BMRB Entry 50801

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignment for Brd3-BD1
Deposition date:
2021-03-04
Original release date:
2022-12-16
Authors:
Zerio, Christopher; Clarkson, Michael; Chapman, Eli
Citation:

Citation: Zerio, Christopher; Sivinski, Jared; Wijeratne, E; Xu, Ya-Ming; Ngo, Duc; Ambrose, Andrew; Villa-Celis, Luis; Ghadirian, Niloofar; Clarkson, Michael; Zhang, Donna; Horton, Nancy; Gunatilaka, A; Fromme, Raimund; Chapman, Eli. "Physachenolide C is a Potent, Selective BET Inhibitor"  J. Med. Chem. 66, 913-933 (2023).
PubMed: 36577036

Assembly members:

Assembly members:
entity_1, polymer, 122 residues, 14409.65 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: PIPET

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts110
1H chemical shifts110

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Brd3-BD11

Entities:

Entity 1, Brd3-BD1 122 residues - 14409.65 Da.

The first G is a scar from cloning. In the real protein, the numbering would start with P24. In the NMRSTAR file I submitted, it starts as P1.

1   GLYPROGLUVALSERASNPROSERLYSPRO
2   GLYARGLYSTHRASNGLNLEUGLNTYRMET
3   GLNASNVALVALVALLYSTHRLEUTRPLYS
4   HISGLNPHEALATRPPROPHETYRGLNPRO
5   VALASPALAILELYSLEUASNLEUPROASP
6   TYRHISLYSILEILELYSASNPROMETASP
7   METGLYTHRILELYSLYSARGLEUGLUASN
8   ASNTYRTYRTRPSERALASERGLUCYSMET
9   GLNASPPHEASNTHRMETPHETHRASNCYS
10   TYRILETYRASNLYSPROTHRASPASPILE
11   VALLEUMETALAGLNALALEUGLULYSILE
12   PHELEUGLNLYSVALALAGLNMETPROGLN
13   GLUGLU

Samples:

sample_1: Bromodomain-containing Protein 3, Bromodomain 1, [U-99% 13C; U-99% 15N], 350 uM; Tris 20 mM; NaCl 100 mM; DTT 1 mM

sample_conditions_1: pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY v1.414 - chemical shift assignment, peak picking

NMR spectrometers:

  • 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