+Open data
-Basic information
Entry | Database: PDB / ID: 6flk | ||||||
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Title | Crystal structure of Cep120 C2C domain | ||||||
Components | Cep120 | ||||||
Keywords | STRUCTURAL PROTEIN / Centriole / microtubule / Cep120 / C2 domain | ||||||
Function / homology | Function and homology information positive regulation of centriole elongation / positive regulation of establishment of protein localization / interkinetic nuclear migration / positive regulation of centrosome duplication / astral microtubule organization / positive regulation of cilium assembly / centrosome cycle / centriole / neurogenesis / cerebral cortex development ...positive regulation of centriole elongation / positive regulation of establishment of protein localization / interkinetic nuclear migration / positive regulation of centrosome duplication / astral microtubule organization / positive regulation of cilium assembly / centrosome cycle / centriole / neurogenesis / cerebral cortex development / centrosome / cytoplasm Similarity search - Function | ||||||
Biological species | homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.6 Å | ||||||
Authors | Sharma, A. / Gerard, S.F. / Olieric, N. / Steinmetz, M.O. | ||||||
Citation | Journal: J. Struct. Biol. / Year: 2018 Title: Cep120 promotes microtubule formation through a unique tubulin binding C2 domain. Authors: Sharma, A. / Gerard, S.F. / Olieric, N. / Steinmetz, M.O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6flk.cif.gz | 198.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6flk.ent.gz | 168.7 KB | Display | PDB format |
PDBx/mmJSON format | 6flk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fl/6flk ftp://data.pdbj.org/pub/pdb/validation_reports/fl/6flk | 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: 18537.324 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q8N960 #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: 2.39 Å3/Da / Density % sol: 48.55 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.03M magnesium chloride hexahydrate; 0.03M calcium chloride dehydrate, 0.1M Tris(Base)/BICINE pH 8.5, 20% v/v Ethylene glycol and 10 % w/v PEG 8000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 30, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→39.97 Å / Num. obs: 42539 / % possible obs: 93.83 % / Redundancy: 1.8 % / Biso Wilson estimate: 15.125252799 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.0819 / Rrim(I) all: 0.1158 / Net I/σ(I): 6.87 |
Reflection shell | Resolution: 1.6→1.657 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.6926 / Mean I/σ(I) obs: 1.08 / Num. unique obs: 3744 / CC1/2: 0.439 / Rrim(I) all: 0.9794 / % possible all: 83.09 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.6→39.97 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.2 / Phase error: 27.61
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→39.97 Å
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Refine LS restraints |
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LS refinement shell |
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