BMRB Entry 19791
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19791
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Title: Structural Characterization of a Complex Between the Acidic Transactivation Domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. PubMed: 24675874
Deposition date: 2014-02-12 Original release date: 2014-03-03
Authors: R. Chabot, Philippe; Raiola, Luca; Lussier-Price, Mathieu; Morse, Thomas; Arseneault, Genevieve; Archambault, Jacques; Omichinski, James
Citation: Chabot, Philippe; Raiola, Luca; Lussier-Price, Mathieu; Morse, Thomas; Arseneault, Genevieve; Archambault, Jacques; Omichinski, James. "Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH." PLoS Pathog. 10, e1004042-e1004042 (2014).
Assembly members:
Tfb1, polymer, 115 residues, 12903.807 Da.
EBNA2, polymer, 13 residues, 1633.681 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
KMTLQQIISRYKDAD
EBNA2: DLDESWDYIFETT
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 441 |
15N chemical shifts | 121 |
1H chemical shifts | 870 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Tfb1 | 1 |
2 | EBNA2 | 2 |
Entities:
Entity 1, Tfb1 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, EBNA2 13 residues - 1633.681 Da.
1 | ASP | LEU | ASP | GLU | SER | TRP | ASP | TYR | ILE | PHE | ||||
2 | GLU | THR | THR |
Samples:
sample_1: Tfb1, [U-13C; U-15N], 0.7 mM; EBNA2 2.1 mM; sodium phosphate 20 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_2: Tfb1, [U-15N], 0.7 mM; EBNA2 2.1 mM; sodium phosphate 20 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_3: Tfb1, [U-13C; U-15N], 0.7 mM; EBNA2 2.1 mM; sodium phosphate 20 mM; DTT 1 mM; D2O 100%
sample_4: EBNA2, [U-13C; U-15N], 0.5 mM; Tfb1 1.5 mM; sodium phosphate 20 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_5: EBNA2, [U-100% 15N], 0.5 mM; Tfb1 1.5 mM; sodium phosphate 20 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_6: EBNA2, [U-13C; U-15N], 0.5 mM; Tfb1 1.5 mM; sodium phosphate 20 mM; DTT 1 mM; D2O 100%
sample_conditions_1: ionic strength: 20 mM; 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 |
2D 1H-15N HSQC | sample_4 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_6 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_5 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_6 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_6 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_6 | isotropic | sample_conditions_1 |
3D 1H-13C-12C intermolecular NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C-12C intermolecular NOESY | sample_6 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_4 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_4 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_4 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_4 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
CCPNMR, CCPN - data analysis
TALOS vTALOS-N, Cornilescu, Delaglio and Bax - geometry optimization
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
Related Database Links:
BMRB | 18229 18842 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:
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SPARKY: Backbone
or all simulated shifts