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Yorodumi- PDB-1opz: A core mutation affecting the folding properties of a soluble dom... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1opz | ||||||
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Title | A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis | ||||||
Components | Potential copper-transporting ATPase | ||||||
Keywords | HYDROLASE / mutation / folding / abbab fold | ||||||
Function / homology | Function and homology information P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion homeostasis / copper ion binding / ATP hydrolysis activity / ATP binding / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics, restrained energy minimization | ||||||
Model type details | minimized average | ||||||
Authors | Banci, L. / Bertini, I. / Ciofi-Baffoni, S. / Gonneli, L. / Su, X.C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilis. Authors: Banci, L. / Bertini, I. / Ciofi-Baffoni, S. / Gonnelli, L. / Su, X.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1opz.cif.gz | 32.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1opz.ent.gz | 22.1 KB | Display | PDB format |
PDBx/mmJSON format | 1opz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/op/1opz ftp://data.pdbj.org/pub/pdb/validation_reports/op/1opz | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8174.431 Da / Num. of mol.: 1 / Fragment: the first N-terminal water soluble domain of CopA / Mutation: S46V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: YVGX / Plasmid: PET21a / Production host: Escherichia coli (E. coli) / Strain (production host): pLysS / References: UniProt: O32220, Cu2+-exporting ATPase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using 15N labeled D1S46VCopA |
-Sample preparation
Details | Contents: 1.5 mM apoD1S46VCopA, 20mM phosphate, 90%H2O, 10%D2O,2.0 mM DTT Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 20 mM phosphate + 2 mMDTT / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics, restrained energy minimization Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: The submitted conformer model is the average of 30 structures with the lowest energy Conformers calculated total number: 30 / Conformers submitted total number: 1 |