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Open data
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Basic information
| Entry | Database: PDB / ID: 5oen | ||||||
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| Title | Crystal Structure of STAT2 in complex with IRF9 | ||||||
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Keywords | TRANSCRIPTION / STAT2 / IRF9 | ||||||
| Function / homology | Function and homology informationInterferon alpha/beta signaling / cytokine-mediated signaling pathway / transcription cis-regulatory region binding / DNA-binding transcription factor activity / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / DNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.919 Å | ||||||
Authors | Rengachari, S. / Panne, D. | ||||||
Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018Title: Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function. Authors: Rengachari, S. / Groiss, S. / Devos, J.M. / Caron, E. / Grandvaux, N. / Panne, D. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5oen.cif.gz | 136.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5oen.ent.gz | 109.2 KB | Display | PDB format |
| PDBx/mmJSON format | 5oen.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5oen_validation.pdf.gz | 431.1 KB | Display | wwPDB validaton report |
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| Full document | 5oen_full_validation.pdf.gz | 435.3 KB | Display | |
| Data in XML | 5oen_validation.xml.gz | 13.3 KB | Display | |
| Data in CIF | 5oen_validation.cif.gz | 17.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oe/5oen ftp://data.pdbj.org/pub/pdb/validation_reports/oe/5oen | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5oemC ![]() 1bf5S S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 19100.721 Da / Num. of mol.: 1 / Fragment: UNP residues 206-376 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q61179 |
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| #2: Protein | Mass: 20238.412 Da / Num. of mol.: 1 / Fragment: UNP residues 141-315 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q3UDU1 |
| #3: 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: 2.46 Å3/Da / Density % sol: 49.92 % |
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| Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, hanging drop / Details: 0.2M Potassium formate and 20% PEG3350 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.972 Å |
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 9, 2017 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.972 Å / Relative weight: 1 |
| Reflection | Resolution: 2.919→39.389 Å / Num. obs: 7970 / % possible obs: 96 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.194 / Net I/σ(I): 5.9 |
| Reflection shell | Resolution: 2.919→2.93 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.898 / % possible all: 98.7 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1BF5 Resolution: 2.919→32.12 Å / SU ML: 0.46 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 32.95 / 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: 42.46 Å2 | ||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.919→32.12 Å
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| LS refinement shell |
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