+Open data
-Basic information
Entry | Database: PDB / ID: 5uzg | ||||||
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Title | Crystal structure of Glorund qRRM1 domain | ||||||
Components | AT27789p | ||||||
Keywords | RNA BINDING PROTEIN / quasi-RNA recognition motif / qRRM | ||||||
Function / homology | Function and homology information maternal specification of dorsal/ventral axis, oocyte, germ-line encoded / intracellular mRNA localization involved in pattern specification process / Processing of Capped Intron-Containing Pre-mRNA / mRNA Splicing - Major Pathway / pole plasm oskar mRNA localization / regulation of RNA splicing / chromosome organization / wound healing / regulation of translation / ribonucleoprotein complex ...maternal specification of dorsal/ventral axis, oocyte, germ-line encoded / intracellular mRNA localization involved in pattern specification process / Processing of Capped Intron-Containing Pre-mRNA / mRNA Splicing - Major Pathway / pole plasm oskar mRNA localization / regulation of RNA splicing / chromosome organization / wound healing / regulation of translation / ribonucleoprotein complex / mRNA binding / protein-containing complex / RNA binding / nucleoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.541 Å | ||||||
Authors | Teramoto, T. / Hall, T.M.T. | ||||||
Citation | Journal: Cell Rep / Year: 2017 Title: The Drosophila hnRNP F/H Homolog Glorund Uses Two Distinct RNA-Binding Modes to Diversify Target Recognition. Authors: Tamayo, J.V. / Teramoto, T. / Chatterjee, S. / Hall, T.M. / Gavis, E.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5uzg.cif.gz | 55.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5uzg.ent.gz | 38.1 KB | Display | PDB format |
PDBx/mmJSON format | 5uzg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/5uzg ftp://data.pdbj.org/pub/pdb/validation_reports/uz/5uzg | HTTPS FTP |
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-Related structure data
Related structure data | 5uzmC 5uznC 2kfyS C: citing same article (ref.) S: Starting model for refinement |
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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: 11130.540 Da / Num. of mol.: 2 / Fragment: qRRM1 domain residues 45-141 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: glo, CG6946, Dmel_CG6946 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9VGH5 #2: Chemical | ChemComp-GOL / #3: Chemical | #4: 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: 2.33 Å3/Da / Density % sol: 47.31 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: 0.2 M ammonium sulfate, 0.1 M Na acetate pH 4.6, 30% w/v PEGMME 2000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54 Å |
Detector | Type: RIGAKU SATURN 92 / Detector: CCD / Date: Aug 28, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.54→50 Å / Num. obs: 26983 / % possible obs: 90.9 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.065 / Net I/σ(I): 20.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2KFY Resolution: 1.541→23.984 Å / SU ML: 0.12 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 20
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.541→23.984 Å
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Refine LS restraints |
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LS refinement shell |
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