BMRB Entry 36340

Title:
Solution structure of the tandem PH and BSD1 domains of TFIIH p62
Deposition date:
2020-04-07
Original release date:
2025-10-13
Authors:
Okuda, M.; Nishimura, Y.
Citation:

Citation: Okuda, Masahiko; Ekimoto, Toru; Kurita, Jun-Ichi; Ikeguchi, Mitsunori; Nishimura, Yoshifumi. "Structural and dynamical insights into the PH domain of p62 in human TFIIH."  Nucleic Acids Res. 49, 2916-2930 (2021).
PubMed: 33211877

Assembly members:

Assembly members:
General transcription factor IIH subunit 1, polymer, 161 residues, 18348.986 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
13C chemical shifts704
15N chemical shifts173
1H chemical shifts922

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 161 residues - 18348.986 Da.

1   GLYSERHISMETALATHRSERSERGLUGLU
2   VALLEULEUILEVALLYSLYSVALARGGLN
3   LYSLYSGLNASPGLYALALEUTYRLEUMET
4   ALAGLUARGILEALATRPALAPROGLUGLY
5   LYSASPARGPHETHRILESERHISMETTYR
6   ALAASPILELYSCYSGLNLYSILESERPRO
7   GLUGLYLYSALALYSILEGLNLEUGLNLEU
8   VALLEUHISALAGLYASPTHRTHRASNPHE
9   HISPHESERASNGLUSERTHRALAVALLYS
10   GLUARGASPALAVALLYSASPLEULEUGLN
11   GLNLEULEUPROLYSPHELYSARGLYSALA
12   ASNLYSGLULEUGLUGLULYSASNARGMET
13   LEUGLNGLUASPPROVALLEUPHEGLNLEU
14   TYRLYSASPLEUVALVALSERGLNVALILE
15   SERALAGLUGLUPHETRPALAASNARGLEU
16   ASNVALASNALATHRASPSERSERSERTHR
17   SER

Samples:

sample_1: TFIIH p62, [U-99% 13C; U-99% 15N], 1.2 mM; potassium phosphate 20 mM; d-DTT', [U-2H], 5 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: TFIIH p62, [U-99% 13C; U-99% 15N], 0.9 mM; potassium phosphate 20 mM; d-DTT', [U-2H], 5 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 bar; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)HBsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HN(CO)CGsample_1isotropicsample_conditions_1
3D HNCGsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker AVANCE III 950 MHz
  • Bruker AVANCE III 600 MHz

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