BMRB Entry 34540

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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/BMR34540
MolProbity Validation Chart

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Title:
TFIIS N-terminal domain (TND) from human MED26
Deposition date:
2020-07-23
Original release date:
2021-11-28
Authors:
Veverka, V.
Citation:

Citation: Cermakova, Katerina; Demeulemeester, Jonas; Lux, Vanda; Nedomova, Monika; Goldman, Seth; Smith, Eric; Srb, Pavel; Hexnerova, Rozalie; Fabry, Milan; Madlikova, Marcela; Horejsi, Magdalena; De Rijck, Jan; Debyser, Zeger; Adelman, Karen; Hodges, H Courtney; Veverka, Vaclav. "A ubiquitous disordered protein interaction module orchestrates transcription elongation"  Science 374, 1113-1121 (2021).
PubMed: 34822292

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, 10183.872 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMTAAPASPQQIRDRLLQAI DPQSNIRNMVAVLEVISSLE KYPITKEALEETRLGKLIND VRKKTKNEELAKRAKKLLRS WQKLIEPAGS

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts89
1H chemical shifts659

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 90 residues - 10183.872 Da.

1   SERMETTHRALAALAPROALASERPROGLN
2   GLNILEARGASPARGLEULEUGLNALAILE
3   ASPPROGLNSERASNILEARGASNMETVAL
4   ALAVALLEUGLUVALILESERSERLEUGLU
5   LYSTYRPROILETHRLYSGLUALALEUGLU
6   GLUTHRARGLEUGLYLYSLEUILEASNASP
7   VALARGLYSLYSTHRLYSASNGLUGLULEU
8   ALALYSARGALALYSLYSLEULEUARGSER
9   TRPGLNLYSLEUILEGLUPROALAGLYSER

Samples:

sample_1: MED26, [U-13C; U-15N], 0.5 mM; TRIS, [U-2H], 25 mM; sodium chloride 200 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 225 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

Sparky, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA, YASARA - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 850 MHz

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