Header list of 1dpq.pdb file
Complete list - 3 20 Bytes
HEADER CELL ADHESION 27-DEC-99 1DPQ
TITLE SOLUTION STRUCTURE OF THE CONSTITUTIVELY ACTIVE MUTANT OF THE INTEGRIN
TITLE 2 ALPHA IIB CYTOPLASMIC DOMAIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYTOPLASMIC DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF RESIDUES IS NATURALLY FOUND IN THE PLATELETS OF HOMO SAPIENS
SOURCE 5 (HUMAN).
KEYWDS HELIX, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 11
MDLTYP MINIMIZED AVERAGE
AUTHOR O.VINOGRADOVA,T.HAAS,E.F.PLOW,J.QIN
REVDAT 4 03-NOV-21 1DPQ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1DPQ 1 VERSN
REVDAT 2 01-APR-03 1DPQ 1 JRNL
REVDAT 1 28-FEB-00 1DPQ 0
JRNL AUTH O.VINOGRADOVA,T.HAAS,E.F.PLOW,J.QIN
JRNL TITL A STRUCTURAL BASIS FOR INTEGRIN ACTIVATION BY THE
JRNL TITL 2 CYTOPLASMIC TAIL OF THE ALPHA IIB-SUBUNIT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 1450 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10677482
JRNL DOI 10.1073/PNAS.040548197
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.5, X-PLOR 3.2
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010271.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3 MM PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, PIPP, X-PLOR 3.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DEUT. DPC(DODECYL-PHOSPHOCHOLINE) MICELLES USED
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: 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 O GLU A 14 H ASP A 16 1.54
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 VAL A 2 47.38 34.33
REMARK 500 1 ARG A 9 -9.19 -57.42
REMARK 500 1 LEU A 12 41.72 72.60
REMARK 500 1 ASP A 15 53.15 -68.20
REMARK 500 1 ASP A 16 38.53 -69.77
REMARK 500 2 VAL A 2 46.28 34.38
REMARK 500 2 ARG A 9 -8.11 -53.98
REMARK 500 2 LEU A 12 40.18 80.35
REMARK 500 2 ASP A 15 50.83 -68.10
REMARK 500 2 ASP A 16 37.93 -70.08
REMARK 500 3 VAL A 2 48.49 23.22
REMARK 500 3 ARG A 9 -8.08 -53.00
REMARK 500 3 LEU A 12 40.26 81.13
REMARK 500 3 ASP A 15 60.31 -67.14
REMARK 500 3 ASP A 16 36.79 -70.84
REMARK 500 4 VAL A 2 46.92 34.21
REMARK 500 4 ARG A 9 -7.77 -58.24
REMARK 500 4 LEU A 12 40.10 79.92
REMARK 500 4 ASP A 15 60.27 -66.18
REMARK 500 4 ASP A 16 37.92 -70.50
REMARK 500 5 VAL A 2 51.45 22.00
REMARK 500 5 ARG A 9 -8.82 -51.63
REMARK 500 5 LEU A 12 41.30 73.12
REMARK 500 5 ASP A 16 38.53 -70.32
REMARK 500 6 VAL A 2 47.56 34.21
REMARK 500 6 ARG A 9 -8.40 -53.24
REMARK 500 6 LEU A 12 23.56 115.32
REMARK 500 6 GLU A 13 37.19 78.37
REMARK 500 6 ASP A 16 39.24 -70.48
REMARK 500 7 VAL A 2 47.09 33.99
REMARK 500 7 ARG A 9 -9.05 -52.94
REMARK 500 7 LEU A 12 41.46 73.29
REMARK 500 7 GLU A 14 -71.12 -46.03
REMARK 500 7 ASP A 15 67.24 -65.62
REMARK 500 7 ASP A 16 36.01 -71.67
REMARK 500 8 VAL A 2 48.28 23.14
REMARK 500 8 ARG A 9 -6.83 -55.35
REMARK 500 8 LEU A 12 40.98 83.00
REMARK 500 8 ASP A 15 50.83 -66.51
REMARK 500 8 ASP A 16 39.87 -71.71
REMARK 500 9 VAL A 2 48.76 22.88
REMARK 500 9 ARG A 9 -8.88 -54.84
REMARK 500 9 LEU A 12 40.65 70.69
REMARK 500 9 GLU A 14 -84.85 -56.15
REMARK 500 9 ASP A 16 28.30 -73.93
REMARK 500 10 VAL A 2 47.76 34.02
REMARK 500 10 ARG A 9 -8.82 -58.69
REMARK 500 10 LEU A 12 40.91 72.82
REMARK 500 10 ASP A 15 71.44 45.68
REMARK 500 10 ASP A 16 31.14 -142.77
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DPK RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE INTEGRIN ALPHA IIB CYTOPLASMIC DOMAIN
DBREF 1DPQ A 1 20 UNP P08514 ITA2B_HUMAN 1020 1039
SEQADV 1DPQ ALA A 10 UNP P08514 PRO 1029 ENGINEERED MUTATION
SEQADV 1DPQ ALA A 11 UNP P08514 PRO 1030 ENGINEERED MUTATION
SEQRES 1 A 20 LYS VAL GLY PHE PHE LYS ARG ASN ARG ALA ALA LEU GLU
SEQRES 2 A 20 GLU ASP ASP GLU GLU GLY GLU
HELIX 1 1 VAL A 2 ALA A 10 1 9
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 - 3 20 Bytes