BMRB Entry 34557

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34557
MolProbity Validation Chart

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Title:
Solution structure of the TAF4-RST domain
Deposition date:
2020-09-09
Original release date:
2021-10-01
Authors:
Staby, L.; Davidsen, R.; Bugge, K.; Skriver, K.; Kragelund, B.
Citation:

Citation: Friis Theisen, Frederik; Salladini, Edoardo; Davidsen, Rikke; Jo Rasmussen, Christina; Staby, Lasse; Kragelund, Birthe; Skriver, Karen. "aa-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes"  J. Biol. Chem. 298, 101963-101963 (2022).
PubMed: 35452682

Assembly members:

Assembly members:
entity_1, polymer, 75 residues, 8796.450 Da.

Natural source:

Natural source:   Common Name: Mouse-ear cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MMNPINRNPKQVPFAALLPT LMNQLDKDRALQLRTLYARL KKNEIPKEGFTRHMKDIVGD QMLRMAVSKLQQVNY

Data typeCount
13C chemical shifts345
15N chemical shifts68
1H chemical shifts512

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 75 residues - 8796.450 Da.

1   METMETASNPROILEASNARGASNPROLYS
2   GLNVALPROPHEALAALALEULEUPROTHR
3   LEUMETASNGLNLEUASPLYSASPARGALA
4   LEUGLNLEUARGTHRLEUTYRALAARGLEU
5   LYSLYSASNGLUILEPROLYSGLUGLYPHE
6   THRARGHISMETLYSASPILEVALGLYASP
7   GLNMETLEUARGMETALAVALSERLYSLEU
8   GLNGLNVALASNTYR

Samples:

sample_1: RST domain from TAF4, [U-100% 13C; U-100% 15N], 580 uM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.2 % w/v; DSS 0.7 mM

sample_conditions_1: ionic strength: 143 mM; pH: 7.0; pressure: 1 atm; temperature: 298 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
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D (H)N(CA)NNHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

VnmrJ, Varian - collection

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

PROCHECK / PROCHECK-NMR, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker AVANCE 600 MHz

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