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Yorodumi- PDB-1bsn: SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE F... -
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-Basic information
Entry | Database: PDB / ID: 1bsn | ||||||
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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 | ||||||
Components | PROTEIN (EPSILON SUBUNIT) | ||||||
Keywords | HYDROLASE / ATPSYNTHASE / F1-ATPASE / EPSILON SUBUNIT / NMR SPECTROSCOPY | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Wilkens, S. / Capaldi, R.A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1998 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: Journal: Nat.Struct.Biol. / Year: 1995 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bsn.cif.gz | 56.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bsn.ent.gz | 42.4 KB | Display | PDB format |
PDBx/mmJSON format | 1bsn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bsn_validation.pdf.gz | 243.1 KB | Display | wwPDB validaton report |
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Full document | 1bsn_full_validation.pdf.gz | 242.9 KB | Display | |
Data in XML | 1bsn_validation.xml.gz | 4.9 KB | Display | |
Data in CIF | 1bsn_validation.cif.gz | 6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bs/1bsn ftp://data.pdbj.org/pub/pdb/validation_reports/bs/1bsn | HTTPS FTP |
-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: 14956.047 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: UNCC / Plasmid: PES2 / Gene (production host): UNCC / Production host: Escherichia coli (E. coli) / Strain (production host): K38, 594, DL39, 435 / References: UniProt: P0A6E6, EC: 3.6.1.34 |
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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. |
-Sample preparation
Sample conditions | Ionic strength: 0.03 / Label: conditions 1 / pH: 7.4 Not defined / 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 | Conformers calculated total number: 30 / Conformers submitted total number: 1 |