LinkDB: 2K1A
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HEADER CELL ADHESION 25-FEB-08 2K1A
TITLE BICELLE-EMBEDDED INTEGRIN ALPHA(IIB) TRANSMEMBRANE SEGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANSMEMBRANE REGION;
COMPND 5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB,
COMPND 6 GPIIB, CD41 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, GP2B, ITGAB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET44-GB3R-AIIB,TM
KEYWDS SINGLE-PASS TRANSMEMBRANE SEGMENT, ALTERNATIVE SPLICING,
KEYWDS 2 CALCIUM, CELL ADHESION, CLEAVAGE ON PAIR OF BASIC RESIDUES,
KEYWDS 3 DISEASE MUTATION, GLYCOPROTEIN, INTEGRIN, POLYMORPHISM,
KEYWDS 4 PYRROLIDONE CARBOXYLIC ACID, RECEPTOR
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR T.-L.LAU,V.DUA,T.S.ULMER
REVDAT 3 24-FEB-09 2K1A 1 VERSN
REVDAT 2 17-JUN-08 2K1A 1 JRNL
REVDAT 1 15-APR-08 2K1A 0
JRNL AUTH T.L.LAU,V.DUA,T.S.ULMER
JRNL TITL STRUCTURE OF THE INTEGRIN {ALPHA}IIB TRANSMEMBRANE
JRNL TITL 2 SEGMENT.
JRNL REF J.BIOL.CHEM. V. 283 16162 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18417472
JRNL DOI 10.1074/JBC.M801748200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2K1A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-08.
REMARK 100 THE RCSB ID CODE IS RCSB100549.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308.2
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 0.025
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM [U-100% 13C; U-100%
REMARK 210 15N; 80% 2H] PROTEIN, 95% H2O/
REMARK 210 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D TRIPLE RESONANCE, 3D HNCO-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR_NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 21
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 ALA A 958 -50.35 -162.88
REMARK 500 1 ALA A 963 -14.85 72.16
REMARK 500 1 ILE A 964 61.12 17.29
REMARK 500 1 PRO A 965 68.34 -63.57
REMARK 500 1 ARG A 995 -78.67 -115.63
REMARK 500 1 ASN A 996 17.66 45.56
REMARK 500 2 ALA A 963 0.78 -154.82
REMARK 500 2 PHE A 992 -1.64 -52.64
REMARK 500 3 PHE A 992 -1.24 -52.50
REMARK 500 4 ILE A 964 77.35 49.01
REMARK 500 4 PHE A 992 -1.95 -52.98
REMARK 500 5 GLU A 960 -76.33 -56.27
REMARK 500 5 PRO A 965 44.13 -77.47
REMARK 500 5 PHE A 992 -0.93 -54.13
REMARK 500 5 LYS A 994 129.52 60.28
REMARK 500 5 ARG A 997 163.40 -41.39
REMARK 500 6 PHE A 992 0.26 -57.45
REMARK 500 6 LYS A 994 105.22 62.71
REMARK 500 7 PHE A 992 -1.56 -52.63
REMARK 500 7 LYS A 994 -39.64 -161.58
REMARK 500 8 PRO A 965 48.33 -76.83
REMARK 500 8 PHE A 992 -2.91 -53.02
REMARK 500 8 LYS A 994 -178.93 54.80
REMARK 500 9 ALA A 963 -158.85 44.19
REMARK 500 9 ILE A 964 74.63 -172.37
REMARK 500 9 PRO A 965 47.54 -80.19
REMARK 500 9 PHE A 992 -1.37 -52.67
REMARK 500 9 ARG A 997 154.90 -44.50
REMARK 500 11 ILE A 964 84.52 46.89
REMARK 500 11 PHE A 992 -1.58 -53.00
REMARK 500 12 ALA A 963 -165.96 43.01
REMARK 500 12 PHE A 992 -1.37 -52.63
REMARK 500 12 ARG A 997 153.48 -49.57
REMARK 500 13 ALA A 963 13.20 -148.32
REMARK 500 13 PHE A 992 -2.17 -51.93
REMARK 500 13 ARG A 995 -126.47 -88.62
REMARK 500 14 ALA A 958 94.54 46.15
REMARK 500 14 ILE A 964 79.16 60.35
REMARK 500 14 PHE A 992 -1.81 -53.40
REMARK 500 15 GLU A 960 82.83 37.78
REMARK 500 15 PHE A 992 -1.87 -52.79
REMARK 500 15 ARG A 995 36.03 -88.83
REMARK 500 16 ILE A 964 72.28 29.94
REMARK 500 16 PHE A 992 -2.50 -52.16
REMARK 500 17 ILE A 964 72.45 -173.15
REMARK 500 18 ALA A 963 80.16 165.88
REMARK 500 18 ILE A 964 70.41 41.10
REMARK 500 18 PHE A 992 -2.98 -51.92
REMARK 500 19 GLU A 960 -167.95 49.46
REMARK 500 19 ILE A 964 52.75 -142.80
REMARK 500 20 LEU A 959 -169.04 56.11
REMARK 500 20 GLU A 961 68.14 36.45
REMARK 500 21 PHE A 992 -2.67 -53.52
REMARK 500 21 ARG A 997 160.05 -47.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX DETERMINATION METHOD: AUTHOR
DBREF 2K1A A 958 998 UNP P08514 ITA2B_HUMAN 989 1029
SEQADV 2K1A GLY A 957 UNP P08514 EXPRESSION TAG
SEQRES 1 A 42 GLY ALA LEU GLU GLU ARG ALA ILE PRO ILE TRP TRP VAL
SEQRES 2 A 42 LEU VAL GLY VAL LEU GLY GLY LEU LEU LEU LEU THR ILE
SEQRES 3 A 42 LEU VAL LEU ALA MET TRP LYS VAL GLY PHE PHE LYS ARG
SEQRES 4 A 42 ASN ARG PRO
HELIX 1 1 ILE A 966 LYS A 989 1 24
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