BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30444

Title: Solution structure of the Extraterminal (ET) Domain of BRD2

Deposition date: 2018-03-26 Original release date: 2019-03-01

Authors: Houliston, S.; Lemak, A.; Picaud, S.; Filippakopoulos, P.; Arrowsmith, C.

Citation: Houliston, S.; Lemak, A.; Picaud, S.; Filippakopoulos, P.; Arrowsmith, C.. "Solution structure of the Extraterminal (ET) Domain of BRD2"  . ., .-..

Assembly members:
entity_1, polymer, 132 residues, 15275.450 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: SMKTAPPALPTGYDSEEEEE SRPMSYDEKRQLSLDINKLP GEKLGRVVHIIQAREPSLRD SNPEEIEIDFETLKPSTLRE LERYVLSCLRKKPRKPYTIK KPVGKTKEELALEKKRELEK RLQDVSGQLNST

Data sets:
Data typeCount
13C chemical shifts528
15N chemical shifts116
1H chemical shifts864

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 132 residues - 15275.450 Da.

1   SERMETLYSTHRALAPROPROALALEUPRO
2   THRGLYTYRASPSERGLUGLUGLUGLUGLU
3   SERARGPROMETSERTYRASPGLULYSARG
4   GLNLEUSERLEUASPILEASNLYSLEUPRO
5   GLYGLULYSLEUGLYARGVALVALHISILE
6   ILEGLNALAARGGLUPROSERLEUARGASP
7   SERASNPROGLUGLUILEGLUILEASPPHE
8   GLUTHRLEULYSPROSERTHRLEUARGGLU
9   LEUGLUARGTYRVALLEUSERCYSLEUARG
10   LYSLYSPROARGLYSPROTYRTHRILELYS
11   LYSPROVALGLYLYSTHRLYSGLUGLULEU
12   ALALEUGLULYSLYSARGGLULEUGLULYS
13   ARGLEUGLNASPVALSERGLYGLNLEUASN
14   SERTHR

Samples:

sample_1: BRD2-ET, [U-13C; U-15N], 250 uM; NaCl 500 mM

sample_conditions_1: ionic strength: 500 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker AvanceIII 600 MHz

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