BMRB Entry 34535
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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/BMR34535
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Title: Human TFIIS N-terminal domain (TND) PubMed: 34822292
Deposition date: 2020-07-23 Original release date: 2021-11-28
Authors: Veverka, V.
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).
Assembly members:
entity_1, polymer, 81 residues, 9064.700 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MEDEVVRFAKKMDKMVQKKN
AAGALDLLKELKNIPMTLEL
LQSTRIGMSVNAIRKQSTDE
EVTSLAKSLIKSWKKLLDGG
S
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 357 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 609 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 81 residues - 9064.700 Da.
| 1 | MET | GLU | ASP | GLU | VAL | VAL | ARG | PHE | ALA | LYS | ||||
| 2 | LYS | MET | ASP | LYS | MET | VAL | GLN | LYS | LYS | ASN | ||||
| 3 | ALA | ALA | GLY | ALA | LEU | ASP | LEU | LEU | LYS | GLU | ||||
| 4 | LEU | LYS | ASN | ILE | PRO | MET | THR | LEU | GLU | LEU | ||||
| 5 | LEU | GLN | SER | THR | ARG | ILE | GLY | MET | SER | VAL | ||||
| 6 | ASN | ALA | ILE | ARG | LYS | GLN | SER | THR | ASP | GLU | ||||
| 7 | GLU | VAL | THR | SER | LEU | ALA | LYS | SER | LEU | ILE | ||||
| 8 | LYS | SER | TRP | LYS | LYS | LEU | LEU | ASP | GLY | GLY | ||||
| 9 | SER |
Samples:
sample_1: TFIIS, [U-13C; U-15N], 0.5 mM; TRIS, deuterated, 25 mM; sodium phospate 200 mM; TCEP 1 mM
sample_conditions_1: ionic strength: 225 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - processing
Sparky, Goddard - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
YASARA, Yasara - refinement
NMR spectrometers:
- Bruker AVANCE 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts