+Open data
-Basic information
Entry | Database: PDB / ID: 6j6v | ||||||
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Title | Crystal structure of heat shock factor 4-DBD | ||||||
Components | Heat shock factor protein 4 | ||||||
Keywords | TRANSCRIPTION / transcriptional factor | ||||||
Function / homology | Function and homology information : / cell development / lens fiber cell differentiation / visual perception / epithelial cell proliferation / positive regulation of epithelial cell proliferation / positive regulation of cell differentiation / sequence-specific double-stranded DNA binding / protein phosphatase binding / transcription by RNA polymerase II ...: / cell development / lens fiber cell differentiation / visual perception / epithelial cell proliferation / positive regulation of epithelial cell proliferation / positive regulation of cell differentiation / sequence-specific double-stranded DNA binding / protein phosphatase binding / transcription by RNA polymerase II / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.2 Å | ||||||
Authors | Guo, L. / Xiao, Z.Y. / Wang, S. / Liu, W. | ||||||
Citation | Journal: To Be Published Title: Structure of heat shock factor 4-DBD at 1.20 Angstroms resolution. Authors: Guo, L. / Xiao, Z.Y. / Wang, S. / Liu, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6j6v.cif.gz | 59.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6j6v.ent.gz | 42.4 KB | Display | PDB format |
PDBx/mmJSON format | 6j6v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j6/6j6v ftp://data.pdbj.org/pub/pdb/validation_reports/j6/6j6v | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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: 12187.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HSF4 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9ULV5 | ||||
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#2: Chemical | #3: Chemical | #4: 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: 2.5 Å3/Da / Density % sol: 50.82 % |
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Crystal grow | Temperature: 295 K / Method: evaporation / Details: sodium nitrate |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9785 Å |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Oct 25, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9785 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→38.98 Å / Num. obs: 36700 / % possible obs: 99.3 % / Redundancy: 12.3 % / Net I/σ(I): 49.3 |
Reflection shell | Resolution: 1.2→1.22 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.2→38.979 Å / SU ML: 0.07 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 13.23
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.2→38.979 Å
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Refine LS restraints |
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LS refinement shell |
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