Header list of 1drs.pdb file
Complete list - b 16 2 Bytes
HEADER CELL ADHESION PROTEIN 29-SEP-94 1DRS
TITLE THREE-DIMENSIONAL STRUCTURE OF THE RGD-CONTAINING NEUROTOXIN
TITLE 2 HOMOLOGUE, DENDROASPIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DENDROASPIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENDROASPIS JAMESONI KAIMOSAE;
SOURCE 3 ORGANISM_COMMON: EASTERN JAMESON'S MAMBA;
SOURCE 4 ORGANISM_TAXID: 8619;
SOURCE 5 STRAIN: KAIMOSAE
KEYWDS CELL ADHESION PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 39
AUTHOR M.J.SUTCLIFFE,M.JASEJA,E.I.HYDE,X.LU,J.A.WILLIAMS
REVDAT 4 16-FEB-22 1DRS 1 REMARK
REVDAT 3 24-FEB-09 1DRS 1 VERSN
REVDAT 2 01-APR-03 1DRS 1 JRNL
REVDAT 1 20-DEC-94 1DRS 0
JRNL AUTH M.J.SUTCLIFFE,M.JASEJA,E.I.HYDE,X.LU,J.A.WILLIAMS
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE RGD-CONTAINING NEUROTOXIN
JRNL TITL 2 HOMOLOGUE DENDROASPIN.
JRNL REF NAT.STRUCT.BIOL. V. 1 802 1994
JRNL REFN ISSN 1072-8368
JRNL PMID 7634091
JRNL DOI 10.1038/NSB1194-802
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.JASEJA,X.LU,J.A.WILLIAMS,M.J.SUTCLIFFE,V.V.KAKKAR,
REMARK 1 AUTH 2 R.A.PARSLOW,E.I.HYDE
REMARK 1 TITL 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF DENDROASPIN,
REMARK 1 TITL 2 AN RGD-CONTAINING GLYCOPROTEIN IIBIIIA (ALPHAIIB-BETA3)
REMARK 1 TITL 3 ANTAGONIST WITH A NEUROTOXIN FOLD
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER, DGII
REMARK 3 AUTHORS : BIOSYM TECHNOLOGIES INC. (DISCOVER), HAVEL (DGII)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DRS 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_1000172913.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 39
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RGD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1DRS A 1 59 UNP P28375 MAMB_DENJA 1 59
SEQRES 1 A 59 ARG ILE CYS TYR ASN HIS LEU GLY THR LYS PRO PRO THR
SEQRES 2 A 59 THR GLU THR CYS GLN GLU ASP SER CYS TYR LYS ASN ILE
SEQRES 3 A 59 TRP THR PHE ASP ASN ILE ILE ARG ARG GLY CYS GLY CYS
SEQRES 4 A 59 PHE THR PRO ARG GLY ASP MET PRO GLY PRO TYR CYS CYS
SEQRES 5 A 59 GLU SER ASP LYS CYS ASN LEU
SHEET 1 S1 2 ARG A 1 ASN A 5 0
SHEET 2 S1 2 THR A 13 CYS A 17 -1 O GLU A 15 N CYS A 3
SHEET 1 S2 3 TYR A 50 CYS A 52 0
SHEET 2 S2 3 SER A 21 LYS A 24 -1 O CYS A 22 N CYS A 52
SHEET 3 S2 3 GLY A 36 GLY A 38 -1 O GLY A 36 N TYR A 23
SSBOND 1 CYS A 3 CYS A 22 1555 1555 2.05
SSBOND 2 CYS A 17 CYS A 37 1555 1555 2.07
SSBOND 3 CYS A 39 CYS A 51 1555 1555 2.04
SSBOND 4 CYS A 52 CYS A 57 1555 1555 2.06
SITE 1 RGD 3 ARG A 43 GLY A 44 ASP A 45
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 - b 16 2 Bytes