
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5493
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2700
REMARK   3   BIN FREE R VALUE SET COUNT          : 290
REMARK   3   BIN FREE R VALUE                    : 0.2770
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2634
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 100
REMARK   3   SOLVENT ATOMS            : 434
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.87
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.53000
REMARK   3    B22 (A**2) : -0.17000
REMARK   3    B33 (A**2) : -0.36000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.032
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.033
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.029
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.202
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.979
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2776 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2456 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3764 ; 1.719 ; 2.004
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5706 ; 0.802 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   330 ; 7.142 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;37.180 ;24.493
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   480 ;13.825 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;18.923 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   414 ; 0.085 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3078 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   554 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   176 ; 0.241 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1305 ; 0.196 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   673 ; 0.188 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):   875 ; 0.091 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   288 ; 0.214 ; 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):    19 ; 0.301 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.347 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    50 ; 0.188 ; 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):  2142 ; 0.968 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2658 ; 1.042 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1360 ; 1.734 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1106 ; 2.424 ; 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  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   X     1        X   190
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4980  36.9880  15.1460
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0559 T22:  -0.0608
REMARK   3      T33:  -0.0383 T12:  -0.0162
REMARK   3      T13:   0.0084 T23:  -0.0085
REMARK   3    L TENSOR
REMARK   3      L11:   0.5213 L22:   0.8820
REMARK   3      L33:   0.9431 L12:   0.2442
REMARK   3      L13:  -0.1480 L23:   0.1523
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0065 S12:  -0.0462 S13:  -0.0416
REMARK   3      S21:   0.0125 S22:  -0.0080 S23:  -0.0393
REMARK   3      S31:   0.0758 S32:   0.0324 S33:   0.0145
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   X  2001        X  2434
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8340  38.1740  13.4000
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0060 T22:  -0.0066
REMARK   3      T33:   0.0230 T12:  -0.0063
REMARK   3      T13:  -0.0048 T23:  -0.0118
REMARK   3    L TENSOR
REMARK   3      L11:   1.0888 L22:   1.5574
REMARK   3      L33:   1.3060 L12:   0.8576
REMARK   3      L13:  -0.3451 L23:   0.0348
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0546 S12:   0.0211 S13:  -0.0130
REMARK   3      S21:  -0.0717 S22:   0.0229 S23:   0.0240
REMARK   3      S31:   0.0529 S32:   0.0327 S33:   0.0318
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. AN IANBD FLUOROPHORE WAS ATTACHED TO CYS-32.
REMARK   3  THE STRUCTURE WAS REFINED USING TWO ALTERNATIVE CONFORMATIONS
REMARK   3  FOR THE WHOLE PROTEIN CHAIN. THE CLOSE CONTACTS WITH WATER
REMARK   3  MOLECULES ARE CAUSED BY THE TREATMENT OF THE WHOLE PROTEIN
REMARK   3  CHAIN WITH TWO ALTERNATIVE CONFORMATIONS, BUT ONLY ONE
REMARK   3  POSITION PER WATER MOLECULE.
REMARK   4
REMARK   4 2CE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-06.
