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Yorodumi- PDB-6qdj: Molecular features of the UNC-45 chaperone critical for binding a... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6qdj | ||||||
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Title | Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin | ||||||
Components | Myosin-4 | ||||||
Keywords | MOTOR PROTEIN / MYOSIN / MHC-B / UNC-54 | ||||||
Function / homology | Function and homology information egg-laying behavior / striated muscle myosin thick filament / skeletal muscle myosin thick filament assembly / muscle myosin complex / locomotion / A band / structural constituent of muscle / microfilament motor activity / muscle contraction / actin filament binding / ATP binding Similarity search - Function | ||||||
Biological species | Caenorhabditis elegans (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.884 Å | ||||||
Authors | Meinhart, A. / Clausen, T. / Arnese, R. | ||||||
Funding support | Austria, 1items
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Citation | Journal: Nat Commun / Year: 2019 Title: Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin. Authors: Hellerschmied, D. / Lehner, A. / Franicevic, N. / Arnese, R. / Johnson, C. / Vogel, A. / Meinhart, A. / Kurzbauer, R. / Deszcz, L. / Gazda, L. / Geeves, M. / Clausen, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6qdj.cif.gz | 178.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6qdj.ent.gz | 136.9 KB | Display | PDB format |
PDBx/mmJSON format | 6qdj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6qdj_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 6qdj_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 6qdj_validation.xml.gz | 30.8 KB | Display | |
Data in CIF | 6qdj_validation.cif.gz | 44 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qd/6qdj ftp://data.pdbj.org/pub/pdb/validation_reports/qd/6qdj | HTTPS FTP |
-Related structure data
Related structure data | 6qdkC 6qdlC 6qdmC 5m05S 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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Unit cell |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 90372.297 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: unc-54, myo-4, F11C3.3 / Plasmid: bFastBac Dual / Cell line (production host): Hi5 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P02566 |
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-Non-polymers , 7 types, 253 molecules
#2: Chemical | ChemComp-ADP / | ||||||||||
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#3: Chemical | ChemComp-GOL / #4: Chemical | ChemComp-BU1 / | #5: Chemical | #6: Chemical | ChemComp-HEZ / | #7: Chemical | ChemComp-P15 / | #8: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.33 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 100 mM MES/imidazole pH 6.5 10 % PEG 4000 20 % glycerol 20 mM 1,6-hexandiol 20 mM 1-butanol 20 mM (RS)-1,2-propanediol 20 mM 2-propanol 20 mM 1,4-butanediol 20 mM 1,3-propandiol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.9763 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 17, 2016 |
Radiation | Monochromator: KB-mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.884→85 Å / Num. obs: 76208 / % possible obs: 93.8 % / Redundancy: 3.3 % / Biso Wilson estimate: 37.5 Å2 / CC1/2: 0.999 / Rrim(I) all: 0.045 / Net I/σ(I): 19.6 |
Reflection shell | Resolution: 1.884→2.05 Å / Redundancy: 2.9 % / Mean I/σ(I) obs: 2.9 / CC1/2: 0.866 / Rrim(I) all: 0.454 / % possible all: 78 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5m05 Resolution: 1.884→84.026 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 22.81
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.884→84.026 Å
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Refine LS restraints |
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LS refinement shell |
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