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PDBsum entry 1c1y

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Top Page protein ligands metals Protein-protein interface(s) links
Signaling protein PDB id
1c1y
Jmol
Contents
Protein chains
167 a.a. *
77 a.a. *
Ligands
GTP
Metals
_CA
_MG
Waters ×83
* Residue conservation analysis
HEADER    SIGNALING PROTEIN                       22-JUL-99   1C1Y
TITLE     CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-
TITLE    2 BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RAS-RELATED PROTEIN RAP-1A;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RAP, RESIDUES 1-167;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: PROTO-ONKOGENE SERINE/THREONINE PROTEIN KINASE
COMPND   8 RAF-1;
COMPND   9 CHAIN: B;
COMPND  10 FRAGMENT: RAFRBD, RESIDUES 51-131;
COMPND  11 EC: 2.7.1.-;
COMPND  12 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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PBKS;
SOURCE   9 MOL_ID: 2;
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  11 ORGANISM_COMMON: HUMAN;
SOURCE  12 ORGANISM_TAXID: 9606;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS    GTP-BINDING PROTEINS, PROTEIN-PROTEIN COMPLEX, EFFECTORS,
KEYWDS   2 SIGNALING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.NASSAR
REVDAT   5   24-FEB-09 1C1Y    1       VERSN
REVDAT   4   09-SEP-08 1C1Y    1       REMARK
REVDAT   3   08-NOV-00 1C1Y    3       ATOM   REMARK
REVDAT   2   02-AUG-99 1C1Y    1       HEADER
REVDAT   1   02-AUG-99 1C1Y    0
JRNL        AUTH   N.NASSAR
JRNL        TITL   THE 2.2 A CRYSTAL STRUCTURE OF THE RAS-BINDING
JRNL        TITL 2 DOMAIN OF THE SERINE/THREONINE KINASE C-RAF1 IN
JRNL        TITL 3 COMPLEX WITH RAP1A AND A GTP ANALOGUE.
JRNL        REF    NATURE                        V. 375   554 1995
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   7791872
JRNL        DOI    10.1038/375554A0
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   N.NASSAR
REMARK   1  TITL   RAS/RAP EFFECTOR SPECIFICTY DETERMINED BY CHARGE
REMARK   1  TITL 2 REVERSAL.
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   3   723 1996
REMARK   1  REFN                   ISSN 1072-8368
REMARK   1 REFERENCE 2
REMARK   1  AUTH   H.REHMANN,E.ARIAS-PALOMO,M.A.HADDERS,F.SCHWEDE,
REMARK   1  AUTH 2 O.LLORCA,J.L.BOS
REMARK   1  TITL   STRUCTURE OF EPAC2 IN COMPLEX WITH A CYCLIC AMP
REMARK   1  TITL 2 ANALOGUE AND RAP1B.
REMARK   1  REF    NATURE                        V. 455   124 2008
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1  PMID   18660803
REMARK   1  DOI    10.1038/NATURE07187
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.4
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 7734287.570
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3
REMARK   3   NUMBER OF REFLECTIONS             : 24787
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 SET) : 0.229
REMARK   3   FREE R VALUE                     : 0.257
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 2454
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3569
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570
REMARK   3   BIN FREE R VALUE                    : 0.3800
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 392
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2034
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 34
REMARK   3   SOLVENT ATOMS            : 83
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 9.12000
REMARK   3    B22 (A**2) : -2.05000
REMARK   3    B33 (A**2) : -7.08000
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27
REMARK   3   ESD FROM SIGMAA              (A) : 0.28
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.06
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.380 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.300 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.900 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.000 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.33
REMARK   3   BSOL        : 37.03
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PR
REMARK   3  PARAMETER FILE  2  : GTP.PAR
REMARK   3  PARAMETER FILE  3  : WATER.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : GTP.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELYHOOD REFINEMENT USING
REMARK   3  CNS_0.4.
REMARK   4
REMARK   4 1C1Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-99.
REMARK 100 THE RCSB ID CODE IS RCSB009379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-94
REMARK 200  TEMPERATURE           (KELVIN) : 278.0
REMARK 200  PH                             : 7.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
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   : 24787
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 4.300
REMARK 200  R MERGE                    (I) : 0.03800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.32500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MMEPEG5000, MAGNESIUM CHLORIDE,
REMARK 280  CALCIUM CHLORIDE, AMMONIUM SULPHATE., PH 7.6, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       22.08500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.10000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.94000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.10000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.08500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.94000
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 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 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    VAL A  24   C     GLN A  25   N      -0.147
REMARK 500    CYS B  81   CB    CYS B  81   SG     -0.141
REMARK 500    CYS B  81   CB    CYS B  81   SG     -0.298
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    CYS B  81   CA  -  CB  -  SG  ANGL. DEV. =   9.8 DEGREES
REMARK 500    CYS B  81   CA  -  CB  -  SG  ANGL. DEV. =  18.7 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    LYS A 117       31.30     71.73
REMARK 500    LEU A 120       56.32    -97.48
REMARK 500    TRP A 138       43.93    -94.21
REMARK 500    ASN A 166       30.97    -77.69
REMARK 500    LYS B 106       71.32     51.08
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 171  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 401   O
REMARK 620 2 SER A  17   OG   90.2
REMARK 620 3 THR A  35   OG1  96.9  81.5
REMARK 620 4 GTP A 170   O2G  92.8 172.4  91.2
REMARK 620 5 GTP A 170   O2B  89.1 100.4 173.7  86.7
REMARK 620 6 HOH A 402   O   175.4  93.4  86.4  83.9  87.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 173  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 123   O
REMARK 620 2 GLU B 125   OE1  72.3
REMARK 620 3 GLU B 125   OE2  90.9  51.0
REMARK 620 4 HOH B 420   O    78.5 146.7 146.4
REMARK 620 5 HOH B 413   O    94.4 122.0  73.9  75.2
REMARK 620 6 ASP B  80   OD1 151.9  80.9  78.4 123.8 107.1
REMARK 620 7 ASP B  80   OD2 153.0 131.8 113.5  74.7  82.2  51.2
REMARK 620 8 HOH B 405   O    79.4  80.6 131.0  78.7 153.9  88.1  91.9
REMARK 620 N                    1     2     3     4     5     6     7
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 171
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 173
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 170
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GUA   RELATED DB: PDB
REMARK 900 1GUA CONSISTS OF THE SAME COMPLEX WITH RAP MUTATED AT
REMARK 900 POSITIONS 30 AND 31, RAP(E30D, K31E).
DBREF  1C1Y A    1   167  UNP    P62834   RAP1A_HUMAN      1    167
DBREF  1C1Y B   55   131  UNP    P04049   RAF1_HUMAN      55    131
SEQRES   1 A  167  MET ARG GLU TYR LYS LEU VAL VAL LEU GLY SER GLY GLY
SEQRES   2 A  167  VAL GLY LYS SER ALA LEU THR VAL GLN PHE VAL GLN GLY
SEQRES   3 A  167  ILE PHE VAL GLU LYS TYR ASP PRO THR ILE GLU ASP SER
SEQRES   4 A  167  TYR ARG LYS GLN VAL GLU VAL ASP CYS GLN GLN CYS MET
SEQRES   5 A  167  LEU GLU ILE LEU ASP THR ALA GLY THR GLU GLN PHE THR
SEQRES   6 A  167  ALA MET ARG ASP LEU TYR MET LYS ASN GLY GLN GLY PHE
SEQRES   7 A  167  ALA LEU VAL TYR SER ILE THR ALA GLN SER THR PHE ASN
SEQRES   8 A  167  ASP LEU GLN ASP LEU ARG GLU GLN ILE LEU ARG VAL LYS
SEQRES   9 A  167  ASP THR GLU ASP VAL PRO MET ILE LEU VAL GLY ASN LYS
SEQRES  10 A  167  CYS ASP LEU GLU ASP GLU ARG VAL VAL GLY LYS GLU GLN
SEQRES  11 A  167  GLY GLN ASN LEU ALA ARG GLN TRP CYS ASN CYS ALA PHE
SEQRES  12 A  167  LEU GLU SER SER ALA LYS SER LYS ILE ASN VAL ASN GLU
SEQRES  13 A  167  ILE PHE TYR ASP LEU VAL ARG GLN ILE ASN ARG
SEQRES   1 B   77  SER ASN THR ILE ARG VAL PHE LEU PRO ASN LYS GLN ARG
SEQRES   2 B   77  THR VAL VAL ASN VAL ARG ASN GLY MET SER LEU HIS ASP
SEQRES   3 B   77  CYS LEU MET LYS ALA LEU LYS VAL ARG GLY LEU GLN PRO
SEQRES   4 B   77  GLU CYS CYS ALA VAL PHE ARG LEU LEU HIS GLU HIS LYS
SEQRES   5 B   77  GLY LYS LYS ALA ARG LEU ASP TRP ASN THR ASP ALA ALA
SEQRES   6 B   77  SER LEU ILE GLY GLU GLU LEU GLN VAL ASP PHE LEU
HET     MG  A 171       1
HET     CA  B 173       1
HET    GTP  A 170      32
HETNAM      MG MAGNESIUM ION
HETNAM      CA CALCIUM ION
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE
FORMUL   3   MG    MG 2+
FORMUL   4   CA    CA 2+
FORMUL   5  GTP    C10 H16 N5 O14 P3
FORMUL   6  HOH   *83(H2 O)
HELIX    1   1 GLY A   15  GLN A   25  1                                  11
HELIX    2   2 ALA A   66  GLY A   75  1                                  10
HELIX    3   3 ALA A   86  ASP A   92  1                                   7
HELIX    4   4 ASP A   92  ASP A  105  1                                  14
HELIX    5   5 LEU A  120  ARG A  124  5                                   5
HELIX    6   6 GLY A  127  TRP A  138  1                                  12
HELIX    7   7 ASN A  153  ASN A  166  1                                  14
HELIX    8   8 SER B   77  VAL B   88  1                                  12
HELIX    9   9 GLN B   92  GLU B   94  5                                   3
HELIX   10  10 HIS B  103  LYS B  106  5                                   4
HELIX   11  11 ALA B  118  ILE B  122  5                                   5
SHEET    1   A11 ALA A 142  GLU A 145  0
SHEET    2   A11 MET A 111  ASN A 116  1  O  MET A 111   N  ALA A 142
SHEET    3   A11 GLY A  77  SER A  83  1  O  PHE A  78   N  ILE A 112
SHEET    4   A11 GLU A   3  LEU A   9  1  O  LYS A   5   N  GLY A  77
SHEET    5   A11 GLN A  50  THR A  58  1  O  MET A  52   N  TYR A   4
SHEET    6   A11 GLU A  37  GLU A  45 -1  O  ASP A  38   N  ASP A  57
SHEET    7   A11 GLN B  66  ASN B  71 -1  O  ARG B  67   N  SER A  39
SHEET    8   A11 THR B  57  LEU B  62 -1  O  ILE B  58   N  VAL B  70
SHEET    9   A11 GLU B 125  PHE B 130  1  O  LEU B 126   N  PHE B  61
SHEET   10   A11 CYS B  96  LEU B 102 -1  N  ALA B  97   O  ASP B 129
SHEET   11   A11 LYS B 108  LEU B 112 -1  O  LYS B 108   N  LEU B 102
LINK        MG    MG A 171                 O   HOH A 401     1555   1555  2.33
LINK        MG    MG A 171                 OG  SER A  17     1555   1555  2.22
LINK        MG    MG A 171                 OG1 THR A  35     1555   1555  2.21
LINK        MG    MG A 171                 O2G GTP A 170     1555   1555  2.16
LINK        MG    MG A 171                 O2B GTP A 170     1555   1555  2.16
LINK        MG    MG A 171                 O   HOH A 402     1555   1555  2.31
LINK        CA    CA B 173                 O   GLY B 123     1555   1555  2.36
LINK        CA    CA B 173                 OE1 GLU B 125     1555   1555  2.62
LINK        CA    CA B 173                 OE2 GLU B 125     1555   1555  2.46
LINK        CA    CA B 173                 O   HOH B 420     1555   1555  2.56
LINK        CA    CA B 173                 O   HOH B 413     1555   1555  2.43
LINK        CA    CA B 173                 OD1 ASP B  80     1555   4556  2.52
LINK        CA    CA B 173                 OD2 ASP B  80     1555   4556  2.55
LINK        CA    CA B 173                 O   HOH B 405     1555   4556  2.63
SITE     1 AC1  5 SER A  17  THR A  35  GTP A 170  HOH A 401
SITE     2 AC1  5 HOH A 402
SITE     1 AC2  6 ASP B  80  GLY B 123  GLU B 125  HOH B 405
SITE     2 AC2  6 HOH B 413  HOH B 420
SITE     1 AC3 26 GLY A  12  GLY A  13  VAL A  14  GLY A  15
SITE     2 AC3 26 LYS A  16  SER A  17  ALA A  18  PHE A  28
SITE     3 AC3 26 VAL A  29  GLU A  30  TYR A  32  PRO A  34
SITE     4 AC3 26 THR A  35  GLY A  60  ASN A 116  LYS A 117
SITE     5 AC3 26 ASP A 119  SER A 147  ALA A 148  LYS A 149
SITE     6 AC3 26  MG A 171  HOH A 401  HOH A 402  HOH A 412
SITE     7 AC3 26 HOH A 432  HOH A 471
CRYST1   44.170   71.880  100.200  90.00  90.00  90.00 P 21 21 21    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      0.022640  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013912  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009980        0.00000
      
PROCHECK
Go to PROCHECK summary
 References