BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19791

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

Data sets:
Data typeCount
13C chemical shifts441
15N chemical shifts121
1H chemical shifts870

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tfb11
2EBNA22

Entities:

Entity 1, Tfb1 115 residues - 12903.807 Da.

1   PROSERHISSERGLYALAALAILEPHEGLU
2   LYSVALSERGLYILEILEALAILEASNGLU
3   ASPVALSERPROALAGLULEUTHRTRPARG
4   SERTHRASPGLYASPLYSVALHISTHRVAL
5   VALLEUSERTHRILEASPLYSLEUGLNALA
6   THRPROALASERSERGLULYSMETMETLEU
7   ARGLEUILEGLYLYSVALASPGLUSERLYS
8   LYSARGLYSASPASNGLUGLYASNGLUVAL
9   VALPROLYSPROGLNARGHISMETPHESER
10   PHEASNASNARGTHRVALMETASPASNILE
11   LYSMETTHRLEUGLNGLNILEILESERARG
12   TYRLYSASPALAASP

Entity 2, EBNA2 13 residues - 1633.681 Da.

1   ASPLEUASPGLUSERTRPASPTYRILEPHE
2   GLUTHRTHR

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_6isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_6isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_6isotropicsample_conditions_1
3D 1H-13C-12C intermolecular NOESYsample_3isotropicsample_conditions_1
3D 1H-13C-12C intermolecular NOESYsample_6isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_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:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts