+Open data
-Basic information
Entry | Database: PDB / ID: 6sqt | ||||||
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Title | Structure of the U1A variant A1-98 Y31H/Q36R/F56W triple mutant | ||||||
Components | U1 small nuclear ribonucleoprotein A | ||||||
Keywords | RNA BINDING PROTEIN / U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A / U1A / RNA hairpin / co-crystallization | ||||||
Function / homology | Function and homology information U1 snRNP binding / U1 snRNP / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / DNA binding / RNA binding / nucleoplasm ...U1 snRNP binding / U1 snRNP / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.84 Å | ||||||
Authors | Rosenbach, H. / Span, I. | ||||||
Citation | Journal: J.Struct.Biol. / Year: 2020 Title: Expanding crystallization tools for nucleic acid complexes using U1A protein variants. Authors: Rosenbach, H. / Victor, J. / Borggrafe, J. / Biehl, R. / Steger, G. / Etzkorn, M. / Span, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6sqt.cif.gz | 117 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6sqt.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6sqt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sq/6sqt ftp://data.pdbj.org/pub/pdb/validation_reports/sq/6sqt | 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 11379.352 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SNRPA / Production host: Escherichia coli (E. coli) / References: UniProt: P09012 #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: 2.95 Å3/Da / Density % sol: 58.33 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 2.2 M ammonium sulfate, 0.2 M tri-potassium citrate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.0332 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 17, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 1.84→38.89 Å / Num. obs: 29093 / % possible obs: 82.1 % / Redundancy: 13.9 % / CC1/2: 1 / Rmerge(I) obs: 0.054 / Rrim(I) all: 0.056 / Net I/σ(I): 25.4 |
Reflection shell | Resolution: 1.84→1.87 Å / Rmerge(I) obs: 0.871 / Mean I/σ(I) obs: 0.7 / Num. unique obs: 238 / CC1/2: 0.276 / Rrim(I) all: 1.189 / % possible all: 13.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.84→38.89 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.934 / SU B: 4.455 / SU ML: 0.123 / Cross valid method: FREE R-VALUE / ESU R: 0.15 / ESU R Free: 0.14 Details: Hydrogens have been added in their riding positions
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.399 Å2
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Refinement step | Cycle: LAST / Resolution: 1.84→38.89 Å
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Refine LS restraints |
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LS refinement shell |
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