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- PDB-6sqq: Structure of the U1A variant A1-98 Y31H/Q36R/F56W triple mutant i... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6sqq | ||||||
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Title | Structure of the U1A variant A1-98 Y31H/Q36R/F56W triple mutant in complex with RNA obtained by soaking | ||||||
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![]() | RNA BINDING PROTEIN / U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A / U1A / RNA hairpin / soaking | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rosenbach, H. / Span, I. | ||||||
![]() | ![]() 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. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 164.8 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 467.1 KB | Display | ![]() |
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Full document | ![]() | 469.1 KB | Display | |
Data in XML | ![]() | 13.1 KB | Display | |
Data in CIF | ![]() | 18.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6sqnC ![]() 6sqtC ![]() 6sqvC ![]() 6sr7C ![]() 1urnS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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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.) ![]() ![]() ![]() #2: RNA chain | Mass: 6610.940 Da / Num. of mol.: 3 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Chemical | ChemComp-MG / | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.62 Å3/Da / Density % sol: 65.98 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 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: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 1, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 2.37→51.6 Å / Num. obs: 29657 / % possible obs: 100 % / Redundancy: 38.2 % / CC1/2: 0.998 / Rmerge(I) obs: 0.29 / Rrim(I) all: 0.293 / Net I/σ(I): 12.4 |
Reflection shell | Resolution: 2.37→2.41 Å / Redundancy: 40.2 % / Rmerge(I) obs: 2.601 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 1460 / CC1/2: 0.753 / Rrim(I) all: 2.633 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1URN Resolution: 2.37→51.031 Å / Cor.coef. Fo:Fc: 0.923 / Cor.coef. Fo:Fc free: 0.894 / SU B: 8.263 / SU ML: 0.188 / Cross valid method: FREE R-VALUE / ESU R: 0.28 / ESU R Free: 0.244 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: 43.941 Å2
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Refinement step | Cycle: LAST / Resolution: 2.37→51.031 Å
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Refine LS restraints |
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LS refinement shell |
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