Header list of 5hck.pdb file
Complete list - 9 201 Bytes
HEADER TRANSFERASE 09-MAR-98 5HCK
TITLE HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMATOPOIETIC CELL KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: HCK;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 GENE: RESIDUES G72-E143 OF HUMAN HCK;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-14B;
SOURCE 11 EXPRESSION_SYSTEM_GENE: RESIDUES G72-E143 OF HUMAN HCK
KEYWDS SH3, PROTEIN TYROSINE KINASE, SIGNAL TRANSDUCTION, TRANSFERASE
EXPDTA SOLUTION NMR
AUTHOR D.A.HORITA,D.M.BALDISSERI,W.ZHANG,A.S.ALTIERI,T.E.SMITHGALL,
AUTHOR 2 W.H.GMEINER,R.A.BYRD
REVDAT 3 09-MAY-12 5HCK 1 COMPND VERSN
REVDAT 2 24-FEB-09 5HCK 1 VERSN
REVDAT 1 17-JUN-98 5HCK 0
JRNL AUTH D.A.HORITA,D.M.BALDISSERI,W.ZHANG,A.S.ALTIERI,T.E.SMITHGALL,
JRNL AUTH 2 W.H.GMEINER,R.A.BYRD
JRNL TITL SOLUTION STRUCTURE OF THE HUMAN HCK SH3 DOMAIN AND
JRNL TITL 2 IDENTIFICATION OF ITS LIGAND BINDING SITE.
JRNL REF J.MOL.BIOL. V. 278 253 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9571048
JRNL DOI 10.1006/JMBI.1998.1690
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: PRESENTED ENSEMBLE WAS CALCULATED USING
REMARK 3 NOE/DIHEDRAL AND 1H AND 13C CHEMICAL SHIFT RESTRAINTS.
REMARK 4
REMARK 4 5HCK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.25
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE JRNL ARTICLE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY PLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DG, SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
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 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 GLY A 72
REMARK 465 ILE A 73
REMARK 465 ARG A 74
REMARK 465 GLU A 75
REMARK 465 ALA A 76
REMARK 465 GLY A 77
REMARK 465 LEU A 139
REMARK 465 GLU A 140
REMARK 465 THR A 141
REMARK 465 GLU A 142
REMARK 465 GLU A 143
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 ILE A 92 -57.16 -140.82
REMARK 500 HIS A 93 -167.58 -79.11
REMARK 500 HIS A 94 -77.09 -66.55
REMARK 500 SER A 111 -73.42 -110.00
REMARK 500 THR A 122 12.99 -140.49
REMARK 500 ASP A 137 68.49 -113.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HCK RELATED DB: PDB
DBREF 5HCK A 72 143 UNP P08631 HCK_HUMAN 72 143
SEQRES 1 A 72 GLY ILE ARG GLU ALA GLY SER GLU ASP ILE ILE VAL VAL
SEQRES 2 A 72 ALA LEU TYR ASP TYR GLU ALA ILE HIS HIS GLU ASP LEU
SEQRES 3 A 72 SER PHE GLN LYS GLY ASP GLN MET VAL VAL LEU GLU GLU
SEQRES 4 A 72 SER GLY GLU TRP TRP LYS ALA ARG SER LEU ALA THR ARG
SEQRES 5 A 72 LYS GLU GLY TYR ILE PRO SER ASN TYR VAL ALA ARG VAL
SEQRES 6 A 72 ASP SER LEU GLU THR GLU GLU
HELIX 1 1 SER A 130 TYR A 132 5 3
SHEET 1 A 3 ASP A 103 GLU A 109 0
SHEET 2 A 3 ILE A 82 ALA A 85 -1 N VAL A 83 O MET A 105
SHEET 3 A 3 VAL A 133 VAL A 136 -1 N VAL A 136 O ILE A 82
SHEET 1 B 2 TRP A 114 SER A 119 0
SHEET 2 B 2 LYS A 124 PRO A 129 -1 N ILE A 128 O TRP A 115
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 - 9 201 Bytes