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Open data
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Basic information
Entry | Database: PDB / ID: 4icx | ||||||
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Title | N-terminal C2 domain of human CEP120 | ||||||
![]() | Centrosomal protein of 120 kDa | ||||||
![]() | TRANSPORT PROTEIN / C2 domain / lipid binding | ||||||
Function / homology | ![]() positive regulation of centriole elongation / positive regulation of centrosome duplication / positive regulation of establishment of protein localization / interkinetic nuclear migration / astral microtubule organization / positive regulation of cilium assembly / centrosome cycle / centriole / neurogenesis / cerebral cortex development ...positive regulation of centriole elongation / positive regulation of centrosome duplication / positive regulation of establishment of protein localization / interkinetic nuclear migration / astral microtubule organization / positive regulation of cilium assembly / centrosome cycle / centriole / neurogenesis / cerebral cortex development / centrosome / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Janowski, R. / Guarin, N. / Coll, M. | ||||||
![]() | ![]() Title: N-terminal C2 domain tandem of human CEP120 shows lipid binding properties Authors: Janowski, R. / Guarin, N. / Speroni, S. / Serrano, L. / Coll, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 172 KB | Display | ![]() |
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PDB format | ![]() | 145.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 444.6 KB | Display | ![]() |
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Full document | ![]() | 446.9 KB | Display | |
Data in XML | ![]() | 16.3 KB | Display | |
Data in CIF | ![]() | 21.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 19547.953 Da / Num. of mol.: 3 / Fragment: C2 domain, UNP residues 1-151 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.75 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 200 mM sodium chloride and 23% (v/w) PEG 3350 , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 24, 2011 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97933 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / % possible obs: 96.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Biso Wilson estimate: 49.4 Å2 / Rmerge(I) obs: 0.086 / Net I/σ(I): 16.6 |
Reflection shell | Resolution: 2.7→2.77 Å / Rmerge(I) obs: 0.574 / Mean I/σ(I) obs: 3.2 / % possible all: 77.7 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 72.998 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.845 Å / Total num. of bins used: 10
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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