+Open data
-Basic information
Entry | Database: PDB / ID: 4wnn | ||||||||||||||||||||||||
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Title | SPT16-H2A-H2B FACT HISTONE Complex | ||||||||||||||||||||||||
Components |
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Keywords | DNA BINDING PROTEIN / FACT / SPT16 / Histone / POB3 / H2A / H2B | ||||||||||||||||||||||||
Function / homology | Function and homology information Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / FACT complex / Condensation of Prophase Chromosomes / regulation of chromatin organization / nucleosome organization / replication fork protection complex / RMTs methylate histone arginines / postreplication repair / TP53 Regulates Transcription of DNA Repair Genes ...Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / FACT complex / Condensation of Prophase Chromosomes / regulation of chromatin organization / nucleosome organization / replication fork protection complex / RMTs methylate histone arginines / postreplication repair / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Pre-transcription Events / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / transcription elongation by RNA polymerase II / DNA-templated DNA replication / nucleosome assembly / structural constituent of chromatin / nucleosome / chromatin organization / protein heterodimerization activity / DNA repair / chromatin / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / DNA binding / nucleus Similarity search - Function | ||||||||||||||||||||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||||||||||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||||||||||||||||||||
Authors | Kemble, D.J. / Hill, C.P. / Whitby, F.G. / Formosa, T. / McCullough, L.L. | ||||||||||||||||||||||||
Funding support | United States, 7items
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Citation | Journal: Mol.Cell / Year: 2015 Title: FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs. Authors: Kemble, D.J. / McCullough, L.L. / Whitby, F.G. / Formosa, T. / Hill, C.P. | ||||||||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4wnn.cif.gz | 313.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4wnn.ent.gz | 256.9 KB | Display | PDB format |
PDBx/mmJSON format | 4wnn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wn/4wnn ftp://data.pdbj.org/pub/pdb/validation_reports/wn/4wnn | HTTPS FTP |
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-Related structure data
Related structure data | 1id3S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 14013.177 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Strain: ATCC 204508 / S288c / Gene: HTA1, H2A1, SPT11, YDR225W, YD9934.10 / Production host: Escherichia coli (E. coli) / References: UniProt: P04911 #2: Protein | Mass: 11376.043 Da / Num. of mol.: 4 / Fragment: UNP residues 31-131 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Strain: ATCC 204508 / S288c / Gene: HTB1, H2B1, SPT12, YDR224C, YD9934.09C / Production host: Escherichia coli (E. coli) / References: UniProt: P02293 #3: Protein/peptide | | Mass: 2262.250 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Production host: Escherichia coli (E. coli) / References: UniProt: P32558*PLUS #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40.02 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7 Details: Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: single wavelength |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 1.12709 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 6, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.12709 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→40 Å / Num. obs: 77661 / % possible obs: 98.7 % / Redundancy: 3.7 % / Biso Wilson estimate: 34.58 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 20.2 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.928 / % possible all: 95.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1ID3 Resolution: 1.8→21.22 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 24.42 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.02 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→21.22 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 28.6745 Å / Origin y: -6.7327 Å / Origin z: -32.1876 Å
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Refinement TLS group | Selection details: ALL |