BMRB Entry 30368
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30368
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Title: Solution NMR structure of Brd3 ET domain bound to Brg1 peptide PubMed: 29567837
Deposition date: 2017-10-28 Original release date: 2018-03-14
Authors: Szyszka, T.; Wai, D.; 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, 87 residues, 10179.387 Da.
entity_2, polymer, 12 residues, 1417.829 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: ASASYDSEEEEEGLPMSYDE
KRQLSLDINRLPGEKLGRVV
HIIQSREPSLRDSNPDEIEI
DFETLKPTTLRELERYVKSC
LQKKQRK
entity_2: RSVKVKIKLGRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 352 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 669 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 87 residues - 10179.387 Da.
| 1 | ALA | SER | ALA | SER | TYR | ASP | SER | GLU | GLU | GLU | ||||
| 2 | GLU | GLU | GLY | LEU | PRO | MET | SER | TYR | ASP | GLU | ||||
| 3 | LYS | ARG | GLN | LEU | SER | LEU | ASP | ILE | ASN | ARG | ||||
| 4 | LEU | PRO | GLY | GLU | LYS | LEU | GLY | ARG | VAL | VAL | ||||
| 5 | HIS | ILE | ILE | GLN | SER | ARG | GLU | PRO | SER | LEU | ||||
| 6 | ARG | ASP | SER | ASN | PRO | ASP | GLU | ILE | GLU | ILE | ||||
| 7 | ASP | PHE | GLU | THR | LEU | LYS | PRO | THR | THR | LEU | ||||
| 8 | ARG | GLU | LEU | GLU | ARG | TYR | VAL | LYS | SER | CYS | ||||
| 9 | LEU | GLN | LYS | LYS | GLN | ARG | LYS |
Entity 2, entity_2 12 residues - 1417.829 Da.
| 1 | ARG | SER | VAL | LYS | VAL | LYS | ILE | LYS | LEU | GLY | ||||
| 2 | ARG | LYS |
Samples:
sample_1: Brd3_ET 300 uM; Brg1 600 uM; Roche Complete Protease Inhibitor 0.02%; DSS 166 uM; NaCl 50 mM
sample_2: Brd3_ET, [U-15N], 300 uM; Brg1 600 uM; Roche Complete Protease Inhibitor 0.02%; DSS 166 uM; NaCl 50 mM
sample_3: Brd3_ET, [U-13C; U-15N], 300 uM; Brg1 600 uM; Roche Complete Protease Inhibitor 0.02%; DSS 166 uM; NaCl 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K
sample_conditions_3: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_3 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_3 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_2 |
| 3D 13C/15N (F2/F1) Filtered, 1H-1H NOESY | sample_3 | isotropic | sample_conditions_3 |
| 2D 13C/15N (F2/F1) Filtered, 1H-1H NOESY | sample_3 | isotropic | sample_conditions_3 |
| 2D 13C/15N (F2/F1) Filtered, 1H-1H TOCSY | sample_3 | isotropic | sample_conditions_3 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_3 |
| 3D HCCH-COSY | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_3 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_3 |
| 3D H(CC)(CO)HN | sample_3 | isotropic | sample_conditions_3 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_3 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_3 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_3 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- 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