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Yorodumi- PDB-2fuu: NMR solution structure of the PHD domain from the human BPTF in c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fuu | ||||||
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Title | NMR solution structure of the PHD domain from the human BPTF in complex with H3(1-15)K4me3 peptide | ||||||
Components |
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Keywords | PROTEIN BINDING / BPTF / NURF / PHD DOMAIN / HISTONE RECOGNITION / H3K4ME3 | ||||||
Function / homology | Function and homology information NURF complex / endoderm development / anterior/posterior pattern specification / ATPase complex / embryonic placenta development / methylated histone binding / cellular response to nerve growth factor stimulus / brain development / structural constituent of chromatin / nucleosome ...NURF complex / endoderm development / anterior/posterior pattern specification / ATPase complex / embryonic placenta development / methylated histone binding / cellular response to nerve growth factor stimulus / brain development / structural constituent of chromatin / nucleosome / cell body / sequence-specific DNA binding / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein heterodimerization activity / dendrite / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / extracellular exosome / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / The structure was solved using a torsion angle simulated annealing protocol | ||||||
Authors | Ilin, S. / Patel, D.J. | ||||||
Citation | Journal: Nature / Year: 2006 Title: Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Authors: Li, H. / Ilin, S. / Wang, W. / Duncan, E.M. / Wysocka, J. / Allis, C.D. / Patel, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fuu.cif.gz | 472.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fuu.ent.gz | 403.1 KB | Display | PDB format |
PDBx/mmJSON format | 2fuu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fu/2fuu ftp://data.pdbj.org/pub/pdb/validation_reports/fu/2fuu | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 7050.871 Da / Num. of mol.: 1 / Fragment: PHD FINGER DOMAIN (RESIDUES 2583-2639) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGex6p / Production host: Escherichia coli (E. coli) / Strain (production host): Rosseta 2 / References: GenBank: 31322942, UniProt: Q12830*PLUS |
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#2: Protein/peptide | Mass: 1607.877 Da / Num. of mol.: 1 / Fragment: H3(1-15)K4me3 / Mutation: K4(M3L) / Source method: obtained synthetically Details: Synthetic. The sequence ARTKQTARKSTGGKA occurs naturally in humans on Histone 3 References: UniProt: P61836, UniProt: Q7M3Z9*PLUS |
#3: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using various triple-resonance NMR experiments plus filter edit experiments to determine the structure of the peptide. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50 mM KCl / pH: 7.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: The structure was solved using a torsion angle simulated annealing protocol Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 85 / Conformers submitted total number: 20 |