BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34437

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. ., .-. (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)

Entity Sequences (FASTA):
entity_1: SQMSDLPVKVIHVESGKILT GTDAPKAGQLEAWLEMNPGY EVAPRSDSE

Data sets:
Data typeCount
13C chemical shifts172
15N chemical shifts48
1H chemical shifts338

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 49 residues - 5287.906 Da.

1   SERGLNMETSERASPLEUPROVALLYSVAL
2   ILEHISVALGLUSERGLYLYSILELEUTHR
3   GLYTHRASPALAPROLYSALAGLYGLNLEU
4   GLUALATRPLEUGLUMETASNPROGLYTYR
5   GLUVALALAPROARGSERASPSERGLU

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:

NameSampleSample stateSample conditions
2D NOESYsample_2isotropicsample_conditions_1
2D TOCSYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts