Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26599
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Citation: Cukier, Cyprian; Gervais, Virginie. "The C-terminal region of the transcriptional regulator THAP11 forms a parallel coiled-coil domain involved in protein dimerization" J. Struct. Biol. 194, 337-346 (2016).
PubMed: 26975212
Assembly members:
THAP11, polymer, 68 residues, 8038 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: pETM-20
Entity Sequences (FASTA):
THAP11: GAMGTTEEELLRKLNEQRDI
LALMEVKMKEMKGSIRHLRL
TEAKLREELREKDRLLAMAV
IRKKHGMY
Data type | Count |
13C chemical shifts | 130 |
15N chemical shifts | 66 |
1H chemical shifts | 66 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | THAP11 coiled-coil, chain A | 1 |
2 | THAP11 coiled-coil, chain B | 1 |
Entity 1, THAP11 coiled-coil, chain A 68 residues - 8038 Da.
N-terminal GAM residues are the result of clonic procedure. The C-terminal Y residue was introduced to facilitate protein quantification. This is a coiled-coil motif of THAP11 protein.
1 | GLY | ALA | MET | GLY | THR | THR | GLU | GLU | GLU | LEU | ||||
2 | LEU | ARG | LYS | LEU | ASN | GLU | GLN | ARG | ASP | ILE | ||||
3 | LEU | ALA | LEU | MET | GLU | VAL | LYS | MET | LYS | GLU | ||||
4 | MET | LYS | GLY | SER | ILE | ARG | HIS | LEU | ARG | LEU | ||||
5 | THR | GLU | ALA | LYS | LEU | ARG | GLU | GLU | LEU | ARG | ||||
6 | GLU | LYS | ASP | ARG | LEU | LEU | ALA | MET | ALA | VAL | ||||
7 | ILE | ARG | LYS | LYS | HIS | GLY | MET | TYR |
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