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Yorodumi- PDB-2wog: Intermediate and final states of human kinesin Eg5 in complex wit... -
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-Basic information
Entry | Database: PDB / ID: 2wog | ||||||
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Title | Intermediate and final states of human kinesin Eg5 in complex with S-trityl-L-cysteine | ||||||
Components | KINESIN-LIKE PROTEIN KIF11 | ||||||
Keywords | CELL CYCLE / ATP-BINDING / MOTOR PROTEIN / MITOSIS / MICROTUBULE / CELL DIVISION / PHOSPHOPROTEIN / NUCLEOTIDE-BINDING | ||||||
Function / homology | Function and homology information spindle elongation / regulation of mitotic centrosome separation / Kinesins / plus-end-directed microtubule motor activity / mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / microtubule motor activity / kinesin complex / spindle organization / microtubule-based movement ...spindle elongation / regulation of mitotic centrosome separation / Kinesins / plus-end-directed microtubule motor activity / mitotic centrosome separation / COPI-dependent Golgi-to-ER retrograde traffic / microtubule motor activity / kinesin complex / spindle organization / microtubule-based movement / mitotic spindle assembly / MHC class II antigen presentation / mitotic spindle organization / spindle microtubule / mitotic spindle / spindle pole / spindle / mitotic cell cycle / microtubule binding / microtubule / cell division / protein kinase binding / protein-containing complex / ATP binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Kaan, H.Y.K. / Ulaganathan, V. / Hackney, D.D. / Kozielski, F. | ||||||
Citation | Journal: Biochem.J. / Year: 2010 Title: An Allosteric Transition Trapped in an Intermediate State of a New Kinesin-Inhibitor Complex. Authors: Kaan, H.Y.K. / Ulaganathan, V. / Hackney, D.D. / Kozielski, F. | ||||||
History |
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Remark 700 | THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE ... THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2wog.cif.gz | 450.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2wog.ent.gz | 368.5 KB | Display | PDB format |
PDBx/mmJSON format | 2wog.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2wog_validation.pdf.gz | 2.4 MB | Display | wwPDB validaton report |
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Full document | 2wog_full_validation.pdf.gz | 2.4 MB | Display | |
Data in XML | 2wog_validation.xml.gz | 49.1 KB | Display | |
Data in CIF | 2wog_validation.cif.gz | 71.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wo/2wog ftp://data.pdbj.org/pub/pdb/validation_reports/wo/2wog | HTTPS FTP |
-Related structure data
Related structure data | 1x88S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 41055.582 Da / Num. of mol.: 3 / Fragment: MOTOR DOMAIN, RESIDUES 1-368 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) PLYSS / References: UniProt: P52732 #2: Chemical | #3: Chemical | #4: Chemical | #5: 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: 2.79 Å3/Da / Density % sol: 55.9 % / Description: NONE |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 22% PEG 3350, 0.15M SODIUM TARTRATE DIBASIC DIHYDRATE, 0.1M MES PH 6.5 |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1.076 |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 2, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.076 Å / Relative weight: 1 |
Reflection | Resolution: 2→29.16 Å / Num. obs: 87598 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 5.8 % / Biso Wilson estimate: 27.2 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 4 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1X88 Resolution: 2→29.16 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.937 / SU B: 7.431 / SU ML: 0.096 / Cross valid method: THROUGHOUT / ESU R: 0.747 / ESU R Free: 0.147 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.13 Å2
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Refinement step | Cycle: LAST / Resolution: 2→29.16 Å
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