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- PDB-2a7u: NMR solution structure of the E.coli F-ATPase delta subunit N-ter... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2a7u | ||||||
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Title | NMR solution structure of the E.coli F-ATPase delta subunit N-terminal domain in complex with alpha subunit N-terminal 22 residues | ||||||
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![]() | HYDROLASE / alpha helix bundle | ||||||
Function / homology | ![]() proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / photosynthetic electron transport in photosystem I / proton motive force-driven ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / photosynthetic electron transport in photosystem II / H+-transporting two-sector ATPase / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry; simulated annealing; molecular dynamics | ||||||
Model type details | minimized average | ||||||
![]() | Wilkens, S. / Borchardt, D. / Weber, J. / Senior, A.E. | ||||||
![]() | ![]() Title: Structural Characterization of the Interaction of the delta and alpha Subunits of the Escherichia coli F(1)F(0)-ATP Synthase by NMR Spectroscopy Authors: Wilkens, S. / Borchardt, D. / Weber, J. / Senior, A.E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.9 KB | Display | ![]() |
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PDB format | ![]() | 40 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 346 KB | Display | ![]() |
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Full document | ![]() | 351.3 KB | Display | |
Data in XML | ![]() | 4.7 KB | Display | |
Data in CIF | ![]() | 5.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 2563.966 Da / Num. of mol.: 1 / Fragment: N-terminal domain, (residues 1-22) / Source method: obtained synthetically Details: sequence occurs naturally in E.coli, genes atpA, papA, uncA References: UniProt: P00822, UniProt: P0ABB2*PLUS, H+-transporting two-sector ATPase |
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#2: Protein | Mass: 14676.533 Da / Num. of mol.: 1 / Fragment: N-terminal domain, (residues 2-135) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0ABA4, UniProt: P0ABA5*PLUS, H+-transporting two-sector ATPase |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 0.6 mM delta subunit N-terminal domain U-13C,15N; 0.9 mM alpha subunit N-terminal peptide; 10 mM Na,K phosphate, pH 7.2, 3mM NaN3, 0.1 mM EDTA; 93% H20, 7% D20 Solvent system: 93% H20, 7% D20 |
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Sample conditions | Ionic strength: 50 mM / pH: 7.2 / Pressure: ambient / Temperature: 295 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry; simulated annealing; molecular dynamics Software ordinal: 1 Details: rms difference of non-H atoms 1.114, for the backbone atoms 0.6174 | ||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||
NMR ensemble | Conformer selection criteria: averaged minimized structure / Conformers calculated total number: 10 / Conformers submitted total number: 1 |