REMARK 100 THE PDBE ID CODE IS EBI-27542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-04
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.60
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.82655
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 : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82821
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.990
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.99
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4Q21
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 17.22 MG/ML
REMARK 280  PROTEIN, 64 MM TRIS PH 7.6, 20 MM MAGNESIUM CHLORIDE, 10
REMARK 280  MM DTT, 0,1 MM SODIUM AZIDE; RESERVOIR SOLUTION: 64 MM
REMARK 280  TRIS PH 7.6, 20 MM MAGNESIUM CHLORIDE, 10 MM DTT, 0,1 MM
REMARK 280  SODIUM AZIDE, 35% PEG 400 MIXTURE OF EQUAL VOLUMES OF
REMARK 280  PROTEIN AND RESERVOIR SOLUTION, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       58.10000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.10000
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        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       24.50000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.95000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.50000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.95000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.10000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.50000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       26.95000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.10000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.50000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       26.95000
REMARK 290   SMTRY3   8  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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN X, TYR 32 TO CYS
REMARK 400 ENGINEERED RESIDUE IN CHAIN X, CYS 118 TO SER
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  2 CYS X  80   CB B  CYS X  80   SG B   -0.168
REMARK 500  2 CYS X  80   CB B  CYS X  80   SG B   -0.174
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  2 CYS X  32   N   -  CA  -  CB  ANGL. DEV. =  -9.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500  1 GLU X  63     -107.57    -33.76
REMARK 500  1 LYS X 117       37.26     76.13
REMARK 500  1 ALA X 121       43.26    -91.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU X   63     TYR X   64          1      -132.35
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 X 170  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER X  17A  OG
REMARK 620 2 GDP X 180A  O2B  90.6
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG X 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP X 180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XY2 X 190
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 121P   RELATED DB: PDB
REMARK 900 RELATED ID: 1AA9   RELATED DB: PDB
REMARK 900  HUMAN C-HA-RAS(1-171)(DOT)GDP, NMR,
REMARK 900  MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1AGP   RELATED DB: PDB
REMARK 900 RELATED ID: 1BKD   RELATED DB: PDB
REMARK 900  COMPLEX OF HUMAN H-RAS WITH HUMAN SOS-1
REMARK 900 RELATED ID: 1CLU   RELATED DB: PDB
REMARK 900  H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA
REMARK 900  ,GAMMA-IMIDO- GTP
REMARK 900 RELATED ID: 1CRP   RELATED DB: PDB
REMARK 900 RELATED ID: 1CRQ   RELATED DB: PDB
REMARK 900 RELATED ID: 1CRR   RELATED DB: PDB
REMARK 900 RELATED ID: 1CTQ   RELATED DB: PDB
REMARK 900  STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP
REMARK 900  AT 100 K
REMARK 900 RELATED ID: 1GNP   RELATED DB: PDB
REMARK 900 RELATED ID: 1GNQ   RELATED DB: PDB
REMARK 900 RELATED ID: 1GNR   RELATED DB: PDB
REMARK 900 RELATED ID: 1HE8   RELATED DB: PDB
REMARK 900  RAS G12V - PI 3-KINASE GAMMA COMPLEX
REMARK 900 RELATED ID: 1IAQ   RELATED DB: PDB
REMARK 900  C-H-RAS P21 PROTEIN MUTANT WITH THR 35
REMARK 900  REPLACED BY SER(T35S) COMPLEXED WITH
