+Open data
-Basic information
Entry | Database: PDB / ID: 4bn2 | |||||||||
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Title | The crystal structure of kinesin-like protein KIF15 | |||||||||
Components | KINESIN-LIKE PROTEIN KIF15 | |||||||||
Keywords | MOTOR PROTEIN / KINESIN / MOTOR DOMAIN | |||||||||
Function / homology | Function and homology information plus-end kinesin complex / Kinesins / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / microtubule motor activity / microtubule-based movement / cytoskeletal motor activity / MHC class II antigen presentation / spindle / mitotic cell cycle ...plus-end kinesin complex / Kinesins / COPI-dependent Golgi-to-ER retrograde traffic / kinesin complex / microtubule motor activity / microtubule-based movement / cytoskeletal motor activity / MHC class II antigen presentation / spindle / mitotic cell cycle / microtubule binding / microtubule / centrosome / ATP hydrolysis activity / ATP binding / membrane / cytosol Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.695 Å | |||||||||
Authors | Klejnot, M. / Falnikar, A. / Ulaganathan, V. / Cross, R. / Baas, P. / Kozielski, F. | |||||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2014 Title: The Crystal Structure and Biochemical Characterization of Kif15: A Bifunctional Molecular Motor Involved in Bipolar Spindle Formation and Neuronal Development Authors: Klejnot, M. / Falnikar, A. / Ulaganathan, V. / Cross, R.A. / Baas, P.W. / Kozielski, F. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4bn2.cif.gz | 205.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4bn2.ent.gz | 160.5 KB | Display | PDB format |
PDBx/mmJSON format | 4bn2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bn/4bn2 ftp://data.pdbj.org/pub/pdb/validation_reports/bn/4bn2 | HTTPS FTP |
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-Related structure data
Related structure data | 1t5cS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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-Components
#1: Protein | Mass: 39374.340 Da / Num. of mol.: 3 / Fragment: MOTOR DOMAIN, RESIDUES 19-375 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PETM20MOD / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS-RIPL / References: UniProt: Q9NS87 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | RESIDUES 1 TO 4 CHANGED DUE TO CLONING | |
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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: 2.74 Å3/Da / Density % sol: 57.22 % / Description: NONE |
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Crystal grow | Temperature: 292 K / pH: 6 Details: 25% POLYETHYLENE GLYCOL-3350 0.20 M MAGNESIUM CHLORIDE 0.1 M TRIS-HC; PH 8.5 |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.8726 |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 23, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. obs: 29592 / % possible obs: 89.7 % / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Biso Wilson estimate: 37.87 Å2 / Rmerge(I) obs: 0.098 / Net I/σ(I): 8.6 |
Reflection shell | Highest resolution: 2.7 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.378 / Mean I/σ(I) obs: 3.1 / % possible all: 86.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1T5C Resolution: 2.695→29.486 Å / SU ML: 0.88 / σ(F): 1.34 / Phase error: 27.16 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 28.074 Å2 / ksol: 0.335 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.695→29.486 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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