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Yorodumi- PDB-4gkp: Structure of the truncated neck and C-terminal motor homology dom... -
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Basic information
| Entry | Database: PDB / ID: 4gkp | ||||||
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| Title | Structure of the truncated neck and C-terminal motor homology domain of ViK1 from Candida glabrata | ||||||
Components | Spindle pole body-associated protein VIK1 | ||||||
Keywords | STRUCTURAL PROTEIN / kinesin motor domain-like fold / Microtubule binding protein / Kinesin associated protein / Kar3 | ||||||
| Function / homology | Function and homology information | ||||||
| Biological species | Candida glabrata (fungus) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.42 Å | ||||||
Authors | Duan, D. / Allingham, J.S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2012Title: Neck Rotation and Neck Mimic Docking in the Noncatalytic Kar3-associated Protein Vik1. Authors: Duan, D. / Jia, Z. / Joshi, M. / Brunton, J. / Chan, M. / Drew, D. / Davis, D. / Allingham, J.S. | ||||||
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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 | 4gkp.cif.gz | 108.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4gkp.ent.gz | 81.7 KB | Display | PDB format |
| PDBx/mmJSON format | 4gkp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4gkp_validation.pdf.gz | 438.7 KB | Display | wwPDB validaton report |
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| Full document | 4gkp_full_validation.pdf.gz | 442.5 KB | Display | |
| Data in XML | 4gkp_validation.xml.gz | 18.5 KB | Display | |
| Data in CIF | 4gkp_validation.cif.gz | 25.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gk/4gkp ftp://data.pdbj.org/pub/pdb/validation_reports/gk/4gkp | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4gkqC ![]() 4gkrC ![]() 2o0aS C: citing same article ( 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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| 2 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 31902.449 Da / Num. of mol.: 2 / Fragment: UNP residues 313-584 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida glabrata (fungus)Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65 Gene: CAGL0D00638G, CAGL0H00638g / Plasmid: Modified pET16b / Production host: ![]() #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: 2.19 Å3/Da / Density % sol: 43.83 % |
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| Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.1M HEPES, 13% PEG-6000, 5% isopropanol, 75mM NaAcetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
| Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X6A / Wavelength: 0.976 Å | |||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Oct 5, 2008 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 2.42→20 Å / Num. all: 22019 / Num. obs: 21752 / % possible obs: 98.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.8 % / Biso Wilson estimate: 49.904 Å2 / Rmerge(I) obs: 0.035 / Net I/σ(I): 37.65 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB entry 2O0A Resolution: 2.42→19.83 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.913 / WRfactor Rfree: 0.2543 / WRfactor Rwork: 0.2074 / Occupancy max: 1 / Occupancy min: 0.47 / FOM work R set: 0.8162 / SU B: 7.793 / SU ML: 0.184 / SU R Cruickshank DPI: 0.4339 / SU Rfree: 0.2752 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.434 / ESU R Free: 0.275 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 99.62 Å2 / Biso mean: 43.2617 Å2 / Biso min: 17.4 Å2
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| Refinement step | Cycle: LAST / Resolution: 2.42→19.83 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.42→2.482 Å / Total num. of bins used: 20
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Candida glabrata (fungus)
X-RAY DIFFRACTION
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