Header list of 1rax.pdb file
Complete list - t 27 2 Bytes
HEADER RAS-BINDING DOMAIN 13-MAR-99 1RAX
TITLE RA-DOMAIN OF RAL GUANOSINE-NUCLEOTIDE DISSOCIATION STIMULATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (RA-DOMAIN OF RAL GUANOSINE DISSOCIATION
COMPND 3 STIMULATOR);
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RAS-BINDING DOMAIN;
COMPND 6 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: RALGDS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HUMAN RALGDS GENE (RALGDS)
KEYWDS RAS-BINDING DOMAIN, RALGEF, RALGDS, RAS, RA
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.D.MUELLER,L.HANDEL,P.SCHMIEDER,H.OSCHKINAT
REVDAT 5 27-OCT-21 1RAX 1 SOURCE REMARK
REVDAT 4 06-NOV-19 1RAX 1 JRNL REMARK
REVDAT 3 24-FEB-09 1RAX 1 VERSN
REVDAT 2 26-SEP-01 1RAX 3 ATOM
REVDAT 1 19-MAR-99 1RAX 0
JRNL AUTH T.D.MUELLER,L.HANDEL,P.SCHMIEDER,H.OSCHKINAT
JRNL TITL HIGH-RESOLUTION STRUCTURE OF THE RA-DOMAIN OF HUMAN RALGDS
JRNL TITL 2 AND A DYNAMICS STUDY OF ITS BINDING LOOP TO RAS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.HUANG,X.WENG,F.HOFER,G.S.MARTIN,S.H.KIM
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE RAS-INTERACTING DOMAIN OF
REMARK 1 TITL 2 RALGDS.
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 609 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 9253406
REMARK 1 DOI 10.1038/NSB0897-609
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.GEYER,C.HERRMANN,S.WOHLGEMUTH,A.WITTINGHOFER,H.R.KALBITZER
REMARK 1 TITL STRUCTURE OF THE RAS-BINDING DOMAIN OF RALGEF AND
REMARK 1 TITL 2 IMPLICATIONS FOR RAS BINDING AND SIGNALLING.
REMARK 1 REF NAT.STRUCT.BIOL. V. 4 694 1997
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 9302994
REMARK 1 DOI 10.1038/NSB0997-694
REMARK 1 REFERENCE 3
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 PMID 8636102
REMARK 1 DOI 10.1074/JBC.271.12.6794
REMARK 1 REFERENCE 4
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 PMID 7809086
REMARK 1 DOI 10.1073/PNAS.91.26.12609
REMARK 1 REFERENCE 5
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 PMID 7972015
REMARK 1 DOI 10.1073/PNAS.91.23.11089
REMARK 1 REFERENCE 6
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 1 PMID 8094051
REMARK 1 DOI 10.1002/J.1460-2075.1993.TB05662.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RAX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000646.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H; 13C; 15N
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.1, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST TOTAL
REMARK 210 ENERGY AND NOE ENERGY WERE
REMARK 210 SELECTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 HIS A 4
REMARK 465 MET A 5
REMARK 465 LEU A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 CYS A 12
REMARK 465 ASN A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 PRO A 19
REMARK 465 LEU A 20
REMARK 465 TYR A 21
REMARK 465 ASN A 22
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
REMARK 500 REMARK: NULL
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 3 HIS A 65 CG HIS A 65 CD2 0.056
REMARK 500 7 HIS A 65 CG HIS A 65 CD2 0.070
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 GLN A 24 171.60 63.37
REMARK 500 1 ASP A 27 114.33 175.73
REMARK 500 1 ASP A 36 69.05 -69.52
REMARK 500 1 VAL A 37 -82.19 -104.57
REMARK 500 1 ASP A 38 -73.33 168.30
REMARK 500 1 ASN A 41 -149.35 -153.45
REMARK 500 1 SER A 50 -53.02 -24.26
REMARK 500 1 ASP A 52 108.11 -28.63
REMARK 500 1 LEU A 81 -77.22 -106.74
REMARK 500 1 ASP A 83 45.88 -78.67
REMARK 500 1 ASP A 84 -31.89 168.57
REMARK 500 1 ASN A 94 100.12 -43.52
REMARK 500 1 ALA A 103 -149.65 -103.43
REMARK 500 1 PHE A 114 63.66 -62.46
REMARK 500 2 ASP A 27 85.19 173.96
REMARK 500 2 ASP A 38 -82.83 66.59
REMARK 500 2 ASN A 39 162.20 -43.85
REMARK 500 2 TYR A 43 121.52 63.02
REMARK 500 2 SER A 50 -58.23 -28.74
REMARK 500 2 ASP A 74 33.89 -96.23
REMARK 500 2 LEU A 81 -75.18 -100.77
REMARK 500 2 ASP A 83 63.92 31.16
REMARK 500 2 ASP A 84 -29.94 84.40
REMARK 500 2 ASN A 94 104.12 -42.26
REMARK 500 2 ALA A 103 -144.73 -78.88
REMARK 500 2 TYR A 105 54.46 -91.73
REMARK 500 2 THR A 113 173.40 -52.19
REMARK 500 2 PHE A 114 69.77 -61.49
REMARK 500 3 ASP A 36 53.93 -105.06
REMARK 500 3 ASP A 38 -14.90 78.21
REMARK 500 3 ASN A 41 144.77 168.04
REMARK 500 3 GLN A 51 -29.87 175.54
REMARK 500 3 LEU A 81 -90.23 -114.40
REMARK 500 3 ASP A 83 -64.69 -29.14
REMARK 500 3 ASN A 92 21.60 -149.09
REMARK 500 3 ASN A 94 107.17 -41.27
REMARK 500 3 ASN A 100 98.57 -41.26
REMARK 500 3 TYR A 105 49.19 -89.40
REMARK 500 3 ARG A 112 64.36 -62.20
REMARK 500 3 PHE A 114 104.04 63.87
REMARK 500 4 ASP A 27 107.80 72.07
REMARK 500 4 VAL A 37 -75.93 -103.91
REMARK 500 4 ASP A 38 -73.39 167.72
REMARK 500 4 TYR A 43 105.02 62.27
REMARK 500 4 SER A 50 -58.16 -28.39
REMARK 500 4 ASP A 74 30.36 -91.68
REMARK 500 4 SER A 82 174.72 172.53
REMARK 500 4 ASN A 94 107.32 -53.13
REMARK 500 4 ASN A 100 96.64 -43.10
REMARK 500 4 PHE A 114 116.20 -163.20
REMARK 500
REMARK 500 THIS ENTRY HAS 139 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 32 0.24 SIDE CHAIN
REMARK 500 1 ARG A 59 0.24 SIDE CHAIN
REMARK 500 1 ARG A 85 0.30 SIDE CHAIN
REMARK 500 1 ARG A 112 0.27 SIDE CHAIN
REMARK 500 2 ARG A 32 0.12 SIDE CHAIN
REMARK 500 2 ARG A 59 0.19 SIDE CHAIN
REMARK 500 2 ARG A 85 0.09 SIDE CHAIN
REMARK 500 2 ARG A 112 0.19 SIDE CHAIN
REMARK 500 3 ARG A 32 0.29 SIDE CHAIN
REMARK 500 3 ARG A 59 0.22 SIDE CHAIN
REMARK 500 3 ARG A 85 0.12 SIDE CHAIN
REMARK 500 3 ARG A 112 0.32 SIDE CHAIN
REMARK 500 4 ARG A 32 0.20 SIDE CHAIN
REMARK 500 4 ARG A 59 0.14 SIDE CHAIN
REMARK 500 4 ARG A 85 0.32 SIDE CHAIN
REMARK 500 4 ARG A 112 0.32 SIDE CHAIN
REMARK 500 5 ARG A 32 0.31 SIDE CHAIN
REMARK 500 5 ARG A 59 0.22 SIDE CHAIN
REMARK 500 5 ARG A 85 0.14 SIDE CHAIN
REMARK 500 5 ARG A 112 0.22 SIDE CHAIN
REMARK 500 6 ARG A 32 0.33 SIDE CHAIN
REMARK 500 6 ARG A 59 0.31 SIDE CHAIN
REMARK 500 6 ARG A 85 0.24 SIDE CHAIN
REMARK 500 6 ARG A 112 0.28 SIDE CHAIN
REMARK 500 7 ARG A 32 0.30 SIDE CHAIN
REMARK 500 7 ARG A 59 0.32 SIDE CHAIN
REMARK 500 7 ARG A 85 0.28 SIDE CHAIN
REMARK 500 7 ARG A 112 0.14 SIDE CHAIN
REMARK 500 8 ARG A 32 0.12 SIDE CHAIN
REMARK 500 8 ARG A 59 0.31 SIDE CHAIN
REMARK 500 8 ARG A 85 0.21 SIDE CHAIN
REMARK 500 8 ARG A 112 0.22 SIDE CHAIN
REMARK 500 9 ARG A 32 0.14 SIDE CHAIN
REMARK 500 9 ARG A 59 0.31 SIDE CHAIN
REMARK 500 9 ARG A 85 0.31 SIDE CHAIN
REMARK 500 9 ARG A 112 0.32 SIDE CHAIN
REMARK 500 10 ARG A 32 0.25 SIDE CHAIN
REMARK 500 10 ARG A 59 0.30 SIDE CHAIN
REMARK 500 10 ARG A 85 0.12 SIDE CHAIN
REMARK 500 10 ARG A 112 0.24 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RAX A 1 115 UNP Q12967 GNDS_HUMAN 185 300
SEQRES 1 A 115 GLY SER PRO HIS MET LEU SER GLY SER GLY LEU CYS ASN
SEQRES 2 A 115 SER SER SER ALA LEU PRO LEU TYR ASN GLN GLN VAL GLY
SEQRES 3 A 115 ASP CYS CYS ILE ILE ARG VAL SER LEU ASP VAL ASP ASN
SEQRES 4 A 115 GLY ASN MET TYR LYS SER ILE LEU VAL THR SER GLN ASP
SEQRES 5 A 115 LYS ALA PRO ALA VAL ILE ARG LYS ALA MET ASP LYS HIS
SEQRES 6 A 115 ASN LEU GLU GLU GLU GLU PRO GLU ASP TYR GLU LEU LEU
SEQRES 7 A 115 GLN ILE LEU SER ASP ASP ARG LYS LEU LYS ILE PRO GLU
SEQRES 8 A 115 ASN ALA ASN VAL PHE TYR ALA MET ASN SER THR ALA ASN
SEQRES 9 A 115 TYR ASP PHE VAL LEU LYS LYS ARG THR PHE THR
HELIX 1 1 ALA A 54 HIS A 65 1 12
HELIX 2 2 VAL A 95 ALA A 98 1 4
SHEET 1 A 5 LYS A 44 THR A 49 0
SHEET 2 A 5 CYS A 28 LEU A 35 -1 N VAL A 33 O LYS A 44
SHEET 3 A 5 ASP A 106 LYS A 111 1 N PHE A 107 O ARG A 32
SHEET 4 A 5 TYR A 75 ILE A 80 -1 N ILE A 80 O ASP A 106
SHEET 5 A 5 LYS A 86 ILE A 89 -1 N ILE A 89 O LEU A 77
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