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Yorodumi- PDB-1ii9: CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ii9 | ||||||
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Title | CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE IN COMPLEX WITH AMP-PNP | ||||||
Components | ARSENICAL PUMP-DRIVING ATPASE | ||||||
Keywords | HYDROLASE / ArsA ATPase / AMP-PNP / ATP binding site | ||||||
Function / homology | Function and homology information arsenite-transporting ATPase / ATPase-coupled arsenite transmembrane transporter activity / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Zhou, T. / Radaev, S. / Gatti, D.L. / Rosen, B.P. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation. Authors: Zhou, T. / Radaev, S. / Rosen, B.P. / Gatti, D.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ii9.cif.gz | 238.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ii9.ent.gz | 187 KB | Display | PDB format |
PDBx/mmJSON format | 1ii9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ii/1ii9 ftp://data.pdbj.org/pub/pdb/validation_reports/ii/1ii9 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 64084.992 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: ARSA / Production host: Escherichia coli (E. coli) / References: UniProt: P08690, EC: 3.6.3.16 |
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-Non-polymers , 7 types, 303 molecules
#2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-CD / #4: Chemical | ChemComp-CL / #5: Chemical | #6: Chemical | #7: Chemical | #8: 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: 2.46 Å3/Da / Density % sol: 50.03 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 303 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG3000, ADP, MgCl2, NaASO2, CdCl2, Bistrispropane, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 30 ℃ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 18, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→36.52 Å / Num. all: 198246 / Num. obs: 198246 / % possible obs: 93.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.2 % / Biso Wilson estimate: 44.5 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 5.5 |
Reflection | *PLUS Num. obs: 37265 / Num. measured all: 198246 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→36.52 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 301526.59 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 43.62 Å2 / ksol: 0.333 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 46 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→36.52 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS σ(F): 2 / % reflection Rfree: 10 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 46 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.351 / % reflection Rfree: 10.7 % / Rfactor Rwork: 0.256 |