+Open data
-Basic information
Entry | Database: PDB / ID: 7jq8 | ||||||||||||
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Title | Solution NMR structure of human Brd3 ET domain | ||||||||||||
Components |
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Keywords | SIGNALING PROTEIN / BET proteins / BRD3 / extra-terminal domain / MLV-IN TP | ||||||||||||
Function / homology | Function and homology information retroviral 3' processing activity / host cell late endosome membrane / DNA catabolic process / lncRNA binding / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / virion assembly / endodermal cell differentiation / protein localization to chromatin / lysine-acetylated histone binding ...retroviral 3' processing activity / host cell late endosome membrane / DNA catabolic process / lncRNA binding / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / virion assembly / endodermal cell differentiation / protein localization to chromatin / lysine-acetylated histone binding / molecular condensate scaffold activity / protein-DNA complex / host multivesicular body / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / symbiont-mediated suppression of host gene expression / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / chromatin organization / viral nucleocapsid / aspartic-type endopeptidase activity / DNA recombination / structural constituent of virion / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase activity / symbiont entry into host cell / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / host cell plasma membrane / positive regulation of transcription by RNA polymerase II / proteolysis / DNA binding / RNA binding / zinc ion binding / membrane / nucleus Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) Moloney murine leukemia virus | ||||||||||||
Method | SOLUTION NMR / simulated annealing | ||||||||||||
Authors | Aiyer, S. / Swapna, G.V.T. / Roth, J.M. / Montelione, G.T. | ||||||||||||
Funding support | United States, 3items
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Citation | Journal: Structure / Year: 2021 Title: A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins. Authors: Aiyer, S. / Swapna, G.V.T. / Ma, L.C. / Liu, G. / Hao, J. / Chalmers, G. / Jacobs, B.C. / Montelione, G.T. / Roth, M.J. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7jq8.cif.gz | 871.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7jq8.ent.gz | 742.7 KB | Display | PDB format |
PDBx/mmJSON format | 7jq8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jq/7jq8 ftp://data.pdbj.org/pub/pdb/validation_reports/jq/7jq8 | HTTPS FTP |
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-Related structure data
Related structure data | 7jmyC 7jynC 7jyzC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11264.543 Da / Num. of mol.: 1 / Fragment: NET domain, residues 554-640 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BRD3, KIAA0043, RING3L / Plasmid: pET15_NESG / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q15059 |
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#2: Protein/peptide | Mass: 2812.281 Da / Num. of mol.: 1 / Fragment: C-terminal Tail, residues 1716-1738 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Moloney murine leukemia virus (isolate Shinnick) Strain: isolate Shinnick / Gene: gag-pol / Plasmid: pET15_NESG / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P03355, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases, Hydrolases; Acting on ester bonds |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Details: 20 mM sodium phosphate, 100 mM NaCl and 2 mM 2-mercaptoethanol / Ionic strength: 100mM NaCl mM / Ionic strength err: 0.2 / pH: 7 / PH err: 0.05 / Pressure: 1 atm / Pressure err: 0.05 / Temperature: 298 K / Temperature err: 0.1
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-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz / Details: Equipped with 5mm TXI cryoprobe |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |