BMRB Entry 30791

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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/BMR30791
MolProbity Validation Chart

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Title:
Solution NMR structure and dynamics of human Brd3 ET in complex with MLV IN CTD
Deposition date:
2020-09-01
Original release date:
2021-03-01
Authors:
Aiyer, S.; Liu, G.; Swapna, G.; Hao, J.; Ma, L.; 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, 89 residues, 10131.592 Da.
entity_2, polymer, 96 residues, 11264.543 Da.

Natural source:

Natural source:   Common Name: MoMLV   Taxonomy ID: 11801   Superkingdom: Viruses   Kingdom: not available   Genus/species: Gammaretrovirus MoMLV

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHSHMVGDTVWVRRHQ TKNLEPRWKGPYTVLLTTPT ALKVDGIAAWIHAAHVKAAD PGGGPSSRLTWRVQRSQNPL KIRLTREAP
entity_2: HHHHHHSHMGKQASASYDSE EEEEGLPMSYDEKRQLSLDI NRLPGEKLGRVVHIIQSREP SLRDSNPDEIEIDFETLKPT TLRELERYVKSCLQKK

Data typeCount
13C chemical shifts566
15N chemical shifts164
1H chemical shifts1159

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 89 residues - 10131.592 Da.

1   HISHISHISHISHISHISSERHISMETVAL
2   GLYASPTHRVALTRPVALARGARGHISGLN
3   THRLYSASNLEUGLUPROARGTRPLYSGLY
4   PROTYRTHRVALLEULEUTHRTHRPROTHR
5   ALALEULYSVALASPGLYILEALAALATRP
6   ILEHISALAALAHISVALLYSALAALAASP
7   PROGLYGLYGLYPROSERSERARGLEUTHR
8   TRPARGVALGLNARGSERGLNASNPROLEU
9   LYSILEARGLEUTHRARGGLUALAPRO

Entity 2, unit_2 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, [U-100% 13C; U-100% 15N], 0.25 ± 0.02 mM; MLV-IN-CTD, [U-100% 13C; U-100% 15N], 0.25 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; 2-mercaptoethanol 2 ± 0.02 mM

sample_2: Brd3 ET, [U-15N], 0.25 ± 0.02 mM; MLV-IN-CTD, [U-15N], 0.25 ± 0.02 mM; sodium phosphate 20 ± 0.02 mM; sodium chloride 100 ± 0.02 mM; 2-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: 7.2; 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 1H-15N HSQC-TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 15N-T1-relaxationsample_2isotropicsample_conditions_2
3D 13C-NOESY-aromaticsample_1isotropicsample_conditions_1
3D 13C-15N_simNOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 15N-T2-relaxationsample_2isotropicsample_conditions_2
2D HNOEsample_2isotropicsample_conditions_2

Software:

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

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

Sparky, Goddard - data analysis, peak picking

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

I-PINE, Lee, Bahrami, Dashti, Eghbalnia, Tonelli, Westler and Markley - chemical shift assignment

ASDP v2.3, Huang, Y. et al. - geometry optimization, structure calculation

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