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PDB ID: 2knc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16496
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Yang, Jun; Ma, Yan-Qing; Page, Richard; Misra, Saurav; Plow, Edward; Qin, Jun. "Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation." Proc. Natl. Acad. Sci. U.S.A. 106, 17729-17734 (2009).
PubMed: 19805198
Assembly members:
AIIbTMCD, polymer, 54 residues, 5653.673 Da.
B3TMCD, polymer, 79 residues, 8371.900 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMAL-C2
Entity Sequences (FASTA):
AIIbTMCD: GAMGSEERAIPIWWVLVGVL
GGLLLLTILVLAMWKVGFFK
RNRPPLEEDDEEGE
B3TMCD: GAMGSKGPDILVVLLSVMGA
ILLIGLAALLIWKLLITIHD
RKEFAKFEEERARAKWDTAN
NPLYKEATSTFTNITYRGT
Data type | Count |
13C chemical shifts | 529 |
15N chemical shifts | 140 |
1H chemical shifts | 860 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 2 |
Entity 1, entity_1 54 residues - 5653.673 Da.
Residues 1-5 is a non-native remaining after enzymatic cleavage
1 | GLY | ALA | MET | GLY | SER | GLU | GLU | ARG | ALA | ILE | ||||
2 | PRO | ILE | TRP | TRP | VAL | LEU | VAL | GLY | VAL | LEU | ||||
3 | GLY | GLY | LEU | LEU | LEU | LEU | THR | ILE | LEU | VAL | ||||
4 | LEU | ALA | MET | TRP | LYS | VAL | GLY | PHE | PHE | LYS | ||||
5 | ARG | ASN | ARG | PRO | PRO | LEU | GLU | GLU | ASP | ASP | ||||
6 | GLU | GLU | GLY | GLU |
Entity 2, entity_2 79 residues - 8371.900 Da.
Residues 1-5 is a non-native remaining after enzymatic cleavage
1 | GLY | ALA | MET | GLY | SER | LYS | GLY | PRO | ASP | ILE | ||||
2 | LEU | VAL | VAL | LEU | LEU | SER | VAL | MET | GLY | ALA | ||||
3 | ILE | LEU | LEU | ILE | GLY | LEU | ALA | ALA | LEU | LEU | ||||
4 | ILE | TRP | LYS | LEU | LEU | ILE | THR | ILE | HIS | ASP | ||||
5 | ARG | LYS | GLU | PHE | ALA | LYS | PHE | GLU | GLU | GLU | ||||
6 | ARG | ALA | ARG | ALA | LYS | TRP | ASP | THR | ALA | ASN | ||||
7 | ASN | PRO | LEU | TYR | LYS | GLU | ALA | THR | SER | THR | ||||
8 | PHE | THR | ASN | ILE | THR | TYR | ARG | GLY | THR |
BMRB | 16497 15552 16771 17930 17932 |
PDB | 2K1A 2K9J 2KNC 1M8O 1S4X 2KV9 2LJD 2LJF |
DBJ | BAG37735 BAI46167 BAE34283 BAG62151 BAJ17755 |
EMBL | CAA29987 CAD29521 |
GB | AAA52597 AAA53150 AAA60114 AAA65936 AAI17444 AAA35927 AAA52589 AAA52600 AAA60122 AAB27096 |
PRF | 1403305A |
REF | NP_000410 XP_001114526 XP_001150497 XP_002827479 XP_003282434 NP_000203 NP_001003162 NP_001075271 NP_001075535 NP_001193419 |
SP | P08514 P53711 O54890 P05106 |
TPG | DAA18403 |
AlphaFold | P08514 P53711 O54890 P05106 |
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