BMRB Entry 34437
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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/BMR34437
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Title: Structure of the BRK domain of the SWI/SNF chromatin remodelling complex subunit BRG1 reveals a potential role in protein-protein interactions PubMed: 31909846
Deposition date: 2019-09-27 Original release date: 2020-01-17
Authors: Allen, M.; Bycoft, M.; Zinzalla, G.
Citation: Allen, M.; Bycoft, M.; Zinzalla, G.. "Structure of the BRK domain of the SWI/SNF chromatin remodeling complex subunit BRG1 reveals a potential role in protein-protein interactions" Protein Sci. 29, 1047-1053 (2020).
Assembly members:
entity_1, polymer, 49 residues, 5287.906 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 BL21(DE3) Vector: HLTV
Entity Sequences (FASTA):
entity_1: SQMSDLPVKVIHVESGKILT
GTDAPKAGQLEAWLEMNPGY
EVAPRSDSE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 172 |
| 15N chemical shifts | 48 |
| 1H chemical shifts | 338 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 49 residues - 5287.906 Da.
| 1 | SER | GLN | MET | SER | ASP | LEU | PRO | VAL | LYS | VAL | ||||
| 2 | ILE | HIS | VAL | GLU | SER | GLY | LYS | ILE | LEU | THR | ||||
| 3 | GLY | THR | ASP | ALA | PRO | LYS | ALA | GLY | GLN | LEU | ||||
| 4 | GLU | ALA | TRP | LEU | GLU | MET | ASN | PRO | GLY | TYR | ||||
| 5 | GLU | VAL | ALA | PRO | ARG | SER | ASP | SER | GLU |
Samples:
sample_1: BRG1 BRK domain, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 20 mM; NaCl 100 mM; beta-mercaptoethanol 5 mM
sample_2: BRG1 BRK domain 2 mM; potassium phosphate 20 mM; NaCl 100 mM; beta-mercaptoethanol 5 mM
sample_3: BRG1 BRK domain, [U-10% 13C], 1 mM; potassium phosphate 20 mM; NaCl 100 mM; beta-mercaptoethanol 5 mM
sample_conditions_1: ionic strength: 140 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
ANSIG, Kraulis - chemical shift assignment
Azara, Boucher - processing
NMR spectrometers:
- Bruker AVANCE 800 MHz
- Bruker AVANCE 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts