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Yorodumi- PDB-2khk: NMR solution structure of the b30-82 domain of subunit b of Esche... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2khk | ||||||
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Title | NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase | ||||||
Components | ATP synthase subunit b | ||||||
Keywords | TRANSPORT PROTEIN / b30-82 / F1FO ATP synthase / NMR spectroscopy / ATP synthesis / Cell inner membrane / Cell membrane / CF(0) / Hydrogen ion transport / Ion transport / Membrane / Transmembrane / Transport | ||||||
Function / homology | Function and homology information proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Priya, R. / Biukovic, G. / Gayen, S. / Vivekanandan, S. / Gruber, G. | ||||||
Citation | Journal: J.Bacteriol. / Year: 2009 Title: Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase Authors: Priya, R. / Biukovic, G. / Gayen, S. / Vivekanandan, S. / Gruber, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2khk.cif.gz | 167.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2khk.ent.gz | 139.2 KB | Display | PDB format |
PDBx/mmJSON format | 2khk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2khk_validation.pdf.gz | 427.4 KB | Display | wwPDB validaton report |
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Full document | 2khk_full_validation.pdf.gz | 481.6 KB | Display | |
Data in XML | 2khk_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 2khk_validation.cif.gz | 15.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kh/2khk ftp://data.pdbj.org/pub/pdb/validation_reports/kh/2khk | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 5785.630 Da / Num. of mol.: 1 / Fragment: residues in UNP 30-82 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ABA0 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1mM [U-99% 13C; U-99% 15N] subunit b 30-82-1, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: subunit b 30-82-1 / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Ionic strength: 0 / pH: 6.8 / Pressure: AMBIENT / Temperature: 288 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 10 / Conformers submitted total number: 10 / Representative conformer: 1 |