+Open data
-Basic information
Entry | Database: PDB / ID: 4mfu | ||||||
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Title | Crystal structure of human CTNNBL1(residues 77~563) | ||||||
Components | Beta-catenin-like protein 1 | ||||||
Keywords | GENE REGULATION / ARM repeats | ||||||
Function / homology | Function and homology information somatic diversification of immunoglobulins / Prp19 complex / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / adaptive immune response / positive regulation of apoptotic process / centrosome / enzyme binding / nucleoplasm ...somatic diversification of immunoglobulins / Prp19 complex / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / adaptive immune response / positive regulation of apoptotic process / centrosome / enzyme binding / nucleoplasm / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.744 Å | ||||||
Authors | Ahn, J.W. / Kim, S. / Kim, K.J. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2014 Title: Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with the hPrp19-CDC5L complex Authors: Ahn, J.W. / Kim, S. / Kim, E.J. / Kim, Y.J. / Kim, K.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mfu.cif.gz | 108.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mfu.ent.gz | 83.5 KB | Display | PDB format |
PDBx/mmJSON format | 4mfu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mf/4mfu ftp://data.pdbj.org/pub/pdb/validation_reports/mf/4mfu | HTTPS FTP |
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-Related 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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-Components
#1: Protein | Mass: 56379.742 Da / Num. of mol.: 1 / Fragment: UNP residues 77-563 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CTNNBL1, C20orf33, PP8304 / Plasmid: pPosKJ / Production host: Escherichia coli (E. coli) / Strain (production host): B834 / References: UniProt: Q8WYA6 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.74 Å3/Da / Density % sol: 67.08 % / Mosaicity: 0.767 ° |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 9.5 Details: PEG8000, CAPs, NaCl, pH 9.5, vapor diffusion, hanging drop, temperature 295K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Redundancy: 13.9 % / Number: 302721 / Rmerge(I) obs: 0.095 / Χ2: 4.14 / D res high: 2.74 Å / D res low: 50 Å / Num. obs: 21766 / % possible obs: 95.8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Diffraction reflection shell |
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Reflection | Resolution: 2.74→47.38 Å / Num. obs: 22673 / % possible obs: 95.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 13.9 % / Rmerge(I) obs: 0.095 / Rsym value: 0.082 / Net I/σ(I): 36.9 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1,2
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-Phasing
Phasing | Method: SAD |
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-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.744→47.33 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.909 / Occupancy max: 1 / Occupancy min: 1 / SU B: 18.978 / SU ML: 0.379 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.622 / ESU R Free: 0.393 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 192.1 Å2 / Biso mean: 85.3169 Å2 / Biso min: 20 Å2
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Refinement step | Cycle: LAST / Resolution: 2.744→47.33 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.744→2.815 Å / Total num. of bins used: 20
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