REMARK 900  GUANOSINE-5'-[B,G-IMIDO] TRIPHOSPHATE
REMARK 900 RELATED ID: 1IOZ   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE C-HA-RAS PROTEIN
REMARK 900   PREPARED BY THECELL-FREE SYNTHESIS
REMARK 900 RELATED ID: 1JAH   RELATED DB: PDB
REMARK 900  H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED
REMARK 900  WITHGUANOSINE-5'-[BETA,GAMMA-METHYLENE]
REMARK 900  TRIPHOSPHATE ANDMAGNESIUM
REMARK 900 RELATED ID: 1JAI   RELATED DB: PDB
REMARK 900  H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED
REMARK 900  WITHGUANOSINE-5'-[BETA,GAMMA-METHYLENE]
REMARK 900  TRIPHOSPHATEAND MANGANESE
REMARK 900 RELATED ID: 1K8R   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF RAS-BRY2RBD COMPLEX
REMARK 900 RELATED ID: 1LF0   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF RASA59G IN THE GTP-
REMARK 900  BOUND FORM
REMARK 900 RELATED ID: 1LF5   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF RASA59G IN THE GDP-
REMARK 900  BOUND FORM
REMARK 900 RELATED ID: 1LFD   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN
REMARK 900   COMPLEXED WITHTHE RAS-INTERACTING DOMAIN OF
REMARK 900   RALGDS
REMARK 900 RELATED ID: 1NVU   RELATED DB: PDB
REMARK 900  STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY
REMARK 900   RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE
REMARK 900  EXCHANGE FACTOR SOS
REMARK 900 RELATED ID: 1NVV   RELATED DB: PDB
REMARK 900  STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY
REMARK 900   RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE
REMARK 900  EXCHANGE FACTOR SOS
REMARK 900 RELATED ID: 1NVW   RELATED DB: PDB
REMARK 900  STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY
REMARK 900   RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE
REMARK 900  EXCHANGE FACTOR SOS
REMARK 900 RELATED ID: 1NVX   RELATED DB: PDB
REMARK 900  STRUCTURAL EVIDENCE FOR FEEDBACK ACTIVATION BY
REMARK 900   RASGTP OFTHE RAS-SPECIFIC NUCLEOTIDE
REMARK 900  EXCHANGE FACTOR SOS
REMARK 900 RELATED ID: 1P2S   RELATED DB: PDB
REMARK 900  H-RAS 166 IN 50% 2,2,2 TRIFLOUROETHANOL
REMARK 900 RELATED ID: 1P2T   RELATED DB: PDB
REMARK 900  H-RAS 166 IN AQUEOUS MOTHER LIQOUR, RT
REMARK 900 RELATED ID: 1P2U   RELATED DB: PDB
REMARK 900  H-RAS IN 50% ISOPROPANOL
REMARK 900 RELATED ID: 1P2V   RELATED DB: PDB
REMARK 900  H-RAS 166 IN 60 % 1,6 HEXANEDIOL
REMARK 900 RELATED ID: 1PLJ   RELATED DB: PDB
REMARK 900 RELATED ID: 1PLK   RELATED DB: PDB
REMARK 900 RELATED ID: 1PLL   RELATED DB: PDB
REMARK 900 RELATED ID: 1Q21   RELATED DB: PDB
REMARK 900 RELATED ID: 1QRA   RELATED DB: PDB
REMARK 900  STRUCTURE OF P21RAS IN COMPLEX WITH GTP AT
REMARK 900   100 K
REMARK 900 RELATED ID: 1RVD   RELATED DB: PDB
REMARK 900  H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA
REMARK 900  ,GAMMA-IMIDO- GTP
REMARK 900 RELATED ID: 1WQ1   RELATED DB: PDB
REMARK 900  RAS-RASGAP COMPLEX
REMARK 900 RELATED ID: 1XCM   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE GPPNHP-BOUND H-
REMARK 900  RAS G60A MUTANT
REMARK 900 RELATED ID: 1XD2   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF A TERNARY RAS:SOS:RAS
REMARK 900  *GDP COMPLEX
REMARK 900 RELATED ID: 1XJ0   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE GDP-BOUND FORM OF
REMARK 900   THE RASG60AMUTANT
REMARK 900 RELATED ID: 221P   RELATED DB: PDB
REMARK 900 RELATED ID: 2C5L   RELATED DB: PDB
REMARK 900  STRUCTURE OF PLC EPSILON RAS ASSOCIATION
REMARK 900  DOMAIN WITH HRAS
REMARK 900 RELATED ID: 2CL0   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT
REMARK 900  FORM OF H-RAS P21 IN COMPLEX WITH GPPNHP
REMARK 900 RELATED ID: 2CL6   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT
REMARK 900  FORM OF H-RAS P21 IN COMPLEX WITH S-
REMARK 900  CAGED GTP
REMARK 900 RELATED ID: 2CL7   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT
REMARK 900  FORM OF H-RAS P21 IN COMPLEX WITH GTP
REMARK 900 RELATED ID: 2CLC   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT
REMARK 900  FORM OF H-RAS P21 IN COMPLEX WITH GTP (
