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Yorodumi- PDB-2ov6: The NMR structure of subunit F of the Methanogenic A1Ao ATP synth... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ov6 | ||||||
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Title | The NMR structure of subunit F of the Methanogenic A1Ao ATP synthase and its interaction with the nucleotide-binding subunit B | ||||||
Components | V-type ATP synthase subunit F | ||||||
Keywords | HYDROLASE / F subunit / A1Ao ATP synthase | ||||||
Function / homology | Function and homology information proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ATP binding Similarity search - Function | ||||||
Biological species | Methanosarcina mazei (archaea) | ||||||
Method | SOLUTION NMR / Distance constraints, Simulated annealing, Molecular dynamics, Torsion angle dynamics | ||||||
Authors | Gayen, S. / Subramanian, V. / Biukovic, G. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: NMR solution structure of subunit F of the methanogenic A1AO adenosine triphosphate synthase and its interaction with the nucleotide-binding subunit B. Authors: Gayen, S. / Vivekanandan, S. / Biukovic, G. / Gruber, G. / Yoon, H.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ov6.cif.gz | 307.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ov6.ent.gz | 253.8 KB | Display | PDB format |
PDBx/mmJSON format | 2ov6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ov6_validation.pdf.gz | 461.1 KB | Display | wwPDB validaton report |
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Full document | 2ov6_full_validation.pdf.gz | 553.8 KB | Display | |
Data in XML | 2ov6_validation.xml.gz | 26.8 KB | Display | |
Data in CIF | 2ov6_validation.cif.gz | 34.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ov/2ov6 ftp://data.pdbj.org/pub/pdb/validation_reports/ov/2ov6 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10777.303 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei (archaea) / Strain: Go1 / Plasmid: pET9d1-His3 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 References: UniProt: Q60185, H+-transporting two-sector 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 triple-resonance NMR spectroscopy |
-Sample preparation
Details | Contents: 0.5mM F subunit uniformly labeled 15N; 15N, 13C; 25mM phosphate buffer pH 6.5; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.5 / 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: Distance constraints, Simulated annealing, Molecular dynamics, Torsion angle dynamics Software ordinal: 1 Details: Total NMR constraints 863, Torsional angle restraints 184, Hydrogen bond restraints 32 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 10 |