BMRB Entry 11324

Title:
Solution structure of the thap domain of the human thap domain-containing protein 2
Deposition date:
2010-08-10
Original release date:
2011-08-19
Authors:
Miyamoto, K.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation:

Citation: Miyamoto, K.; Kigawa, T.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the thap domain of the human thap domain-containing protein 2"  .

Assembly members:

Assembly members:
THAP, polymer, 99 residues, Formula weight is not available
ZINC ION, 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P050302-85

Data sets:
Data typeCount
13C chemical shifts415
15N chemical shifts81
1H chemical shifts625

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1THAP1
2ZINC ION2

Entities:

Entity 1, THAP 99 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETPROTHR
2   ASNCYSALAALAALAGLYCYSALATHRTHR
3   TYRASNLYSHISILEASNILESERPHEHIS
4   ARGPHEPROLEUASPPROLYSARGARGLYS
5   GLUTRPVALARGLEUVALARGARGLYSASN
6   PHEVALPROGLYLYSHISTHRPHELEUCYS
7   SERLYSHISPHEGLUALASERCYSPHEASP
8   LEUTHRGLYGLNTHRARGARGLEULYSMET
9   ASPALAVALPROTHRILEPHEASPPHECYS
10   THRHISILESERGLYPROSERSERGLY

Entity 2, ZINC ION - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: THAP domain, [U-13C; U-15N], 0.84 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; ZnCl2 0.05 mM; IDA 1.0 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B., A. - data analysis

Kujira v0.9321, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAG36240 BAI46412
EMBL CAB66542 CAG38516 CAH91411 CAL37961
GB AAH08358 AIC52465 EAW97265 EHH20970 EHH66496
REF NP_001153224 NP_001180430 NP_113623 XP_002752807 XP_003126431
SP Q9H0W7
AlphaFold Q9H0W7

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