+Open data
-Basic information
Entry | Database: PDB / ID: 6jik | ||||||
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Title | Aspergillus fumigatus Rho1 GsGTP | ||||||
Components | Rho GTPase Rho1 | ||||||
Keywords | SIGNALING PROTEIN / Aspergillus fumigateurs / 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 var. fumigatus (mold) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.35 Å | ||||||
Authors | Bartual, S.G. / Van Aalten, D.M.F. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: To Be Published Title: Aspergillus fumigatus Rho1 gSGTP complex Authors: Sergio, G.B. / 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 | 6jik.cif.gz | 91.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6jik.ent.gz | 66.7 KB | Display | PDB format |
PDBx/mmJSON format | 6jik.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ji/6jik ftp://data.pdbj.org/pub/pdb/validation_reports/ji/6jik | HTTPS FTP |
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-Related structure data
Related structure data | 5zvpS S: Starting model for refinement |
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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: 21701.008 Da / Num. of mol.: 1 / Mutation: F25N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus fumigatus var. fumigatus (mold) Production host: Escherichia coli (E. coli) / References: UniProt: A0A068C8U8 |
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#2: Chemical | ChemComp-GSP / |
#3: Chemical | ChemComp-MG / |
#4: 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: 2.11 Å3/Da / Density % sol: 41.84 % |
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Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, sitting drop Details: crystals were obtained in Morpheus commercial crystallization screen, Imidazole and MES monohydrate (acid) at pH 6.5, 40% v/v PEG 500 MME and 20 % w/v PEG 20000, and 0.2M 1,6-Hexanediol, 0. ...Details: crystals were obtained in Morpheus commercial crystallization screen, Imidazole and MES monohydrate (acid) at pH 6.5, 40% v/v PEG 500 MME and 20 % w/v PEG 20000, and 0.2M 1,6-Hexanediol, 0.2M 1-Butanol 0.2M 1,2-Propanediol, 0.2M 2-Propanol, 0.2M 1,4- Butanediol and 0.2M 1,3-Propanediol. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SEALED TUBE / Type: RIGAKU MICROMAX-003 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU SATURN 944 / Detector: CCD / Date: Jan 8, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→30.11 Å / Num. obs: 8136 / % possible obs: 99.9 % / Redundancy: 6.5 % / CC1/2: 0.982 / Rmerge(I) all: 0.182 / Rmerge(I) obs: 0.192 / Rpim(I) all: 0.115 / Net I/av σ(I): 5.8 / Net I/σ(I): 5.8 |
Reflection shell | Resolution: 2.35→2.43 Å / Redundancy: 5.3 % / Rmerge(I) all: 0.35 / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 3.2 / Num. unique obs: 767 / CC1/2: 0.909 / Rpim(I) all: 0.246 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5ZVP Resolution: 2.35→30.11 Å / Cor.coef. Fo:Fc: 0.895 / Cor.coef. Fo:Fc free: 0.835 / SU B: 16.221 / SU ML: 0.232 / Cross valid method: THROUGHOUT / ESU R: 0.623 / ESU R Free: 0.3 / 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: 18.237 Å2
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Refinement step | Cycle: 1 / Resolution: 2.35→30.11 Å
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Refine LS restraints |
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