HEADER CELL ADHESION 19-JAN-04 1S4W
TITLE NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF INTEGRIN AIIB IN DPC
TITLE 2 MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYTOPLASMIC DOMAIN (RESIDUES 1020-1039);
COMPND 5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB, CD41
COMPND 6 ANTIGEN;
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 GENE: ITGA2B, ITGAB, GP2B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET31B
KEYWDS CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR O.VINOGRADOVA,J.VAYNBERG,X.KONG,T.A.HAAS,E.F.PLOW,J.QIN
REVDAT 4 02-MAR-22 1S4W 1 REMARK
REVDAT 3 24-FEB-09 1S4W 1 VERSN
REVDAT 2 06-APR-04 1S4W 1 JRNL
REVDAT 1 09-MAR-04 1S4W 0
JRNL AUTH O.VINOGRADOVA,J.VAYNBERG,X.KONG,T.A.HAAS,E.F.PLOW,J.QIN
JRNL TITL MEMBRANE-MEDIATED STRUCTURAL TRANSITIONS AT THE CYTOPLASMIC
JRNL TITL 2 FACE DURING INTEGRIN ACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 4094 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15024114
JRNL DOI 10.1073/PNAS.0400742101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, X-PLOR
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S4W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021370.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 300 MM DDPC, 95/5% H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
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
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY AND
REMARK 210 DYNAMIC SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 99
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
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 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 H GLU A 13 H GLU A 14 1.34
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 PHE A 4 -68.94 -26.27
REMARK 500 1 PRO A 11 -156.21 -44.94
REMARK 500 1 LEU A 12 12.97 58.91
REMARK 500 1 GLU A 14 30.22 32.54
REMARK 500 1 ASP A 15 37.60 -160.37
REMARK 500 1 GLU A 17 16.43 87.89
REMARK 500 1 GLU A 18 19.01 80.54
REMARK 500 2 VAL A 2 50.11 -68.77
REMARK 500 2 PHE A 4 -68.34 -25.26
REMARK 500 2 ARG A 9 107.56 -44.41
REMARK 500 2 PRO A 11 -160.44 -45.53
REMARK 500 2 GLU A 14 28.87 32.58
REMARK 500 2 ASP A 15 35.67 -168.79
REMARK 500 2 GLU A 17 13.91 88.59
REMARK 500 2 GLU A 18 17.40 81.21
REMARK 500 3 VAL A 2 45.15 -145.40
REMARK 500 3 PHE A 4 -69.55 -26.81
REMARK 500 3 PRO A 11 -153.55 -56.94
REMARK 500 3 LEU A 12 12.85 58.41
REMARK 500 3 GLU A 14 24.58 34.56
REMARK 500 3 ASP A 15 34.38 -163.73
REMARK 500 3 GLU A 17 14.03 94.98
REMARK 500 3 GLU A 18 16.64 80.47
REMARK 500 4 VAL A 2 47.98 -74.06
REMARK 500 4 PHE A 4 -69.59 -26.99
REMARK 500 4 PRO A 11 -153.18 -46.32
REMARK 500 4 GLU A 14 31.66 31.08
REMARK 500 4 ASP A 15 35.44 -160.86
REMARK 500 4 GLU A 17 15.85 96.56
REMARK 500 4 GLU A 18 16.24 80.64
REMARK 500 5 VAL A 2 49.52 -153.15
REMARK 500 5 PHE A 4 -69.43 -27.05
REMARK 500 5 PRO A 11 176.47 -42.82
REMARK 500 5 LEU A 12 -10.40 67.82
REMARK 500 5 GLU A 14 178.41 -53.00
REMARK 500 5 ASP A 15 25.22 -74.06
REMARK 500 5 GLU A 18 -10.22 -145.01
REMARK 500 6 PHE A 4 -69.04 -26.83
REMARK 500 6 PRO A 11 -155.93 -48.76
REMARK 500 6 LEU A 12 -54.43 76.90
REMARK 500 6 GLU A 14 -34.51 -33.83
REMARK 500 6 ASP A 16 -18.23 -38.71
REMARK 500 6 GLU A 18 -75.91 -39.17
REMARK 500 7 VAL A 2 54.42 -68.52
REMARK 500 7 PHE A 4 -69.17 -29.57
REMARK 500 7 PRO A 11 40.05 -56.51
REMARK 500 7 GLU A 14 26.29 33.25
REMARK 500 7 ASP A 15 37.72 -165.95
REMARK 500 7 GLU A 17 10.46 108.23
REMARK 500 8 VAL A 2 44.50 -78.12
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S4X RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE CYTOPLASMIC DOMAIN OF INTEGRIN B3 IN DPC
REMARK 900 MICELLES
DBREF 1S4W A 1 20 UNP P08514 ITA2B_HUMAN 1020 1039
SEQRES 1 A 20 LYS VAL GLY PHE PHE LYS ARG ASN ARG PRO PRO LEU GLU
SEQRES 2 A 20 GLU ASP ASP GLU GLU GLY GLU
HELIX 1 1 VAL A 2 ARG A 7 1 6
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
(ATOM LINES ARE NOT SHOWN.)
END