+Open data
-Basic information
Entry | Database: PDB / ID: 2m16 | ||||||
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Title | P75/LEDGF PWWP Domain | ||||||
Components | PC4 and SFRS1-interacting protein | ||||||
Keywords | TRANSCRIPTION / protein / PWWP domain / DNA binding | ||||||
Function / homology | Function and homology information supercoiled DNA binding / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Formation of WDR5-containing histone-modifying complexes / 2-LTR circle formation / Vpr-mediated nuclear import of PICs / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / mRNA 5'-splice site recognition / heterochromatin ...supercoiled DNA binding / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Formation of WDR5-containing histone-modifying complexes / 2-LTR circle formation / Vpr-mediated nuclear import of PICs / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / mRNA 5'-splice site recognition / heterochromatin / nuclear periphery / euchromatin / response to heat / DNA-binding transcription factor binding / response to oxidative stress / transcription coactivator activity / chromatin remodeling / chromatin binding / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Crowe, B.L. / Foster, M.P. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2013 Title: Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes. Authors: Eidahl, J.O. / Crowe, B.L. / North, J.A. / McKee, C.J. / Shkriabai, N. / Feng, L. / Plumb, M. / Graham, R.L. / Gorelick, R.J. / Hess, S. / Poirier, M.G. / Foster, M.P. / Kvaratskhelia, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m16.cif.gz | 672.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m16.ent.gz | 576.5 KB | Display | PDB format |
PDBx/mmJSON format | 2m16.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m1/2m16 ftp://data.pdbj.org/pub/pdb/validation_reports/m1/2m16 | HTTPS FTP |
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-Related structure data
Related structure data | 2m15 |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11031.594 Da / Num. of mol.: 1 / Fragment: unp residues 1-93 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DFS70, LEDGF, PSIP1, PSIP2 / Plasmid: pFT-1-LEDGF / Production host: Escherichia coli (E. coli) / References: UniProt: O75475 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.35-0.45 mM [U-99% 13C; U-99% 15N] entity, 50 mM HEPES, 150 mM sodium chloride, 2 mM beta-mercaptoethanol, 0.66 mM DSS, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.35 / pH: 7.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1439 / NOE intraresidue total count: 302 / NOE long range total count: 471 / NOE medium range total count: 245 / NOE sequential total count: 421 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 150 / Conformers submitted total number: 20 / Maximum torsion angle constraint violation: 10.9 ° / Maximum upper distance constraint violation: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.01 Å |