BMRB Entry 26599

Title:
1H, 13Ca, 13Cb and 15N chemical shift assignment of coiled-coil motif from human Thanatos-associated protein 11
Deposition date:
2015-07-06
Original release date:
2016-05-09
Authors:
Cukier, Cyprian; Milon, Alain; Gervais, Virginie
Citation:

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:

Assembly members:
THAP11, polymer, 68 residues, 8038 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-20

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts130
15N chemical shifts66
1H chemical shifts66

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1THAP11 coiled-coil, chain A1
2THAP11 coiled-coil, chain B1

Entities:

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   GLYALAMETGLYTHRTHRGLUGLUGLULEU
2   LEUARGLYSLEUASNGLUGLNARGASPILE
3   LEUALALEUMETGLUVALLYSMETLYSGLU
4   METLYSGLYSERILEARGHISLEUARGLEU
5   THRGLUALALYSLEUARGGLUGLULEUARG
6   GLULYSASPARGLEULEUALAMETALAVAL
7   ILEARGLYSLYSHISGLYMETTYR

Related Database Links:

UNP Q96EK4
AlphaFold O94795

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks