BMRB Entry 26041

Title:
Solution NMR structures of BRD4 ET domain in complex with NSD3_1 peptide
Deposition date:
2016-04-18
Original release date:
2016-06-30
Authors:
Zeng, Lei; ZHOU, MING-MING
Citation:

Citation: Zhang, Qiang; Zeng, Lei; Shen, Chen; Ju, Ying; Konuma, Tsuyoshi; Zhao, Chengcheng; Vakoc, Christopher; ZHOU, MING-MING. "Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4"  Structure 24, 1201-1208 (2016).
PubMed: 27291650

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 9745.218 Da.
entity_2, polymer, 12 residues, 1431.754 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   Vector: pET32A

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts82
1H chemical shifts663

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 83 residues - 9745.218 Da.

1   SERGLUGLUGLUASPLYSCYSLYSPROMET
2   SERTYRGLUGLULYSARGGLNLEUSERLEU
3   ASPILEASNLYSLEUPROGLYGLULYSLEU
4   GLYARGVALVALHISILEILEGLNSERARG
5   GLUPROSERLEULYSASNSERASNPROASP
6   GLUILEGLUILEASPPHEGLUTHRLEULYS
7   PROSERTHRLEUARGGLULEUGLUARGTYR
8   VALTHRSERCYSLEUARGLYSLYSARGLYS
9   PROGLNALA

Entity 2, entity_2 12 residues - 1431.754 Da.

1   GLUILELYSLEULYSILETHRLYSTHRILE
2   GLNASN

Samples:

sample_1: entity_1 mM; entity_2 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 2 mM; D2O, [U-2H], 100%

sample_2: entity_1 mM; entity_2 mM; sodium phosphate 10 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 2 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D filtered 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D filtered 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift calculation, processing

NMRView v5.04, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - refinement

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

TOPSPIN v2.1, Bruker Biospin - collection

ProcheckNMR, Laskowski and MacArthur - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

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