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
MolProbity Validation Chart

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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
Deposition date:
2019-09-27
Original release date:
2020-01-17
Authors:
Allen, M.; Bycoft, M.; Zinzalla, G.
Citation:

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).
PubMed: 31909846

Assembly members:

Assembly members:
entity_1, polymer, 49 residues, 5287.906 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: HLTV

Entity Sequences (FASTA):

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
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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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks