+Open data
-Basic information
Entry | Database: PDB / ID: 5zvp | ||||||
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Title | Aspergillus fumigatus Rho1 F25N | ||||||
Components | Rho GTPase Rho1 | ||||||
Keywords | ANTIBIOTIC / Aspergillus fumigatus / Rho1 GTPase / cell wall target | ||||||
Function / homology | Function and homology information asexual sporulation resulting in formation of a cellular spore / 1,3-beta-D-glucan synthase complex / hyphal tip / small GTPase-mediated signal transduction / GTPase activity / GTP binding Similarity search - Function | ||||||
Biological species | Aspergillus fumigatus Af293 (mold) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.42 Å | ||||||
Authors | Wei, W.F. / Van Aalten, D.M.F. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: To Be Published Title: Aspergillus fumigateurs Rho1 F25N Authors: Wei, W.F. / Van Aalten, D.M.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5zvp.cif.gz | 56.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5zvp.ent.gz | 38.4 KB | Display | PDB format |
PDBx/mmJSON format | 5zvp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5zvp_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 5zvp_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 5zvp_validation.xml.gz | 11.4 KB | Display | |
Data in CIF | 5zvp_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zv/5zvp ftp://data.pdbj.org/pub/pdb/validation_reports/zv/5zvp | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20328.240 Da / Num. of mol.: 1 / Mutation: F25N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus fumigatus Af293 (mold) / Strain: Af293 / Gene: rho1, AFUA_6G06900 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A068C8U8 |
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#2: Chemical | ChemComp-GDP / |
#3: Chemical | ChemComp-MG / |
#4: Chemical | ChemComp-SO4 / |
#5: 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: 2.24 Å3/Da / Density % sol: 45 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8 Details: 37.1% w/v PEG 5000 MME, 150 mM Tris pH 8.0, 40 mM magnesium sulphate. |
-Data collection
Diffraction | Mean temperature: 253 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: MASSIF-3 / Wavelength: 0.988 Å |
Detector | Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Mar 7, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.988 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→100 Å / Num. obs: 31770 / % possible obs: 99 % / Redundancy: 4.14 % / Net I/σ(I): 18.79 |
Reflection shell | Resolution: 1.42→1.47 Å |
-Processing
Software |
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Refinement | Resolution: 1.42→53.82 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.965 / SU B: 1.138 / SU ML: 0.043 / Cross valid method: THROUGHOUT / ESU R: 0.058 / ESU R Free: 0.061 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.694 Å2
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Refinement step | Cycle: 1 / Resolution: 1.42→53.82 Å
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Refine LS restraints |
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