REMARK 900  2)
REMARK 900 RELATED ID: 2CLD   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT
REMARK 900  FORM OF H-RAS P21 IN COMPLEX WITH GDP (
REMARK 900  2)
REMARK 900 RELATED ID: 2GDP   RELATED DB: PDB
REMARK 900 RELATED ID: 2Q21   RELATED DB: PDB
REMARK 900 RELATED ID: 421P   RELATED DB: PDB
REMARK 900 RELATED ID: 4Q21   RELATED DB: PDB
REMARK 900 RELATED ID: 521P   RELATED DB: PDB
REMARK 900 RELATED ID: 5P21   RELATED DB: PDB
REMARK 900 RELATED ID: 621P   RELATED DB: PDB
REMARK 900 RELATED ID: 6Q21   RELATED DB: PDB
REMARK 900 RELATED ID: 721P   RELATED DB: PDB
REMARK 900 RELATED ID: 821P   RELATED DB: PDB
DBREF  2CE2 X    1   166  UNP    P01112   RASH_HUMAN       1    166
SEQADV 2CE2 CYS X   32  UNP  P01112    TYR    32 ENGINEERED MUTATION
SEQADV 2CE2 SER X  118  UNP  P01112    CYS   118 ENGINEERED MUTATION
SEQRES   1 X  166  MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES   2 X  166  VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES   3 X  166  HIS PHE VAL ASP GLU CYS ASP PRO THR ILE GLU ASP SER
SEQRES   4 X  166  TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU
SEQRES   5 X  166  LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER
SEQRES   6 X  166  ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES   7 X  166  LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES   8 X  166  ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES   9 X  166  ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES  10 X  166  SER ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES  11 X  166  GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES  12 X  166  THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES  13 X  166  TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
HET     MG  X 170       1
HET    GDP  X 180      28
HET    XY2  X 190      21
HETNAM      MG MAGNESIUM ION
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM     XY2 N,N'-DIMETHYL-N-(ACETYL)-N'-(7-NITROBENZ-2-
HETNAM   2 XY2  OXA-1,3-DIAZOL-4-YL)ETHYLENEDIAMINE
FORMUL   2   MG    MG 2+
FORMUL   3  GDP    C10 H15 N5 O11 P2
FORMUL   4  XY2    C12 H15 N5 O4
FORMUL   5  HOH   *434(H2 O)
HELIX    1   1 GLY X   15  ASN X   26  1                                  12
HELIX    2   2 SER X   65  GLY X   75  1                                  11
HELIX    3   3 ASN X   86  ASP X  105  1                                  20
HELIX    4   4 GLU X  126  TYR X  137  1                                  12
HELIX    5   5 GLY X  151  GLN X  165  1                                  15
SHEET    1  XA 6 ASP X  38  ILE X  46  0
SHEET    2  XA 6 GLU X  49  ASP X  57 -1  O  GLU X  49   N  ILE X  46
SHEET    3  XA 6 GLU X   3  GLY X  10  1  O  TYR X   4   N  ASP X  54
SHEET    4  XA 6 GLY X  77  ALA X  83  1  O  GLY X  77   N  VAL X   7
SHEET    5  XA 6 MET X 111  ASN X 116  1  O  VAL X 112   N  CYS X  80
SHEET    6  XA 6 TYR X 141  THR X 144  1  O  ILE X 142   N  GLY X 115
LINK         SG ACYS X  32                 C19AXY2 X 190     1555   1555  1.76
LINK        MG  A MG X 170                 O2BAGDP X 180     1555   1555  2.01
LINK        MG  A MG X 170                 OG ASER X  17     1555   1555  2.21
SITE     1 AC1  2 SER X  17  GDP X 180
SITE     1 AC2 20 MET X   1  THR X   2  GLY X  13  VAL X  14
SITE     2 AC2 20 GLY X  15  LYS X  16  SER X  17  ALA X  18
SITE     3 AC2 20 PHE X  28  VAL X  29  ASP X  30  CYS X  32
SITE     4 AC2 20 ASN X 116  LYS X 117  ASP X 119  LEU X 120
SITE     5 AC2 20 SER X 145  ALA X 146  LYS X 147   MG X 170
SITE     1 AC3  7 ILE X  21  GLN X  25  CYS X  32  ASP X  33
SITE     2 AC3  7 ILE X  36  TYR X  40  GLN X  43
CRYST1   49.000   53.900  116.200  90.00  90.00  90.00 C 2 2 21      8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.020408  0.000000  0.000000        0.00000
SCALE2      0.000000  0.018553  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008606        0.00000
      
PROCHECK
Go to PROCHECK summary
 References