BMRB Entry 30790

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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/BMR30790
MolProbity Validation Chart

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Title:
Solution NMR structure of human Brd3 ET complexed with NSD3(148-184) peptide
Deposition date:
2020-08-31
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.
entity_2, polymer, 39 residues, 4329.835 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)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHSHMGKQASASYDSE EEEEGLPMSYDEKRQLSLDI NRLPGEKLGRVVHIIQSREP SLRDSNPDEIEIDFETLKPT TLRELERYVKSCLQKK
entity_2: EFTGSPEIKLKITKTIQNGR ELFESSLCGDLLNEVQASE

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts123
1H chemical shifts837

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

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

Entity 2, unit_2 39 residues - 4329.835 Da.

1   GLUPHETHRGLYSERPROGLUILELYSLEU
2   LYSILETHRLYSTHRILEGLNASNGLYARG
3   GLULEUPHEGLUSERSERLEUCYSGLYASP
4   LEULEUASNGLUVALGLNALASERGLU

Samples:

sample_1: NSD3(148-184), [U-100% 13C; U-100% 15N], 0.5 ± 0.02 mM; sodium chloride 100 mM; sodium phosphate 20 mM; 2-mercaptoethanol 2 mM

sample_2: NSD3(148-184) 0.25 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM; Brd3ET, U-100% 13C; U-100% 15, 0.25 ± 0.02 mM

sample_3: NSD3(148-184), [U-100% 13C; U-100% 15N], 0.25 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM; Brd3ET, [U-100% 13C; U-100% 15N], 0.2 ± 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

sample_conditions_3: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D HNOEsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 13C_15N_simNOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_3isotropicsample_conditions_3
3D HBHA(CO)NHsample_3isotropicsample_conditions_3
3D CBCA(CO)NHsample_3isotropicsample_conditions_3
3D HNCACBsample_3isotropicsample_conditions_3
3D HNCAsample_3isotropicsample_conditions_3
3D HNCOsample_3isotropicsample_conditions_3
2D HNOEsample_3isotropicsample_conditions_3
2D 1H-13C HSQCsample_3isotropicsample_conditions_3
2D 1H-15N HSQCsample_3isotropicsample_conditions_3
3D X-filtered_NOESYsample_2isotropicsample_conditions_2
3D 13C_edited_NOESY_aromaticsample_2isotropicsample_conditions_2
3D 13C_15N_simNOESYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
2D HNOEsample_2isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
3D 13C_15N_simNOESYsample_3isotropicsample_conditions_3
3D 13C_edited_NOESY_aromaticsample_3isotropicsample_conditions_3

Software:

TopSpin v2.3b, 3.2, Bruker Biospin - collection

NMRPipe v10.8, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin v2.3b, Bruker Biospin - processing

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

PINE Server, PINE - chemical shift assignment

Sparky, Goddard - data analysis, peak picking

ASDP v2.3, Huang et al. - geometry optimization

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 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