+Open data
-Basic information
Entry | Database: PDB / ID: 5ojf | ||||||
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Title | Crystal Structure of KLC2-TPR domain (fragment [A1-B6] | ||||||
Components | Kinesin light chain 2 | ||||||
Keywords | MOTOR PROTEIN / Kinesin1 / KLC2 / TPR domain | ||||||
Function / homology | Function and homology information lysosome localization / kinesin complex / microtubule / mitochondrion / nucleoplasm / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å | ||||||
Authors | Nguyen, T.Q. / Chenon, M. / Vilela, F. / Velours, C. / Andreani, J. / Fernandez-Varela, P. / Llinas, P. / Menetrey, J. | ||||||
Citation | Journal: PLoS ONE / Year: 2017 Title: Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain. Authors: Nguyen, T.Q. / Chenon, M. / Vilela, F. / Velours, C. / Aumont-Nicaise, M. / Andreani, J. / Varela, P.F. / Llinas, P. / Menetrey, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ojf.cif.gz | 327.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ojf.ent.gz | 271.4 KB | Display | PDB format |
PDBx/mmJSON format | 5ojf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5ojf_validation.pdf.gz | 454.6 KB | Display | wwPDB validaton report |
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Full document | 5ojf_full_validation.pdf.gz | 471.1 KB | Display | |
Data in XML | 5ojf_validation.xml.gz | 28 KB | Display | |
Data in CIF | 5ojf_validation.cif.gz | 37.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oj/5ojf ftp://data.pdbj.org/pub/pdb/validation_reports/oj/5ojf | HTTPS FTP |
-Related structure data
Related structure data | 5oj8C 3ceqS 3nf1S S: Starting model for refinement C: citing same article (ref.) |
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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: 35470.137 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Klc2, mCG_8395 / Production host: Escherichia coli (E. coli) / References: UniProt: Q91YS4 |
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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: 2.85 Å3/Da / Density % sol: 56.81 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: 12 % PEG 3350, 0.5 M Phos. pH 7.5 Glycerol 25 % |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.980097 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 15, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.980097 Å / Relative weight: 1 |
Reflection | Resolution: 3.4→48.14 Å / Num. obs: 16593 / % possible obs: 99.2 % / Redundancy: 3.6 % / Biso Wilson estimate: 135.76 Å2 / Rrim(I) all: 0.236 / Net I/σ(I): 4.55 |
Reflection shell | Resolution: 3.4→3.59 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 1.08 / Rrim(I) all: 1.168 / % possible all: 95.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3CEQ, 3NF1 Resolution: 3.4→20 Å / Cor.coef. Fo:Fc: 0.902 / Cor.coef. Fo:Fc free: 0.885 / Rfactor Rfree error: 0 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.529
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Displacement parameters | Biso mean: 127.81 Å2
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Refine analyze | Luzzati coordinate error obs: 0.54 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 3.4→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.4→3.63 Å / Rfactor Rfree error: 0 / Total num. of bins used: 8
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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