Header list of 1i98.pdb file
Complete list - 23 20 Bytes
HEADER CELL ADHESION 18-MAR-01 1I98
TITLE NMR ENSEMBLE OF ION-SELECTIVE LIGAND D18 FOR PLATELET INTEGRIN
TITLE 2 ALPHAIIB-BETA3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ION-SELECTIVE LIGAND D18;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED: COMMERCIAL
SOURCE 4 SOLID PHASE WITH CYCLIZATION WITH SELECTIVE DISULPHIDE OXIDATION.
KEYWDS INTEGRIN, RGD, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR J.W.SMITH,H.LE CALVEZ,L.PARRA-GESSERT,N.E.PREECE,X.JIA,N.ASSA-MUNT
REVDAT 3 23-FEB-22 1I98 1 REMARK LINK
REVDAT 2 24-FEB-09 1I98 1 VERSN
REVDAT 1 10-JUL-02 1I98 0
JRNL AUTH J.W.SMITH,H.LE CALVEZ,L.PARRA-GESSERT,N.E.PREECE,X.JIA,
JRNL AUTH 2 N.ASSA-MUNT
JRNL TITL SELECTION AND STRUCTURE OF ION-SELECTIVE LIGANDS FOR
JRNL TITL 2 PLATELET INTEGRIN ALPHA IIB(BETA) 3.
JRNL REF J.BIOL.CHEM. V. 277 10298 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11748219
JRNL DOI 10.1074/JBC.M108071200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8.5.1 (CHEM.SHIFT.MODULE)
REMARK 3 AUTHORS : BRUNGER A. NILGES M. (KUSZWESKI J. CLORE G.M.)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ENSEMBLE D18 IS BASED ON A TOTAL OF 70 NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS,
REMARK 3 8 DIHEDRAL ANGLE RESTRAINTS, 1 COVALENT ACE-CYS-SS-CYS BOND AND 1
REMARK 3 LRGD I,I+3
REMARK 3 HYDROGEN BOND RESPECTIVELY. REFINEMENTS INCORPORATED ALPHA PROTON
REMARK 3 AND ALPHA,
REMARK 3 BETA CARBON SHIFTS OF 10 RESIDUES.
REMARK 4
REMARK 4 1I98 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013063.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278.00
REMARK 210 PH : 6.50
REMARK 210 IONIC STRENGTH : 10MM PHOSPHATE/5% D2O
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3MG D18/ML
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY & DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, FELIX 2000
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210 AND CHEMICAL SHIFT REFINEMENT.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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: THE ENSEMBLE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR
REMARK 210 NMR TECHNIQUES (CIRCA 2000)
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: 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 ASP A 8 -157.49 -98.18
REMARK 500 1 ARG A 10 -167.33 -71.84
REMARK 500 1 GLN A 11 -175.82 -56.09
REMARK 500 2 TRP A 4 53.46 -115.16
REMARK 500 2 LEU A 5 52.97 -91.93
REMARK 500 2 ASP A 8 32.89 38.41
REMARK 500 3 ARG A 3 -82.88 -122.46
REMARK 500 3 LEU A 5 59.25 -91.12
REMARK 500 3 ASP A 8 -151.08 64.08
REMARK 500 3 ARG A 10 46.19 -89.36
REMARK 500 4 TRP A 9 -105.64 -91.35
REMARK 500 4 ARG A 10 47.50 -101.36
REMARK 500 5 ASP A 8 -89.34 55.58
REMARK 500 7 LEU A 5 64.45 -112.72
REMARK 500 7 ASP A 8 -72.96 64.89
REMARK 500 8 TRP A 9 -78.81 -101.11
REMARK 500 9 TRP A 4 -156.57 -155.86
REMARK 500 9 LEU A 5 -145.02 -77.76
REMARK 500 9 ASP A 8 -138.74 60.98
REMARK 500 10 ARG A 3 66.45 -118.91
REMARK 500 10 LEU A 5 53.63 -101.53
