+Open data
-Basic information
Entry | Database: PDB / ID: 5ng4 | |||||||||
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Title | Human CEP135 parallel dimeric coiled coil 82-144 | |||||||||
Components | Centrosomal protein of 135 kDaCentrosome | |||||||||
Keywords | MICROTUBULE-BINDING PROTEIN / coiled coil / CEP135 / centrosome / disulfide bridges | |||||||||
Function / homology | Function and homology information positive regulation of establishment of protein localization / positive regulation of non-motile cilium assembly / centriole-centriole cohesion / centriole replication / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / centriole ...positive regulation of establishment of protein localization / positive regulation of non-motile cilium assembly / centriole-centriole cohesion / centriole replication / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / centriole / AURKA Activation by TPX2 / Regulation of PLK1 Activity at G2/M Transition / centrosome / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.14 Å | |||||||||
Authors | Kraatz, S.H.W. / Bianchi, S. / Steinmetz, M.O. | |||||||||
Funding support | Switzerland, 2items
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Citation | Journal: Biosci. Rep. / Year: 2018 Title: Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils. Authors: Kraatz, S.H.W. / Bianchi, S. / 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 | 5ng4.cif.gz | 32 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ng4.ent.gz | 23.9 KB | Display | PDB format |
PDBx/mmJSON format | 5ng4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ng/5ng4 ftp://data.pdbj.org/pub/pdb/validation_reports/ng/5ng4 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 7727.894 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CEP135, CEP4, KIAA0635 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q66GS9 #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: 2.41 Å3/Da / Density % sol: 48.92 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop / Details: 25% PEG 1500, SPG buffer, pH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 2.0664 Å |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Mar 20, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 2.0664 Å / Relative weight: 1 |
Reflection | Resolution: 2.14→39.5 Å / Num. obs: 7467 / % possible obs: 86 % / Redundancy: 41.5 % / CC1/2: 0.999 / Rmerge(I) obs: 0.089 / Net I/σ(I): 31.3 |
Reflection shell | Resolution: 2.14→2.21 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.178 / Num. unique obs: 356 / CC1/2: 0.973 / % possible all: 43 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.14→39.5 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.44 / Phase error: 29.06
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.14→39.5 Å
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Refine LS restraints |
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LS refinement shell |
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