+Open data
-Basic information
Entry | Database: PDB / ID: 4rvq | ||||||
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Title | PWI-like domain of Chaetomium thermophilum Brr2 | ||||||
Components | Pre-mRNA splicing helicase-like protein | ||||||
Keywords | PROTEIN BINDING / PWI domain / protein-protein interaction / protein-RNA interaction / pre-mRNA splicing | ||||||
Function / homology | Function and homology information helicase activity / mRNA processing / nucleic acid binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | Chaetomium thermophilum (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.135 Å | ||||||
Authors | Absmeier, E. / Rosenberger, L. / Santos, K.F. / Becke, C. / Wahl, M.C. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2015 Title: A noncanonical PWI domain in the N-terminal helicase-associated region of the spliceosomal Brr2 protein. Authors: Absmeier, E. / Rosenberger, L. / Apelt, L. / Becke, C. / Santos, K.F. / Stelzl, U. / Wahl, M.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rvq.cif.gz | 105.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rvq.ent.gz | 84.7 KB | Display | PDB format |
PDBx/mmJSON format | 4rvq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rv/4rvq ftp://data.pdbj.org/pub/pdb/validation_reports/rv/4rvq | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 16371.359 Da / Num. of mol.: 1 / Fragment: PWI-like domain (UNP residues 287-422) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chaetomium thermophilum (fungus) / Gene: Brr2 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta2 / References: UniProt: G0S0B9 | ||||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal |
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Crystal grow |
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.135→42.79 Å / Num. all: 54190 / Num. obs: 54190 / % possible obs: 100 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 3.5 % / Net I/σ(I): 13 | ||||||||||||||||||
Reflection shell | Resolution: 1.14→1.2 Å / Redundancy: 3.4 % / Mean I/σ(I) obs: 2.9 / % possible all: 92.8 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.135→26.764 Å / SU ML: 0.08 / σ(F): 1.99 / Phase error: 14.91 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.135→26.764 Å
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Refine LS restraints |
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LS refinement shell |
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