REMARK 500 10 ASP A 8 81.38 55.92
REMARK 500 10 TRP A 9 -155.79 -101.02
REMARK 500 10 ARG A 10 -165.56 -70.61
REMARK 500 11 TRP A 4 54.13 -117.67
REMARK 500 11 LEU A 5 52.34 -115.82
REMARK 500 12 LEU A 5 78.48 -113.05
REMARK 500 12 ASP A 8 44.08 39.48
REMARK 500 12 TRP A 9 -166.37 -78.91
REMARK 500 13 LEU A 5 66.01 -100.77
REMARK 500 14 ASP A 8 49.08 -86.55
REMARK 500 15 ASP A 8 -147.06 -91.47
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 3 0.31 SIDE CHAIN
REMARK 500 1 ARG A 6 0.30 SIDE CHAIN
REMARK 500 1 ARG A 10 0.31 SIDE CHAIN
REMARK 500 2 ARG A 3 0.29 SIDE CHAIN
REMARK 500 2 ARG A 6 0.30 SIDE CHAIN
REMARK 500 2 ARG A 10 0.28 SIDE CHAIN
REMARK 500 3 ARG A 3 0.31 SIDE CHAIN
REMARK 500 3 ARG A 6 0.31 SIDE CHAIN
REMARK 500 3 ARG A 10 0.31 SIDE CHAIN
REMARK 500 4 ARG A 3 0.28 SIDE CHAIN
REMARK 500 4 ARG A 6 0.24 SIDE CHAIN
REMARK 500 4 ARG A 10 0.26 SIDE CHAIN
REMARK 500 5 ARG A 3 0.32 SIDE CHAIN
REMARK 500 5 ARG A 6 0.30 SIDE CHAIN
REMARK 500 5 ARG A 10 0.26 SIDE CHAIN
REMARK 500 6 ARG A 3 0.32 SIDE CHAIN
REMARK 500 6 ARG A 6 0.31 SIDE CHAIN
REMARK 500 6 ARG A 10 0.24 SIDE CHAIN
REMARK 500 7 ARG A 3 0.24 SIDE CHAIN
REMARK 500 7 ARG A 6 0.31 SIDE CHAIN
REMARK 500 7 ARG A 10 0.29 SIDE CHAIN
REMARK 500 8 ARG A 3 0.29 SIDE CHAIN
REMARK 500 8 ARG A 6 0.29 SIDE CHAIN
REMARK 500 8 ARG A 10 0.27 SIDE CHAIN
REMARK 500 9 ARG A 3 0.29 SIDE CHAIN
REMARK 500 9 ARG A 6 0.30 SIDE CHAIN
REMARK 500 9 ARG A 10 0.26 SIDE CHAIN
REMARK 500 10 ARG A 3 0.30 SIDE CHAIN
REMARK 500 10 ARG A 6 0.32 SIDE CHAIN
REMARK 500 10 ARG A 10 0.30 SIDE CHAIN
REMARK 500 11 ARG A 3 0.30 SIDE CHAIN
REMARK 500 11 ARG A 6 0.31 SIDE CHAIN
REMARK 500 11 ARG A 10 0.25 SIDE CHAIN
REMARK 500 12 ARG A 3 0.32 SIDE CHAIN
REMARK 500 12 ARG A 6 0.32 SIDE CHAIN
REMARK 500 12 ARG A 10 0.32 SIDE CHAIN
REMARK 500 13 ARG A 3 0.32 SIDE CHAIN
REMARK 500 13 ARG A 6 0.31 SIDE CHAIN
REMARK 500 13 ARG A 10 0.25 SIDE CHAIN
REMARK 500 14 ARG A 3 0.31 SIDE CHAIN
REMARK 500 14 ARG A 6 0.32 SIDE CHAIN
REMARK 500 14 ARG A 10 0.21 SIDE CHAIN
REMARK 500 15 ARG A 3 0.30 SIDE CHAIN
REMARK 500 15 ARG A 6 0.23 SIDE CHAIN
REMARK 500 15 ARG A 10 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 13
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6Y RELATED DB: PDB
REMARK 900 NMR ENSEMBLE OF ION-SELECTIVE LIGAND A1 FOR PLATELET INTEGRIN
REMARK 900 ALPHAIIB-BETA3
REMARK 900 RELATED ID: 1I8E RELATED DB: PDB
REMARK 900 NMR ENSEMBLE OF ION-SELECTIVE LIGAND A22 FOR PLATELET INTEGRIN
REMARK 900 ALPHAIIB-BETA3
REMARK 900 RELATED ID: 1I93 RELATED DB: PDB
REMARK 900 NMR ENSEMBLE OF ION-SELECTIVE LIGAND D16 FOR PLATELET INTEGRIN
REMARK 900 ALPHAIIB-BETA3
DBREF 1I98 A 1 13 PDB 1I98 1I98 1 13
SEQRES 1 A 13 ACE CYS ARG TRP LEU ARG GLY ASP TRP ARG GLN CYS NH2
HET ACE A 1 6
HET NH2 A 13 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 2 CYS A 12 1555 1555 2.02
LINK C ACE A 1 N CYS A 2 1555 1555 1.31
LINK C CYS A 12 N NH2 A 13 1555 1555 1.31
SITE 1 AC1 2 ASP A 8 ARG A 10
SITE 1 AC2 1 CYS A 12
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 - 23 20 Bytes