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Yorodumi- PDB-3pa6: Structure of the N-terminal BRCT domain of human microcephalin (MCPH1) -
+Open data
-Basic information
Entry | Database: PDB / ID: 3pa6 | ||||||
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Title | Structure of the N-terminal BRCT domain of human microcephalin (MCPH1) | ||||||
Components | Microcephalin | ||||||
Keywords | CELL CYCLE / BRCT DOMAIN | ||||||
Function / homology | Function and homology information regulation of chromosome condensation / neuronal stem cell population maintenance / regulation of centrosome cycle / protein localization to centrosome / establishment of mitotic spindle orientation / Condensation of Prophase Chromosomes / bone development / cerebral cortex development / mitotic cell cycle / regulation of inflammatory response ...regulation of chromosome condensation / neuronal stem cell population maintenance / regulation of centrosome cycle / protein localization to centrosome / establishment of mitotic spindle orientation / Condensation of Prophase Chromosomes / bone development / cerebral cortex development / mitotic cell cycle / regulation of inflammatory response / centrosome / negative regulation of transcription by RNA polymerase II / nucleoplasm / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.5 Å | ||||||
Authors | Singh, N. / Heroux, A. / Thompson, J.R. / Mer, G. | ||||||
Citation | Journal: To be Published Title: Structure of the N-terminal BRCT domain of human microcephalin (MCPH1) Authors: Singh, N. / Heroux, A. / Thompson, J.R. / Mer, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3pa6.cif.gz | 189.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3pa6.ent.gz | 162.2 KB | Display | PDB format |
PDBx/mmJSON format | 3pa6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pa/3pa6 ftp://data.pdbj.org/pub/pdb/validation_reports/pa/3pa6 | 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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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 12087.342 Da / Num. of mol.: 3 / Fragment: BRCT DOMAIN, UNP residues 1-105 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MCPH1 / Plasmid: pGB1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8NEM0 #2: Chemical | ChemComp-CL / | #3: 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: 2.02 Å3/Da / Density % sol: 39.24 % |
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Crystal grow | Temperature: 295 K / pH: 7 Details: 0.2M sodium succinate, 15% PEG 3350, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.979095 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 10, 2008 |
Radiation | Monochromator: SI(111) / Protocol: SAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979095 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→35.53 Å / Num. obs: 41554 / % possible obs: 88.9 % / Redundancy: 6.4 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 46.1 |
Reflection shell | Resolution: 1.5→1.55 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.431 / Mean I/σ(I) obs: 1.9 / % possible all: 43.1 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.5→35.53 Å / SU ML: 0.15 / σ(F): 0 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 78.52 Å2 / ksol: 0.5 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.5→35.53 Å
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Refine LS restraints |
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LS refinement shell |
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