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- PDB-1c99: ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c99 | ||||||
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Title | ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI | ||||||
![]() | PROTEOLIPID F1FO OF ATP SYNTHASE | ||||||
![]() | PROTON TRANSPORT / HYDROLASE / PROTEOLIPID F1FO / ATP SYNTHASE / PROTON TRANSLOCATION | ||||||
Function / homology | ![]() proton-transporting ATP synthase complex / proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton motive force-driven ATP synthesis / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / lipid binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Rastogi, V.K. / Girvin, M.E. | ||||||
![]() | ![]() Title: Structural changes linked to proton translocation by subunit c of the ATP synthase. Authors: Rastogi, V.K. / Girvin, M.E. #1: Journal: J.Biomol.Nmr / Year: 1999 Title: 1H, 13C, and 15N assignments and secondary structure of the high pH form of subunit c of the F1F0 ATP synthase. Authors: Rastogi, V.K. / Girvin, M.E. #2: ![]() Title: Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. Authors: Girvin, M.E. / Rastogi, V.K. / Abildgaard, F. / Markley, J.L. / Fillingame, R.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 213.5 KB | Display | ![]() |
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PDB format | ![]() | 177 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 339.5 KB | Display | ![]() |
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Full document | ![]() | 410.6 KB | Display | |
Data in XML | ![]() | 18.6 KB | Display | |
Data in CIF | ![]() | 28.5 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: 8259.064 Da / Num. of mol.: 1 / Fragment: subunit c 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 WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED SUBUNIT C |
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Sample preparation
Sample conditions | pH: 8.0 / Temperature: 300 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX600 / Manufacturer: Bruker / Model: DRX600 / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 20 / Conformers submitted total number: 9 |