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Yorodumi- PDB-1yr7: PAB0955 crystal structure : a GTPase in GTP-gamma-S bound form fr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1yr7 | ||||||
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Title | PAB0955 crystal structure : a GTPase in GTP-gamma-S bound form from Pyrococcus abyssi | ||||||
Components | ATP(GTP)binding protein | ||||||
Keywords | HYDROLASE / GTP binding protein / GTPase / P-loop / Rossmann Fold / GTP analog | ||||||
Function / homology | Function and homology information Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / GTPase activity / GTP binding Similarity search - Function | ||||||
Biological species | Pyrococcus abyssi (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.08 Å | ||||||
Authors | Gras, S. / Carpentier, P. / Armengaud, J. / Housset, D. | ||||||
Citation | Journal: Embo Rep. / Year: 2007 Title: Structural insights into a new homodimeric self-activated GTPase family. Authors: Gras, S. / Chaumont, V. / Fernandez, B. / Carpentier, P. / Charrier-Savournin, F. / Schmitt, S. / Pineau, C. / Flament, D. / Hecker, A. / Forterre, P. / Armengaud, J. / Housset, D. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2005 Title: Expression, purification, crystallization and preliminary crystallographic analysis of the PAB0955 gene product Authors: Gras, S. / Fernandez, B. / Chaumont, V. / Carpentier, P. / Armengaud, J. / Housset, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1yr7.cif.gz | 67.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1yr7.ent.gz | 49.3 KB | Display | PDB format |
PDBx/mmJSON format | 1yr7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yr/1yr7 ftp://data.pdbj.org/pub/pdb/validation_reports/yr/1yr7 | HTTPS FTP |
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-Related structure data
Related structure data | 1yr6SC 1yr8C 1yr9C 1yraC 1yrbC 2oxrC 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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Details | The biological assembly is a dimer generated by the two fold axis : y, x, -z |
-Components
#1: Protein | Mass: 30334.795 Da / Num. of mol.: 1 / Fragment: residues 1-248 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus abyssi (archaea) / Gene: PAB0955 / Plasmid: pCRT7/NT-topo / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta(DE3)pLys / References: GenBank: 5458856, UniProt: Q9UYR9*PLUS |
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#2: Chemical | ChemComp-GSP / |
#3: 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 Å3/Da / Density % sol: 38.5 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 13% PEG 4000, 0.2M ammonium acetate, 0.1M tri-sodium citrate dihydrate, 20mM DTT, 0.65mM GTP-gamma-S, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.979 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 18, 2004 / Details: mirror |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.08→50 Å / Num. all: 15141 / Num. obs: 15034 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.5 % / Biso Wilson estimate: 45 Å2 / Rmerge(I) obs: 0.069 / Rsym value: 0.069 / Net I/σ(I): 17.75 |
Reflection shell | Resolution: 2.08→2.15 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.232 / Mean I/σ(I) obs: 6.36 / Num. unique all: 893 / Rsym value: 0.232 / % possible all: 64.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1YR6 Resolution: 2.08→15 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.899 / SU B: 7.122 / SU ML: 0.193 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.426 / ESU R Free: 0.295 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 45.443 Å2
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Refinement step | Cycle: LAST / Resolution: 2.08→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.087→2.159 Å / Total num. of bins used: 15
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