BMRB Entry 18229
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18229
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Title: NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2 PubMed: 22373916
Deposition date: 2012-01-27 Original release date: 2012-03-02
Authors: Lafrance-Vanasse, Julien; Legault, Pascale; Omichinski, James G.
Citation: Lafrance-Vanasse, Julien; Arseneault, Genevieve; Cappadocia, Laurent; Chen, Hung-Ta; Legault, Pascale; Omichinski, James. "Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2." Nucleic Acids Res. 40, 5739-5750 (2012).
Assembly members:
Tfb1, polymer, 119 residues, 12903.807 Da.
Rad2, polymer, 52 residues, 2279.496 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Tfb1: PSHSGAAIFEKVSGIIAINE
DVSPAELTWRSTDGDKVHTV
VLSTIDKLQATPASSEKMML
RLIGKVDESKKRKDNEGNEV
VPKPQRHMFSFNNRTVMDNI
KMTLQQIISRYKDADGNSS
Rad2: GSEILERESEKESSNDENKD
DDLEVLSEELFEDVPTKSQI
SKEAEDNDSRKY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 690 |
| 15N chemical shifts | 173 |
| 1H chemical shifts | 1092 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tfb1 | 1 |
| 2 | Rad2 | 2 |
Entities:
Entity 1, Tfb1 119 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 | GLY | ASN | SER | SER |
Entity 2, Rad2 52 residues - 2279.496 Da.
| 1 | GLY | SER | GLU | ILE | LEU | GLU | ARG | GLU | SER | GLU | ||||
| 2 | LYS | GLU | SER | SER | ASN | ASP | GLU | ASN | LYS | ASP | ||||
| 3 | ASP | ASP | LEU | GLU | VAL | LEU | SER | GLU | GLU | LEU | ||||
| 4 | PHE | GLU | ASP | VAL | PRO | THR | LYS | SER | GLN | ILE | ||||
| 5 | SER | LYS | GLU | ALA | GLU | ASP | ASN | ASP | SER | ARG | ||||
| 6 | LYS | TYR |
Samples:
sample_1: Tfb1, [U-100% 13C; U-100% 15N], 1 mM; Rad2 1.25 mM; sodium phosphate 20 mM; EDTA 1 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_2: Tfb1, [U-100% 13C; U-100% 15N], 1 mM; Rad2 1.25 mM; sodium phosphate 20 mM; EDTA 1 mM; DTT 1 mM; D2O 100%
sample_3: Tfb1, [U-100% 15N], 1 mM; Rad2 1.25 mM; sodium phosphate 20 mM; EDTA 1 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_4: Tfb1 1.25 mM; Rad2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; EDTA 1 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_5: Tfb1 1.25 mM; Rad2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; EDTA 1 mM; DTT 1 mM; D2O 100%
sample_6: Tfb1 1.25 mM; Rad2, [U-100% 15N], 1 mM; sodium phosphate 20 mM; EDTA 1 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_6 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_5 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_4 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_5 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_6 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_5 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.1, CCPN - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRView, Johnson, One Moon Scientific - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
VNMR, Varian - collection
TALOS, Cornilescu, Delaglio and Bax - data analysis
VNMRJ, Varian - collection
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Related Database Links:
| BMRB | 18842 19791 25540 |
| PDB | |
| DBJ | GAA22531 |
| EMBL | CAY78811 |
| GB | AAA35143 AAB64747 AAU09707 AHY75284 AJP38011 |
| REF | NP_010597 |
| SP | P32776 |
| TPG | DAA12150 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts