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Yorodumi- PDB-5ums: Crystal structure of middle double PH domain of human FACT comple... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5ums | |||||||||
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Title | Crystal structure of middle double PH domain of human FACT complex subunit SSRP1 | |||||||||
Components | FACT complex subunit SSRP1FACT (biology) | |||||||||
Keywords | TRANSCRIPTION / Histone chaperone / Double PH domain / FACT | |||||||||
Function / homology | Function and homology information FACT complex / regulation of chromatin organization / nucleosome disassembly / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / nucleosome binding / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat ...FACT complex / regulation of chromatin organization / nucleosome disassembly / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / nucleosome binding / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / nucleosome assembly / histone binding / Regulation of TP53 Activity through Phosphorylation / DNA replication / DNA repair / nucleolus / DNA binding / RNA binding / nucleoplasm / nucleus Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.569 Å | |||||||||
Authors | Su, D. / Hu, Q. / Thompson, J.R. / Botuyan, M.V. / Mer, G. | |||||||||
Funding support | United States, 2items
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Citation | Journal: To Be Published Title: Crystal structure of middle double PH domain of human FACT complex subunit SSRP1 Authors: Hu, Q. / Su, D. / Thompson, J.R. / Botuyan, M.V. / Mer, G. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ums.cif.gz | 118.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ums.ent.gz | 90.5 KB | Display | PDB format |
PDBx/mmJSON format | 5ums.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/um/5ums ftp://data.pdbj.org/pub/pdb/validation_reports/um/5ums | HTTPS FTP |
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-Related structure data
Related structure data | 2gclS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 30460.014 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SSRP1, FACT80 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q08945 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.16 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 100 mM Bis-Tris, pH 6.5, 28% polyethylene glycol monomethyl ether 2000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 0.9792 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 1, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 1.569→28.16 Å / Num. obs: 35760 / % possible obs: 93.1 % / Redundancy: 2.3 % / Net I/σ(I): 29.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2GCL Resolution: 1.569→28.157 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.42
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Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Bsol: 40.436 Å2 / ksol: 0.323 e/Å3 | |||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.569→28.157 Å
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Refine LS restraints |
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LS refinement shell |
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