+Open data
-Basic information
Entry | Database: PDB / ID: 1oia | |||||||||
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Title | U1A rnp domain 1-95 | |||||||||
Components | U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A | |||||||||
Keywords | RIBONUCLEOPROTEIN / NUCLEAR PROTEIN / RNA-BINDING | |||||||||
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 / MIR / Resolution: 2.4 Å | |||||||||
Authors | Nagai, K. / Evans, P.R. | |||||||||
Citation | Journal: Nature / Year: 1990 Title: Crystal Structure of the RNA-Binding Domain of the U1 Small Nuclear Ribonucleoprotein A Authors: Nagai, K. / Oubridge, C. / Jessen, T.H. / Li, J. / Evans, P.R. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oia.cif.gz | 44.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oia.ent.gz | 36.5 KB | Display | PDB format |
PDBx/mmJSON format | 1oia.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oi/1oia ftp://data.pdbj.org/pub/pdb/validation_reports/oi/1oia | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.1263, 0.1311, -0.9833), Vector: |
-Components
#1: Protein | Mass: 10946.722 Da / Num. of mol.: 2 / Fragment: RNP DOMAIN RESIDUES 1-95 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / 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: 3.09 Å3/Da / Density % sol: 60.23 % Description: DATA WERE COLLECTED USING THE WEISSENBERG METHOD. |
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Crystal grow | pH: 5.5 / Details: 2M NA/K PHOSPHATE PH 5.5 |
-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Type: PHOTON FACTORY / Wavelength: 1 |
Detector | Detector: WEISENBERG / Date: Mar 15, 1991 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→100 Å / Num. obs: 12666 / % possible obs: 95 % / Observed criterion σ(I): 6 / Redundancy: 9.4 % / Rmerge(I) obs: 0.074 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.4→105.41 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.918 / SU B: 7.095 / SU ML: 0.162 / Cross valid method: THROUGHOUT / ESU R: 0.283 / ESU R Free: 0.229 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. LOOP B48-B52 IS FLEXIBLE AND MAY BE WRONG
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.72 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→105.41 Å
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