+Open data
-Basic information
Entry | Database: PDB / ID: 1zuy | ||||||
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Title | High-resolution structure of yeast Myo5 SH3 domain | ||||||
Components | Myosin-5 isoform | ||||||
Keywords | CONTRACTILE PROTEIN / SH3 domain | ||||||
Function / homology | Function and homology information bipolar cellular bud site selection / myosin I complex / actin cortical patch localization / cellular bud / positive regulation of Arp2/3 complex-mediated actin nucleation / cell tip / fungal-type cell wall organization / actin cortical patch / mating projection tip / vesicle transport along actin filament ...bipolar cellular bud site selection / myosin I complex / actin cortical patch localization / cellular bud / positive regulation of Arp2/3 complex-mediated actin nucleation / cell tip / fungal-type cell wall organization / actin cortical patch / mating projection tip / vesicle transport along actin filament / response to osmotic stress / microfilament motor activity / exocytosis / response to salt stress / receptor-mediated endocytosis / actin filament organization / cell periphery / endocytosis / actin filament binding / actin cytoskeleton / vesicle / hydrolase activity / ATP binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.39 Å | ||||||
Authors | Wilmanns, M. / Kursula, P. / Gonfloni, S. / Ferracuti, S. / Cesareni, G. | ||||||
Citation | Journal: To be published Title: High-resolution structure of yeast Myo5 SH3 domain Authors: Wilmanns, M. / Kursula, P. / Gonfloni, S. / Ferracuti, S. / Cesareni, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zuy.cif.gz | 62.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zuy.ent.gz | 47.2 KB | Display | PDB format |
PDBx/mmJSON format | 1zuy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zu/1zuy ftp://data.pdbj.org/pub/pdb/validation_reports/zu/1zuy | HTTPS FTP |
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-Related structure data
Related structure data | |
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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
#1: Protein | Mass: 6376.206 Da / Num. of mol.: 2 / Fragment: SH3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Production host: Escherichia coli (E. coli) / References: UniProt: Q04439 #2: Chemical | ChemComp-IPA / | #3: 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 Å3/Da / Density % sol: 38 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop Details: ammonium sulfate, isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.813 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 3, 2004 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.813 Å / Relative weight: 1 |
Reflection | Resolution: 1.39→20 Å / Num. all: 21535 / Num. obs: 21535 / % possible obs: 99 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 6.1 % / Biso Wilson estimate: 23 Å2 / Rsym value: 0.04 / Net I/σ(I): 20 |
Reflection shell | Resolution: 1.39→1.43 Å / Redundancy: 3.8 % / Mean I/σ(I) obs: 3.3 / Num. unique all: 1598 / Rsym value: 0.393 / % possible all: 90.6 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.39→20 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.957 / SU B: 2.99 / SU ML: 0.052 / Isotropic thermal model: ANISOTROPIC REFINEMENT / Cross valid method: THROUGHOUT / σ(F): -3 / ESU R: 0.074 / ESU R Free: 0.067 / Stereochemistry target values: Engh & Huber / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.972 Å2
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Refinement step | Cycle: LAST / Resolution: 1.39→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.39→1.426 Å / Total num. of bins used: 20
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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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