BMRB Entry 30444
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30444
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Title: Solution structure of the Extraterminal (ET) Domain of BRD2
Deposition date: 2018-03-26 Original release date: 2019-03-01
Authors: Houliston, S.; Lemak, A.; Picaud, S.; Filippakopoulos, P.; Arrowsmith, C.
Citation: Houliston, S.; Lemak, A.; Picaud, S.; Filippakopoulos, P.; Arrowsmith, C.. "Solution structure of the Extraterminal (ET) Domain of BRD2" . ., .-..
Assembly members:
entity_1, polymer, 132 residues, 15275.450 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):
entity_1: SMKTAPPALPTGYDSEEEEE
SRPMSYDEKRQLSLDINKLP
GEKLGRVVHIIQAREPSLRD
SNPEEIEIDFETLKPSTLRE
LERYVLSCLRKKPRKPYTIK
KPVGKTKEELALEKKRELEK
RLQDVSGQLNST
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 528 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 864 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 132 residues - 15275.450 Da.
| 1 | SER | MET | LYS | THR | ALA | PRO | PRO | ALA | LEU | PRO | ||||
| 2 | THR | GLY | TYR | ASP | SER | GLU | GLU | GLU | GLU | GLU | ||||
| 3 | SER | ARG | PRO | MET | SER | TYR | ASP | GLU | LYS | ARG | ||||
| 4 | GLN | LEU | SER | LEU | ASP | ILE | ASN | LYS | LEU | PRO | ||||
| 5 | GLY | GLU | LYS | LEU | GLY | ARG | VAL | VAL | HIS | ILE | ||||
| 6 | ILE | GLN | ALA | ARG | GLU | PRO | SER | LEU | ARG | ASP | ||||
| 7 | SER | ASN | PRO | GLU | GLU | ILE | GLU | ILE | ASP | PHE | ||||
| 8 | GLU | THR | LEU | LYS | PRO | SER | THR | LEU | ARG | GLU | ||||
| 9 | LEU | GLU | ARG | TYR | VAL | LEU | SER | CYS | LEU | ARG | ||||
| 10 | LYS | LYS | PRO | ARG | LYS | PRO | TYR | THR | ILE | LYS | ||||
| 11 | LYS | PRO | VAL | GLY | LYS | THR | LYS | GLU | GLU | LEU | ||||
| 12 | ALA | LEU | GLU | LYS | LYS | ARG | GLU | LEU | GLU | LYS | ||||
| 13 | ARG | LEU | GLN | ASP | VAL | SER | GLY | GLN | LEU | ASN | ||||
| 14 | SER | THR |
Samples:
sample_1: BRD2-ET, [U-13C; U-15N], 250 uM; NaCl 500 mM
sample_conditions_1: ionic strength: 500 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
ABACUS, Lemak and Arrowsmith - chemical shift assignment
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker AvanceII 800 MHz
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts