BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30367

Title: Solution NMR structures of the BRD3 ET domain in complex with a CHD4 peptide   PubMed: 29567837

Deposition date: 2017-10-28 Original release date: 2018-03-14

Authors: Wai, D.; Szyszka, T.; Campbell, A.; Kwong, C.; Wilkinson-White, L.; Silva, A.; Low, J.; Kwan, A.; Gamsjaeger, R.; Lu, B.; Vakoc, C.; Blobel, G.; Mackay, J.

Citation: Wai, Dorothy; Szyszka, Taylor; Campbell, Amy; Kwong, Cherry; Wilkinson-White, Lorna; Silva, Ana; Low, Jason; Kwan, Ann; Gamsjaeger, Roland; Chalmers, James; Patrick, Wayne; Lu, Bin; Vakoc, Christopher; Blobel, Gerd; Mackay, Joel. "The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators"  J. Biol. Chem. 293, 7160-7175 (2018).

Assembly members:
entity_1, polymer, 12 residues, 1273.629 Da.
entity_2, polymer, 93 residues, 10687.956 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: KVAPLKIKLGGF
entity_2: GPLGSASASYDSEEEEEGLP MSYDEKRQLSLDINRLPGEK LGRVVHIIQSREPSLRDSNP DEIEIDFETLKPTTLRELER YVKSCLQKKQRKP

Data typeCount
13C chemical shifts354
15N chemical shifts82
1H chemical shifts603

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 12 residues - 1273.629 Da.

1   LYSVALALAPROLEULYSILELYSLEUGLY
2   GLYPHE

Entity 2, entity_2 93 residues - 10687.956 Da.

1   GLYPROLEUGLYSERALASERALASERTYR
2   ASPSERGLUGLUGLUGLUGLUGLYLEUPRO
3   METSERTYRASPGLULYSARGGLNLEUSER
4   LEUASPILEASNARGLEUPROGLYGLULYS
5   LEUGLYARGVALVALHISILEILEGLNSER
6   ARGGLUPROSERLEUARGASPSERASNPRO
7   ASPGLUILEGLUILEASPPHEGLUTHRLEU
8   LYSPROTHRTHRLEUARGGLULEUGLUARG
9   TYRVALLYSSERCYSLEUGLNLYSLYSGLN
10   ARGLYSPRO

Samples:

sample_1: BRD3, [U-13C; U-15N], 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_2: BRD3, [U-13C; U-15N], 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_3: BRD3 500 uM; CHD4 500 uM; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C (F1)-filtered NOESY aliphaticsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 15N13C (F2,F1)-filtered) 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY v3.1.3, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.5.6, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AvanceIII 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts