BMRB Entry 19610
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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/BMR19610
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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: Langelaan, David; Smith, Steven; Chitayat, Seth. "Solution NMR structure of the p300 Taz2:ETAD1 complex" Not known ., .-..
Assembly members:
ETAD1, polymer, 39 residues, 4267.949 Da.
Taz2, polymer, 92 residues, 10107.968 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ETAD1: GSMNQPQRMAPVGTDKELSD
LLDFSMMFPLPVTNGKGRP
Taz2: GSATQSPGDSRRLSIQRAIQ
SLVHAAQCRNANCSLPSCQK
MKRVVQHTKGCKRKTNGGCP
ICKQLIALAAYHAKHCQENK
CPVPFCLNIKQK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 558 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 841 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E2A ETAD1 | 1 |
| 2 | p300 Taz2 | 2 |
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 | GLY | SER | MET | ASN | GLN | PRO | GLN | ARG | MET | ALA | ||||
| 2 | PRO | VAL | GLY | THR | ASP | LYS | GLU | LEU | SER | ASP | ||||
| 3 | LEU | LEU | ASP | PHE | SER | MET | MET | PHE | PRO | LEU | ||||
| 4 | PRO | VAL | THR | ASN | GLY | LYS | GLY | ARG | PRO |
Entity 2, p300 Taz2 92 residues - 10107.968 Da.
N terminal GS is remnant of thrombin cleavage site.
| 1 | GLY | SER | ALA | THR | GLN | SER | PRO | GLY | ASP | SER | ||||
| 2 | ARG | ARG | LEU | SER | ILE | GLN | ARG | ALA | ILE | GLN | ||||
| 3 | SER | LEU | VAL | HIS | ALA | ALA | GLN | CYS | ARG | ASN | ||||
| 4 | ALA | ASN | CYS | SER | LEU | PRO | SER | CYS | GLN | LYS | ||||
| 5 | MET | LYS | ARG | VAL | VAL | GLN | HIS | THR | LYS | GLY | ||||
| 6 | CYS | LYS | ARG | LYS | THR | ASN | GLY | GLY | CYS | PRO | ||||
| 7 | ILE | CYS | LYS | GLN | LEU | ILE | ALA | LEU | ALA | ALA | ||||
| 8 | TYR | HIS | ALA | LYS | HIS | CYS | GLN | GLU | ASN | LYS | ||||
| 9 | CYS | PRO | VAL | PRO | PHE | CYS | LEU | ASN | ILE | LYS | ||||
| 10 | GLN | LYS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D HNCACB | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D HNCO | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D HCACO | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | Sample1_ETAD | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | Sample1_ETAD | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2_Taz2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2_Taz2 | isotropic | sample_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
Related Database Links:
| PDB | |
| DBJ | BAG10911 |
| GB | AAA52331 AAA58445 AAA61146 AAC99797 AAI10580 |
| REF | NP_001129611 NP_003191 XP_002923565 XP_003788747 XP_003805069 |
| SP | P15923 |
| BMRB | 15944 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts