Header list of 2rgf.pdb file
Complete list - t 27 2 Bytes
HEADER RAS-BINDING DOMAIN 13-FEB-97 2RGF
TITLE RBD OF RAL GUANOSINE-NUCLEOTIDE EXCHANGE FACTOR (PROTEIN), NMR, 10
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RALGEF-RBD;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HUMAN RALGEF GENE (RALGDS);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T3;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HUMAN RALGEF GENE (RALGDS)
KEYWDS RAS-BINDING DOMAIN, RALGEF, RALGDS, RAS, RBD
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.GEYER,C.HERRMANN,A.WITTINGHOFER,H.R.KALBITZER
REVDAT 4 27-OCT-21 2RGF 1 REMARK
REVDAT 3 24-FEB-09 2RGF 1 VERSN
REVDAT 2 24-JUN-98 2RGF 1 COMPND SHEET
REVDAT 1 04-MAR-98 2RGF 0
JRNL AUTH M.GEYER,C.HERRMANN,S.WOHLGEMUTH,A.WITTINGHOFER,H.R.KALBITZER
JRNL TITL STRUCTURE OF THE RAS-BINDING DOMAIN OF RALGEF AND
JRNL TITL 2 IMPLICATIONS FOR RAS BINDING AND SIGNALLING.
JRNL REF NAT.STRUCT.BIOL. V. 4 694 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9302994
JRNL DOI 10.1038/NSB0997-694
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.HERRMANN,G.HORN,M.SPAARGAREN,A.WITTINGHOFER
REMARK 1 TITL DIFFERENTIAL INTERACTION OF THE RAS FAMILY GTP-BINDING
REMARK 1 TITL 2 PROTEINS H-RAS, RAP1A, AND R-RAS WITH THE PUTATIVE EFFECTOR
REMARK 1 TITL 3 MOLECULES RAF KINASE AND RAL-GUANINE NUCLEOTIDE EXCHANGE
REMARK 1 TITL 4 FACTOR
REMARK 1 REF J.BIOL.CHEM. V. 271 6794 1996
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.SPAARGAREN,J.R.BISCHOFF
REMARK 1 TITL IDENTIFICATION OF THE GUANINE NUCLEOTIDE DISSOCIATION
REMARK 1 TITL 2 STIMULATOR FOR RAL AS A PUTATIVE EFFECTOR MOLECULE OF R-RAS,
REMARK 1 TITL 3 H-RAS, K-RAS, AND RAP
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 12609 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.HOFER,S.FIELDS,C.SCHNEIDER,G.S.MARTIN
REMARK 1 TITL ACTIVATED RAS INTERACTS WITH THE RAL GUANINE NUCLEOTIDE
REMARK 1 TITL 2 DISSOCIATION STIMULATOR
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 11089 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.F.ALBRIGHT,B.W.GIDDINGS,J.LIU,M.VITO,R.A.WEINBERG
REMARK 1 TITL CHARACTERIZATION OF A GUANINE NUCLEOTIDE DISSOCIATION
REMARK 1 TITL 2 STIMULATOR FOR A RAS-RELATED GTPASE
REMARK 1 REF EMBO J. V. 12 339 1993
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RGF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178558.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H; 13C; 15N HETERONUCLEAR
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.0, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 O ASP A 20 HZ3 LYS A 94 1.57
REMARK 500 H GLU A 60 O LYS A 94 1.57
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 TYR A 5 108.52 -52.90
REMARK 500 1 ASN A 6 -62.47 -130.15
REMARK 500 1 ASP A 11 46.39 -106.62
REMARK 500 1 ASP A 20 69.76 -154.44
REMARK 500 1 VAL A 21 -80.86 -151.49
REMARK 500 1 GLN A 35 51.38 -109.77
REMARK 500 1 HIS A 49 49.64 -98.69
REMARK 500 1 GLU A 54 73.86 -115.65
REMARK 500 1 GLU A 57 48.46 -100.77
REMARK 500 1 ASP A 58 31.61 -153.76
REMARK 500 1 ASP A 68 62.46 -107.84
REMARK 500 1 ARG A 69 -64.80 -19.61
REMARK 500 1 PRO A 74 -171.35 -65.70
REMARK 500 1 ALA A 77 43.25 -81.04
REMARK 500 1 ALA A 87 -65.72 -152.15
REMARK 500 1 ARG A 96 95.79 -68.46
REMARK 500 2 TYR A 5 108.75 -51.71
REMARK 500 2 ASN A 6 -62.63 -130.73
REMARK 500 2 ASP A 20 64.02 -150.90
REMARK 500 2 VAL A 21 -79.66 -155.32
REMARK 500 2 HIS A 49 47.25 -109.15
REMARK 500 2 GLU A 57 44.70 -106.82
REMARK 500 2 ASP A 58 44.63 -152.73
REMARK 500 2 SER A 66 -65.47 -98.60
REMARK 500 2 ARG A 69 -65.92 -12.74
REMARK 500 2 PRO A 74 -177.02 -60.47
REMARK 500 2 ALA A 77 29.39 -77.95
REMARK 500 2 MET A 83 -45.84 -140.61
REMARK 500 2 SER A 85 94.19 -53.98
REMARK 500 2 THR A 86 -45.93 -139.45
REMARK 500 2 ALA A 87 -67.29 -148.35
REMARK 500 2 TYR A 89 46.45 -147.24
REMARK 500 3 TYR A 5 109.40 -50.02
REMARK 500 3 ASN A 6 -62.11 -136.70
REMARK 500 3 ASP A 11 57.50 -101.46
REMARK 500 3 ASP A 20 66.56 -155.24
REMARK 500 3 VAL A 21 -79.05 -148.57
REMARK 500 3 HIS A 49 54.38 -111.88
REMARK 500 3 ASN A 50 54.35 -69.58
REMARK 500 3 LEU A 65 -165.10 -128.61
REMARK 500 3 SER A 66 -64.42 -103.99
REMARK 500 3 ARG A 69 -66.05 -7.52
REMARK 500 3 PRO A 74 179.19 -58.10
REMARK 500 3 ALA A 87 -79.61 -148.37
REMARK 500 3 TYR A 89 46.38 -144.11
REMARK 500 4 TYR A 5 106.91 -51.99
REMARK 500 4 ASN A 6 -61.80 -126.62
REMARK 500 4 ASP A 20 69.63 -154.22
REMARK 500 4 VAL A 21 -80.27 -148.34
REMARK 500 4 HIS A 49 48.34 -102.25
REMARK 500
REMARK 500 THIS ENTRY HAS 136 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2RGF A 1 97 UNP Q12967 GNDS_HUMAN 202 298
SEQRES 1 A 97 ALA LEU PRO LEU TYR ASN GLN GLN VAL GLY ASP CYS CYS
SEQRES 2 A 97 ILE ILE ARG VAL SER LEU ASP VAL ASP ASN GLY ASN MET
SEQRES 3 A 97 TYR LYS SER ILE LEU VAL THR SER GLN ASP LYS ALA PRO
SEQRES 4 A 97 ALA VAL ILE ARG LYS ALA MET ASP LYS HIS ASN LEU GLU
SEQRES 5 A 97 GLU GLU GLU PRO GLU ASP TYR GLU LEU LEU GLN ILE LEU
SEQRES 6 A 97 SER ASP ASP ARG LYS LEU LYS ILE PRO GLU ASN ALA ASN
SEQRES 7 A 97 VAL PHE TYR ALA MET ASN SER THR ALA ASN TYR ASP PHE
SEQRES 8 A 97 VAL LEU LYS LYS ARG THR
HELIX 1 1 ALA A 38 LYS A 48 1 11
HELIX 2 2 PHE A 80 MET A 83 1 4
SHEET 1 A 5 LYS A 28 THR A 33 0
SHEET 2 A 5 CYS A 12 LEU A 19 -1 N VAL A 17 O LYS A 28
SHEET 3 A 5 ASP A 90 LYS A 95 1 N PHE A 91 O ARG A 16
SHEET 4 A 5 TYR A 59 ILE A 64 -1 N ILE A 64 O ASP A 90
SHEET 5 A 5 LYS A 70 ILE A 73 -1 N ILE A 73 O LEU A 61
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - t 27 2 Bytes