+Open data
-Basic information
Entry | Database: PDB / ID: 4rza | ||||||
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Title | Pre-mRNA-splicing factor 38A AS 1-205 | ||||||
Components | Pre-mRNA-splicing factor 38A | ||||||
Keywords | RNA BINDING PROTEIN / RNA-splicing | ||||||
Function / homology | Function and homology information U2-type precatalytic spliceosome / precatalytic spliceosome / mRNA Splicing - Major Pathway / mRNA splicing, via spliceosome / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Schuetze, T. / Ulrich, A. / Wahl, M.C. | ||||||
Citation | Journal: To be Published Title: The N-terminal domain of the unusual SR protein hPrp38 is an interaction hub in the spliceosome Authors: Schuetze, T. / Apelt, L. / Ulrich, A. / Weber, G. / Bartlick, N. / 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 | 4rza.cif.gz | 88.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rza.ent.gz | 68 KB | Display | PDB format |
PDBx/mmJSON format | 4rza.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rz/4rza ftp://data.pdbj.org/pub/pdb/validation_reports/rz/4rza | HTTPS FTP |
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-Related 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: 24216.627 Da / Num. of mol.: 1 / Fragment: UNP residues 1-205 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PRPF38A / Plasmid: pETM11 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta 2 (DE3) / References: UniProt: Q8NAV1 |
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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: 1.8 Å3/Da / Density % sol: 31.62 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 5 Details: 0.1 M MES pH 5.0, 16% PEG 3350, 0.2 M (NH4)2SO4, and 5% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.3 / Wavelength: 0.895 Å |
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Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Oct 31, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.895 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→44.98 Å / Num. all: 14302 / Num. obs: 14297 |
-Processing
Software | Name: PHENIX / Version: (phenix.refine: 1.9_1692) / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→44.98 Å / SU ML: 0.18 / σ(F): 1.36 / Phase error: 20.52 / 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: 1.9→44.98 Å
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Refine LS restraints |
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LS refinement shell |
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