BMRB Entry 30367
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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/BMR30367
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Title: Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide PubMed: 29567837
Deposition date: 2017-10-28 Original release date: 2018-03-14
Authors: Wai, D.; Szyszka, T.; Campbell, A.; Kwong, C.; Wilkinson-White, L.; Silva, A.; Low, J.; Kwan, A.; Gamsjaeger, R.; Lu, B.; Vakoc, C.; Blobel, G.; Mackay, J.
Citation: Wai, Dorothy; Szyszka, Taylor; Campbell, Amy; Kwong, Cherry; Wilkinson-White, Lorna; Silva, Ana; Low, Jason; Kwan, Ann; Gamsjaeger, Roland; Chalmers, James; Patrick, Wayne; Lu, Bin; Vakoc, Christopher; Blobel, Gerd; Mackay, Joel. "The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators" J. Biol. Chem. 293, 7160-7175 (2018).
Assembly members:
entity_1, polymer, 12 residues, 1273.629 Da.
entity_2, polymer, 93 residues, 10687.956 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: KVAPLKIKLGGF
entity_2: GPLGSASASYDSEEEEEGLP
MSYDEKRQLSLDINRLPGEK
LGRVVHIIQSREPSLRDSNP
DEIEIDFETLKPTTLRELER
YVKSCLQKKQRKP
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 354 |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 603 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 12 residues - 1273.629 Da.
| 1 | LYS | VAL | ALA | PRO | LEU | LYS | ILE | LYS | LEU | GLY | ||||
| 2 | GLY | PHE |
Entity 2, entity_2 93 residues - 10687.956 Da.
| 1 | GLY | PRO | LEU | GLY | SER | ALA | SER | ALA | SER | TYR | ||||
| 2 | ASP | SER | GLU | GLU | GLU | GLU | GLU | GLY | LEU | PRO | ||||
| 3 | MET | SER | TYR | ASP | GLU | LYS | ARG | GLN | LEU | SER | ||||
| 4 | LEU | ASP | ILE | ASN | ARG | LEU | PRO | GLY | GLU | LYS | ||||
| 5 | LEU | GLY | ARG | VAL | VAL | HIS | ILE | ILE | GLN | SER | ||||
| 6 | ARG | GLU | PRO | SER | LEU | ARG | ASP | SER | ASN | PRO | ||||
| 7 | ASP | GLU | ILE | GLU | ILE | ASP | PHE | GLU | THR | LEU | ||||
| 8 | LYS | PRO | THR | THR | LEU | ARG | GLU | LEU | GLU | ARG | ||||
| 9 | TYR | VAL | LYS | SER | CYS | LEU | GLN | LYS | LYS | GLN | ||||
| 10 | ARG | LYS | PRO |
Samples:
sample_1: BRD3, [U-13C; U-15N], 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM
sample_2: BRD3, [U-13C; U-15N], 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM
sample_3: BRD3 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C (F1)-filtered NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N13C (F2,F1)-filtered) 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY v3.1.3, Goddard - chemical shift assignment, peak picking
TOPSPIN v3.5.6, Bruker Biospin - processing
NMR spectrometers:
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts