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- PDB-1bsh: SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE F... -
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Basic information
Entry | Database: PDB / ID: 1bsh | ||||||
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Title | SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX | ||||||
![]() | PROTEIN (EPSILON SUBUNIT) | ||||||
![]() | HYDROLASE / ATPSYNTHASE / F1-ATPASE / EPSILON SUBUNIT / NMR SPECTROSCOPY | ||||||
Function / homology | ![]() proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton motive force-driven ATP synthesis / proton-transporting ATP synthase complex, catalytic core F(1) / proton-transporting ATP synthase activity, rotational mechanism / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
![]() | Wilkens, S. / Capaldi, R.A. | ||||||
![]() | ![]() Title: Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex. Authors: Wilkens, S. / Capaldi, R.A. #1: ![]() Title: Structural Features of the Epsilon Subunit of the Escherichia Coli ATP Synthase Determined by NMR Spectroscopy Authors: Wilkens, S. / Dahlquist, F.W. / Mcintosh, L.P. / Donaldson, L.W. / Capaldi, R.A. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 1019.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 342.5 KB | Display | ![]() |
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Full document | ![]() | 692.6 KB | Display | |
Data in XML | ![]() | 121.8 KB | Display | |
Data in CIF | ![]() | 157.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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 | Mass: 14956.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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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 OF THE E. COLI ATPASE EPSILON SUBUNIT WAS DETERMINED USING TRIPLE-RESONANCE NMR EXPERIMENTS WITH 15N AND 13C/15N LABELED PROTEIN. |
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Sample preparation
Sample conditions | Ionic strength: 0.03 / pH: 7.4 / Pressure: 10000 Pa / Temperature: 295 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 / Details: simulated annealing and molecular dynamics | ||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 30 / Conformers submitted total number: 30 |