+Open data
-Basic information
Entry | Database: PDB / ID: 7ejs | ||||||
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Title | Structure of ERH-2 bound to PICS-1 | ||||||
Components | Enhancer of rudimentary homolog 2,Protein pid-3 | ||||||
Keywords | PEPTIDE BINDING PROTEIN / PICS complex | ||||||
Function / homology | Function and homology information 21U-RNA metabolic process / positive regulation of chromosome segregation / RNA cap binding complex / piRNA processing / embryo development ending in birth or egg hatching / positive regulation of cell division / chromosome segregation / cell division / perinuclear region of cytoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Caenorhabditis elegans (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.387 Å | ||||||
Authors | Wang, X. / Xu, C. | ||||||
Citation | Journal: Nat Commun / Year: 2021 Title: Molecular basis for PICS-mediated piRNA biogenesis and cell division. Authors: Wang, X. / Zeng, C. / Liao, S. / Zhu, Z. / Zhang, J. / Tu, X. / Yao, X. / Feng, X. / Guang, S. / Xu, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7ejs.cif.gz | 100.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7ejs.ent.gz | 75.1 KB | Display | PDB format |
PDBx/mmJSON format | 7ejs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ej/7ejs ftp://data.pdbj.org/pub/pdb/validation_reports/ej/7ejs | HTTPS FTP |
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-Related structure data
Related structure data | 7d1lC 7d2yC 7ejoC 1wz7S S: Starting model for refinement C: citing same article (ref.) |
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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
#1: Protein | Mass: 15942.616 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: erh-2, F35G12.11, pid-3, pics-1, Y23H5A.3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q20057, UniProt: O76616 #2: 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: 2.31 Å3/Da / Density % sol: 46.75 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: 15% v/v 2-propanol, 0.1M sodium citrate tribasic dihydrate pH 5.0, 10% PEG 10000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9792 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 26, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→50 Å / Num. obs: 11991 / % possible obs: 100 % / Redundancy: 11.6 % / CC1/2: 0.996 / Net I/σ(I): 24 |
Reflection shell | Resolution: 2.4→2.44 Å / Num. unique obs: 1679 / CC1/2: 0.83 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1WZ7 Resolution: 2.387→26.264 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 23.58 / 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 max: 149.76 Å2 / Biso mean: 71.0806 Å2 / Biso min: 40.62 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.387→26.264 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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