BMRB Entry 19610

Title:
Solution NMR structure of the p300 Taz2:ETAD1 complex
Deposition date:
2013-11-12
Original release date:
2014-11-10
Authors:
Langelaan, David; Smith, Steven; Chitayat, Seth
Citation:

Citation: Lochhead, Marina; Brown, Alexandra; Kirlin, Alyssa; Chitayat, Seth; Munro, Kim; Findlay, Jane; Baillie, George; LeBrun, David; Langelaan, David; Smith, Steven. "Structural insights into TAZ2 domain-mediated CBP/p300 recruitment by transactivation domain 1 of the lymphopoietic transcription factor E2A"  J. Biol. Chem. 295, 4303-4315 (2020).
PubMed: 32098872

Assembly members:

Assembly members:
ETAD1, polymer, 39 residues, 4267.949 Da.
Taz2, polymer, 92 residues, 10107.968 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Pet21

Data sets:
Data typeCount
13C chemical shifts558
15N chemical shifts134
1H chemical shifts841

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E2A ETAD11
2p300 Taz22

Entities:

Entity 1, E2A ETAD1 39 residues - 4267.949 Da.

The first activation domain of the E2A protein. Corresponds to residues 1-37 of E2A. The N terminal GS is an artifact from protease cleavage.

1   GLYSERMETASNGLNPROGLNARGMETALA
2   PROVALGLYTHRASPLYSGLULEUSERASP
3   LEULEUASPPHESERMETMETPHEPROLEU
4   PROVALTHRASNGLYLYSGLYARGPRO

Entity 2, p300 Taz2 92 residues - 10107.968 Da.

N terminal GS is remnant of thrombin cleavage site.

1   GLYSERALATHRGLNSERPROGLYASPSER
2   ARGARGLEUSERILEGLNARGALAILEGLN
3   SERLEUVALHISALAALAGLNCYSARGASN
4   ALAASNCYSSERLEUPROSERCYSGLNLYS
5   METLYSARGVALVALGLNHISTHRLYSGLY
6   CYSLYSARGLYSTHRASNGLYGLYCYSPRO
7   ILECYSLYSGLNLEUILEALALEUALAALA
8   TYRHISALALYSHISCYSGLNGLUASNLYS
9   CYSPROVALPROPHECYSLEUASNILELYS
10   GLNLYS

Samples:

Sample1_ETAD: ETAD1, [U-99% 13C; U-99% 15N], 1.4 mM; Taz2 2 mM; MES 20 mM; sodium azide 1 mM; beta-mercaptoethanol 5 mM; H2O 90%; D2O 10%

sample_2_Taz2: ETAD1 3078 uM; Taz2, [U-99% 13C; U-99% 15N], 1038 uM; MES 20 mM; sodium azide 1 mM; beta-mercaptoethanol 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCSample1_ETADisotropicsample_conditions_1
3D CBCA(CO)NHSample1_ETADisotropicsample_conditions_1
3D HNCACBSample1_ETADisotropicsample_conditions_1
3D HNCOSample1_ETADisotropicsample_conditions_1
3D HCACOSample1_ETADisotropicsample_conditions_1
3D 1H-15N NOESYSample1_ETADisotropicsample_conditions_1
3D HCCH-TOCSYSample1_ETADisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticSample1_ETADisotropicsample_conditions_1
3D 1H-13C NOESY aromaticSample1_ETADisotropicsample_conditions_1
2D 1H-15N HSQCsample_2_Taz2isotropicsample_conditions_1
3D HNCOsample_2_Taz2isotropicsample_conditions_1
3D HCACOsample_2_Taz2isotropicsample_conditions_1
3D HNCACBsample_2_Taz2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2_Taz2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2_Taz2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2_Taz2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2_Taz2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2_Taz2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

Analysis v3, CCPN - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz
  • Varian INOVA 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks