BMRB Entry 30782

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30782
MolProbity Validation Chart

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Title:
A common binding motif in the ET domain of BRD3 participates in polymorphic structural interfaces with host and viral proteins
Deposition date:
2020-08-03
Original release date:
2021-03-01
Authors:
Aiyer, S.; Swapna, G.; Roth, M.; Montelione, G.
Citation:

Citation: Aiyer, S.; Swapna, G.; Ma, L.; Liu, G.; Hao, J.; Chalmers, G.; Jacobs, B.; Montelione, G.; Roth, M.. "A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins"  Structure 29, 886-898 (2021).
PubMed: 33592170

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 11264.543 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 BL21(DE3)   Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHSHMGKQASASYDSE EEEEGLPMSYDEKRQLSLDI NRLPGEKLGRVVHIIQSREP SLRDSNPDEIEIDFETLKPT TLRELERYVKSCLQKK

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts87
1H chemical shifts601

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 96 residues - 11264.543 Da.

1   HISHISHISHISHISHISSERHISMETGLY
2   LYSGLNALASERALASERTYRASPSERGLU
3   GLUGLUGLUGLUGLYLEUPROMETSERTYR
4   ASPGLULYSARGGLNLEUSERLEUASPILE
5   ASNARGLEUPROGLYGLULYSLEUGLYARG
6   VALVALHISILEILEGLNSERARGGLUPRO
7   SERLEUARGASPSERASNPROASPGLUILE
8   GLUILEASPPHEGLUTHRLEULYSPROTHR
9   THRLEUARGGLULEUGLUARGTYRVALLYS
10   SERCYSLEUGLNLYSLYS

Samples:

sample_1: Brd3 ET Domain, [U-15N], 0.5 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; Na3PO4 20 ± 0.02 mM; 2-mercapto ethanol 2 ± 0.02 mM

sample_2: Brd3 ET Domain, [U-13C; U-15N], 0.5 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; Na3PO4 20 ± 0.02 mM; beta-mercaptoethanol 2 ± 0.02 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
1D T1sample_1isotropicsample_conditions_1
1D T2sample_1isotropicsample_conditions_1
2D HNOEsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D 1H-13C,15N simNOESYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2

Software:

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

AutoAssign v2.4, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

ASDP v1.2, Huang et al - geometry optimization

Sparky, Goddard - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin v2.3b, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 800 MHz

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