Header list of 1ef5.pdb file
Complete list - 16 20 Bytes
HEADER SIGNALING PROTEIN 07-FEB-00 1EF5
TITLE SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RGL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RAS-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS RAS-BINDING DOMAIN, RGL, RAS, RBD, RA, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, SIGNALING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR T.KIGAWA,M.ENDO,Y.ITO,M.SHIROUZU,A.KIKUCHI,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 16-FEB-22 1EF5 1 REMARK
REVDAT 2 24-FEB-09 1EF5 1 VERSN
REVDAT 1 23-FEB-00 1EF5 0
JRNL AUTH T.KIGAWA,M.ENDO,Y.ITO,M.SHIROUZU,A.KIKUCHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF RGL.
JRNL REF FEBS LETT. V. 441 413 1998
JRNL REFN ISSN 0014-5793
JRNL PMID 9891982
JRNL DOI 10.1016/S0014-5793(98)01596-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER, AG. (UXNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1309 RESTRAINTS, 1211 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 56
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 42 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS. N-TERMINAL RESIDUES 632-646 ARE NOT DEFINED BY NMR
REMARK 3 RESTRAINTS AND EXCLUDED FROM THE COORDINATE FILE.
REMARK 4
REMARK 4 1EF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010517.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 200MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM RGL-RBD U-15N,13C; 50MM
REMARK 210 TRIS-HCL; 5MM DTT; 10MM MGCL2;
REMARK 210 200MM NACL; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 1.3, AZARA 1.0, FELIX
REMARK 210 95, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 RES C SSSEQI
REMARK 465 SER A 632
REMARK 465 ILE A 633
REMARK 465 THR A 634
REMARK 465 SER A 635
REMARK 465 THR A 636
REMARK 465 VAL A 637
REMARK 465 LEU A 638
REMARK 465 PRO A 639
REMARK 465 PRO A 640
REMARK 465 VAL A 641
REMARK 465 TYR A 642
REMARK 465 ASN A 643
REMARK 465 GLN A 644
REMARK 465 GLN A 645
REMARK 465 ASN A 646
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 ASP A 648 84.58 45.05
REMARK 500 VAL A 656 56.50 -101.72
REMARK 500 GLU A 657 64.72 -154.76
REMARK 500 ASP A 658 -142.96 42.06
REMARK 500 ASN A 659 114.19 57.64
REMARK 500 TYR A 664 -78.17 -110.05
REMARK 500 SER A 666 48.72 173.09
REMARK 500 LEU A 669 169.31 -44.17
REMARK 500 SER A 671 58.30 170.13
REMARK 500 GLN A 672 104.71 -179.50
REMARK 500 ASP A 673 139.94 170.29
REMARK 500 LYS A 674 -75.72 -174.74
REMARK 500 THR A 675 -179.55 -38.70
REMARK 500 PRO A 676 -27.51 -28.20
REMARK 500 MET A 683 -72.28 -90.06
REMARK 500 LYS A 685 -84.37 -61.92
REMARK 500 HIS A 686 -86.12 -48.34
REMARK 500 ASN A 687 56.59 159.31
REMARK 500 LEU A 688 -163.86 -125.71
REMARK 500 GLU A 689 165.45 -40.19
REMARK 500 ASP A 691 125.54 51.86
REMARK 500 PRO A 692 32.69 -87.22
REMARK 500 ALA A 693 -102.43 -55.90
REMARK 500 ILE A 702 -88.69 -121.13
REMARK 500 GLU A 704 -94.08 56.67
REMARK 500 LYS A 706 76.62 -155.23
REMARK 500 ILE A 710 151.04 58.39
REMARK 500 PRO A 711 -159.57 -64.18
REMARK 500 VAL A 716 91.74 -40.67
REMARK 500 PHE A 717 -62.05 171.90
REMARK 500 ASN A 721 -151.50 -177.10
REMARK 500 GLN A 723 105.92 178.12
REMARK 500 VAL A 724 -162.38 38.24
REMARK 500 LYS A 733 -152.37 -151.93
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 ARG A 653 0.22 SIDE CHAIN
REMARK 500 ARG A 681 0.18 SIDE CHAIN
REMARK 500 ARG A 731 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TRT001000187.1 RELATED DB: TARGETDB
DBREF 1EF5 A 632 734 UNP Q60695 RGL1_MOUSE 632 734
SEQADV 1EF5 ASN A 662 UNP Q60695 HIS 662 SEE REMARK 999
SEQRES 1 A 103 SER ILE THR SER THR VAL LEU PRO PRO VAL TYR ASN GLN
SEQRES 2 A 103 GLN ASN GLU ASP THR CYS ILE ILE ARG ILE SER VAL GLU
SEQRES 3 A 103 ASP ASN ASN GLY ASN MET TYR LYS SER ILE MET LEU THR
SEQRES 4 A 103 SER GLN ASP LYS THR PRO ALA VAL ILE GLN ARG ALA MET
SEQRES 5 A 103 SER LYS HIS ASN LEU GLU SER ASP PRO ALA GLU GLU TYR
SEQRES 6 A 103 GLU LEU VAL GLN VAL ILE SER GLU ASP LYS GLU LEU VAL
SEQRES 7 A 103 ILE PRO ASP SER ALA ASN VAL PHE TYR ALA MET ASN SER
SEQRES 8 A 103 GLN VAL ASN PHE ASP PHE ILE LEU ARG LYS LYS ASN
HELIX 1 1 THR A 675 MET A 683 1 9
SHEET 1 A 4 ILE A 652 VAL A 656 0
SHEET 2 A 4 PHE A 726 LYS A 732 1 O PHE A 726 N ARG A 653
SHEET 3 A 4 TYR A 696 VAL A 701 -1 O GLU A 697 N ARG A 731
SHEET 4 A 4 LEU A 708 VAL A 709 -1 O LEU A 708 N GLN A 700
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
Complete list - 16 20 Bytes