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
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NMR-STAR v3 text file.
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Title: Solution NMR structure and dynamics of human Brd3 ET in complex with MLV IN CTD PubMed: 33592170
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: 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).
Assembly members:
entity_1, polymer, 89 residues, 10131.592 Da.
entity_2, polymer, 96 residues, 11264.543 Da.
Natural source: Common Name: MoMLV Taxonomy ID: 11801 Superkingdom: Viruses Kingdom: not available Genus/species: Gammaretrovirus MoMLV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: HHHHHHSHMVGDTVWVRRHQ
TKNLEPRWKGPYTVLLTTPT
ALKVDGIAAWIHAAHVKAAD
PGGGPSSRLTWRVQRSQNPL
KIRLTREAP
entity_2: HHHHHHSHMGKQASASYDSE
EEEEGLPMSYDEKRQLSLDI
NRLPGEKLGRVVHIIQSREP
SLRDSNPDEIEIDFETLKPT
TLRELERYVKSCLQKK
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 566 |
| 15N chemical shifts | 164 |
| 1H chemical shifts | 1159 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 2 |
Entities:
Entity 1, unit_1 89 residues - 10131.592 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | MET | VAL | ||||
| 2 | GLY | ASP | THR | VAL | TRP | VAL | ARG | ARG | HIS | GLN | ||||
| 3 | THR | LYS | ASN | LEU | GLU | PRO | ARG | TRP | LYS | GLY | ||||
| 4 | PRO | TYR | THR | VAL | LEU | LEU | THR | THR | PRO | THR | ||||
| 5 | ALA | LEU | LYS | VAL | ASP | GLY | ILE | ALA | ALA | TRP | ||||
| 6 | ILE | HIS | ALA | ALA | HIS | VAL | LYS | ALA | ALA | ASP | ||||
| 7 | PRO | GLY | GLY | GLY | PRO | SER | SER | ARG | LEU | THR | ||||
| 8 | TRP | ARG | VAL | GLN | ARG | SER | GLN | ASN | PRO | LEU | ||||
| 9 | LYS | ILE | ARG | LEU | THR | ARG | GLU | ALA | PRO |
Entity 2, unit_2 96 residues - 11264.543 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | MET | GLY | ||||
| 2 | LYS | GLN | ALA | SER | ALA | SER | TYR | ASP | SER | GLU | ||||
| 3 | GLU | GLU | GLU | GLU | GLY | LEU | PRO | MET | SER | TYR | ||||
| 4 | ASP | GLU | LYS | ARG | GLN | LEU | SER | LEU | ASP | ILE | ||||
| 5 | ASN | ARG | LEU | PRO | GLY | GLU | LYS | LEU | GLY | ARG | ||||
| 6 | VAL | VAL | HIS | ILE | ILE | GLN | SER | ARG | GLU | PRO | ||||
| 7 | SER | LEU | ARG | ASP | SER | ASN | PRO | ASP | GLU | ILE | ||||
| 8 | GLU | ILE | ASP | PHE | GLU | THR | LEU | LYS | PRO | THR | ||||
| 9 | THR | LEU | ARG | GLU | LEU | GLU | ARG | TYR | VAL | LYS | ||||
| 10 | SER | CYS | LEU | GLN | LYS | LYS |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N-T1-relaxation | sample_2 | isotropic | sample_conditions_2 |
| 3D 13C-NOESY-aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-15N_simNOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N-T2-relaxation | sample_2 | isotropic | sample_conditions_2 |
| 2D HNOE | sample_2 | isotropic | sample_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 shifts
SPARKY: Backbone
or all simulated shifts