BMRB Entry 17456

Title:
1H, 15N, 13C chemical shift assignment of the THAP domain 1-81 from the cell growth suppressor human THAP11 protein
Deposition date:
2011-02-11
Original release date:
2012-09-24
Authors:
Durand, Jade; Milon, Alain; Gervais, Virginie
Citation:

Citation: Gervais, Virginie; Campagne, Sebastien; Durand, Jade; Muller, Isabelle; Milon, Alain. "NMR studies of a new family of DNA binding proteins: the THAP proteins."  J. Biomol. NMR 56, 3-15 (2013).
PubMed: 23306615

Assembly members:

Assembly members:
THAP_domain, polymer, 81 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: pGEX-4T2

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts342
15N chemical shifts76
1H chemical shifts530

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1THAP domain of human THAP111
2ZINC ION2

Entities:

Entity 1, THAP domain of human THAP11 81 residues - Formula weight is not available

1   GLYSERPROGLYPHETHRCYSCYSVALPRO
2   GLYCYSTYRASNASNSERHISARGASPLYS
3   ALALEUHISPHETYRTHRPHEPROLYSASP
4   ALAGLULEUARGARGLEUTRPLEULYSASN
5   VALSERARGALAGLYVALSERGLYCYSPHE
6   SERTHRPHEGLNPROTHRTHRGLYHISARG
7   LEUCYSSERVALHISPHEGLNGLYGLYARG
8   LYSTHRTYRTHRVALARGVALPROTHRILE
9   PHE

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: THAP domain, [U-99% 13C; U-99% 15N], 0,5 mM; Tris-HCl 50 mM; sodium chloride 30 mM; DTT 5 mM

sample_2: THAP domain 0,7 mM; Tris-HCl 50 mM; sodium chloride 30 mM; DTT 5 mM

sample_3: THAP domain, [U-99% 15N], 0,7 mM; Tris-HCl 50 mM; sodium chloride 30 mM; DTT 5 mM

sample_conditions_1: ionic strength: 30 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking, processing

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz
  • Bruker Avance 600 MHz

Related Database Links:

SP Q96EK4 A5PKF5 Q96EK4 Q9JJD0
PDB
DBJ BAA95063 BAE38498 BAE41810 BAF82056
GB AAH12182 AAI38967 AAI38988 AAI42470 ABM83526
REF NP_001098464 NP_001100892 NP_001233111 NP_065190 NP_067488
TPG DAA20120
AlphaFold O94795 A5PKF5 Q96EK4 Q9JJD0

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