BMRB Entry 25584
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25584
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Title: NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and the N-terminal activation domain of EKLF (TAD1)
Deposition date: 2015-04-27 Original release date: 2016-04-25
Authors: Lecoq, Lauriane; Morse, Thomas; Raiola, Luca; Arseneault, Genevieve; Omichinski, James G.
Citation: Morse, Thomas; Lecoq, Lauriane; Raiola, Luca; Arseneault, Genevieve; Omichinski, James. "Structural Characterization of the Complex between the N-terminal Transactivation Domain of EKLF and the p62/Tfb1 subunit of TFIIH" Not known ., .-..
Assembly members:
RNA_polymerase_II_transcription_factor_B_subunit_1, polymer, 115 residues, 12903.807 Da.
N-terminal_transactivation_domain_of_Krueppel-like_factor_1, polymer, 19 residues, 2359.502 Da.
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RNA_polymerase_II_transcription_factor_B_subunit_1: PSHSGAAIFEKVSGIIAINE
DVSPAELTWRSTDGDKVHTV
VLSTIDKLQATPASSEKMML
RLIGKVDESKKRKDNEGNEV
VPKPQRHMFSFNNRTVMDNI
KMTLQQIISRYKDAD
N-terminal_transactivation_domain_of_Krueppel-like_factor_1: DTQDDFLKWWRSEEAQDMG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 578 |
| 15N chemical shifts | 144 |
| 1H chemical shifts | 938 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 115 residues - 12903.807 Da.
| 1 | PRO | SER | HIS | SER | GLY | ALA | ALA | ILE | PHE | GLU | ||||
| 2 | LYS | VAL | SER | GLY | ILE | ILE | ALA | ILE | ASN | GLU | ||||
| 3 | ASP | VAL | SER | PRO | ALA | GLU | LEU | THR | TRP | ARG | ||||
| 4 | SER | THR | ASP | GLY | ASP | LYS | VAL | HIS | THR | VAL | ||||
| 5 | VAL | LEU | SER | THR | ILE | ASP | LYS | LEU | GLN | ALA | ||||
| 6 | THR | PRO | ALA | SER | SER | GLU | LYS | MET | MET | LEU | ||||
| 7 | ARG | LEU | ILE | GLY | LYS | VAL | ASP | GLU | SER | LYS | ||||
| 8 | LYS | ARG | LYS | ASP | ASN | GLU | GLY | ASN | GLU | VAL | ||||
| 9 | VAL | PRO | LYS | PRO | GLN | ARG | HIS | MET | PHE | SER | ||||
| 10 | PHE | ASN | ASN | ARG | THR | VAL | MET | ASP | ASN | ILE | ||||
| 11 | LYS | MET | THR | LEU | GLN | GLN | ILE | ILE | SER | ARG | ||||
| 12 | TYR | LYS | ASP | ALA | ASP |
Entity 2, entity_2 19 residues - 2359.502 Da.
| 1 | ASP | THR | GLN | ASP | ASP | PHE | LEU | LYS | TRP | TRP | ||||
| 2 | ARG | SER | GLU | GLU | ALA | GLN | ASP | MET | GLY |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 2 mM; H2O 90%; D2O 10%
sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 2 mM; D2O 100%
sample_3: entity_2, [U-100% 13C; U-100% 15N], 0.8 mM; entity_1 2 mM; H2O 90%; D2O 10%
sample_4: entity_2, [U-100% 13C; U-100% 15N], 0.8 mM; entity_1 2 mM; D2O 100%
sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D intermolecular NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_4 | isotropic | sample_conditions_1 |
| 3D intermolecular NOESY | sample_4 | isotropic | sample_conditions_1 |
Software:
No software information available
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts