+Open data
-Basic information
Entry | Database: PDB / ID: 6q8f | ||||||
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Title | Nterminal domain of human SMU1 | ||||||
Components | WD40 repeat-containing protein SMU1 | ||||||
Keywords | SPLICING / Splicing factor | ||||||
Function / homology | Function and homology information U2-type precatalytic spliceosome / precatalytic spliceosome / regulation of alternative mRNA splicing, via spliceosome / mRNA Splicing - Major Pathway / RNA splicing / mRNA splicing, via spliceosome / nuclear speck / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.9 Å | ||||||
Authors | Tengo, L. / Le Corre, L. / Fournier, G. / Ashraf, U. / Busca, P. / Rameix-Welti, M.-A. / Gravier-Pelletier, C. / Ruigrok, R.W.H. / Jacob, Y. / Vidalain, P.-O. ...Tengo, L. / Le Corre, L. / Fournier, G. / Ashraf, U. / Busca, P. / Rameix-Welti, M.-A. / Gravier-Pelletier, C. / Ruigrok, R.W.H. / Jacob, Y. / Vidalain, P.-O. / Pietrancosta, N. / Naffakh, N. / McCarthy, A.A. / Crepin, T. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2019 Title: Destabilization of the human RED-SMU1 splicing complex as a basis for host-directed antiinfluenza strategy. Authors: Ashraf, U. / Tengo, L. / Le Corre, L. / Fournier, G. / Busca, P. / McCarthy, A.A. / Rameix-Welti, M.A. / Gravier-Pelletier, C. / Ruigrok, R.W.H. / Jacob, Y. / Vidalain, P.O. / Pietrancosta, ...Authors: Ashraf, U. / Tengo, L. / Le Corre, L. / Fournier, G. / Busca, P. / McCarthy, A.A. / Rameix-Welti, M.A. / Gravier-Pelletier, C. / Ruigrok, R.W.H. / Jacob, Y. / Vidalain, P.O. / Pietrancosta, N. / Crepin, T. / Naffakh, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6q8f.cif.gz | 99.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6q8f.ent.gz | 75.5 KB | Display | PDB format |
PDBx/mmJSON format | 6q8f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q8/6q8f ftp://data.pdbj.org/pub/pdb/validation_reports/q8/6q8f | 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: 57673.797 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMU1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q2TAY7 #2: Chemical | ChemComp-BTB / | #3: Chemical | ChemComp-CL / | #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 grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.1 M Bis-Tris pH 5.5, 16-20 % PEG 10K, 0.1 M ammonium acetate |
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-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.95373 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 10, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95373 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 31423 / % possible obs: 97.2 % / Redundancy: 5.6 % / Rrim(I) all: 0.064 / Net I/σ(I): 22.3 |
Reflection shell | Resolution: 1.9→1.95 Å / Redundancy: 3.3 % / Mean I/σ(I) obs: 2.36 / Num. unique obs: 1956 / Rrim(I) all: 0.536 / % possible all: 81.5 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.9→39.14 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.939 / SU B: 3.483 / SU ML: 0.1 / Cross valid method: THROUGHOUT / ESU R: 0.15 / ESU R Free: 0.138 / Details: HYDROGENS HAVE BEEN ADDED IN THE 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: 25.692 Å2
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Refinement step | Cycle: 1 / Resolution: 1.9→39.14 Å
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Refine LS restraints |
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