BMRB Entry 34004

Title:
Solution structure of the human SNF5/INI1 domain
Deposition date:
2016-06-02
Original release date:
2017-05-04
Authors:
Allen, M.; Zinzalla, G.; Bycroft, Mark
Citation:

Citation: Sammak, Susan; Allen, Mark; Hamdani, Najoua; Bycroft, Mark; Zinzalla, Giovanna. "The structure of INI1/hSNF5 RPT1 and its interactions with the c-MYC:MAX heterodimer provide insights into the interplay between MYC and the SWI/SNF chromatin remodeling complex"  FEBS J. 285, 4165-4180 (2018).
PubMed: 30222246

Assembly members:

Assembly members:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1, polymer, 78 residues, 8821.944 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1: GGSEVLVPIRLDMEIDGQKL RDAFTWNMNEKLMTPEMFSE ILCDDLDLNPLTFVPAIASA IRQQIESYPTDSILEDQS

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts77
1H chemical shifts568

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 78 residues - 8821.944 Da.

1   GLYGLYSERGLUVALLEUVALPROILEARG
2   LEUASPMETGLUILEASPGLYGLNLYSLEU
3   ARGASPALAPHETHRTRPASNMETASNGLU
4   LYSLEUMETTHRPROGLUMETPHESERGLU
5   ILELEUCYSASPASPLEUASPLEUASNPRO
6   LEUTHRPHEVALPROALAILEALASERALA
7   ILEARGGLNGLNILEGLUSERTYRPROTHR
8   ASPSERILELEUGLUASPGLNSER

Samples:

sample_1: beta-mercaptoethanol, [U-100% 2H], 5 mM; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: beta-mercaptoethanol, [U-100% 2H], 5 mM; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 600 MHz

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