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Open data
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Basic information
| Entry | Database: PDB / ID: 5c9n | ||||||
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| Title | Crystal structure of GEMC1 coiled-coil domain | ||||||
Components | Geminin coiled-coil domain-containing protein 1 | ||||||
Keywords | CELL CYCLE / Geminin Idas coiled coil DNA replication license | ||||||
| Function / homology | Function and homology informationmulti-ciliated epithelial cell differentiation / cerebrospinal fluid circulation / regulation of DNA-templated DNA replication initiation / seminiferous tubule development / negative regulation of cell cycle / cilium assembly / single fertilization / multicellular organism growth / spermatogenesis / DNA replication ...multi-ciliated epithelial cell differentiation / cerebrospinal fluid circulation / regulation of DNA-templated DNA replication initiation / seminiferous tubule development / negative regulation of cell cycle / cilium assembly / single fertilization / multicellular organism growth / spermatogenesis / DNA replication / chromatin binding / extracellular region / nucleus Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Caillat, C. / Perrakis, A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2015Title: The structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins. Authors: Caillat, C. / Fish, A. / Pefani, D.E. / Taraviras, S. / Lygerou, Z. / Perrakis, A. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5c9n.cif.gz | 71.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5c9n.ent.gz | 54.3 KB | Display | PDB format |
| PDBx/mmJSON format | 5c9n.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5c9n_validation.pdf.gz | 448.2 KB | Display | wwPDB validaton report |
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| Full document | 5c9n_full_validation.pdf.gz | 448.7 KB | Display | |
| Data in XML | 5c9n_validation.xml.gz | 7.4 KB | Display | |
| Data in CIF | 5c9n_validation.cif.gz | 9.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c9/5c9n ftp://data.pdbj.org/pub/pdb/validation_reports/c9/5c9n | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1uiiS S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 10062.223 Da / Num. of mol.: 2 / Fragment: UNP residues 64-148 / Mutation: L123E, L130E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GMNC, GEMC1 / Production host: ![]() #2: Chemical | #3: Water | ChemComp-HOH / | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 3.64 Å3/Da / Density % sol: 66.24 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.1 M Hepes buffer pH 7.5, 7% Ethanol, 10% 2-Methyl-2,4-pentanediol (MPD) 0.01 M Ethylene-diamine-tetra-acetic acid disodium salt dihydrate. |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726 Å |
| Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 3, 2012 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
| Reflection | Resolution: 2.2→53.8 Å / Num. obs: 15376 / % possible obs: 99.5 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 11.8 |
| Reflection shell | Resolution: 2.2→2.32 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.871 / Mean I/σ(I) obs: 1.5 / % possible all: 99.8 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1UII Resolution: 2.2→53.78 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.945 / SU B: 11.959 / SU ML: 0.14 / Cross valid method: THROUGHOUT / ESU R: 0.175 / ESU R Free: 0.16 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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| Solvent computation | Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 54.241 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.2→53.78 Å
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| Refine LS restraints |
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Homo sapiens (human)
X-RAY DIFFRACTION
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