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- PDB-1aty: DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1aty | ||||||
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Title | DETERMINATION OF LOCAL PROTEIN STRUCTURE BY SPIN LABEL DIFFERENCE 2D NMR: THE REGION NEIGHBORING ASP61 OF SUBUNIT C OF THE F1FO ATP SYNTHASE | ||||||
![]() | F1F0 ATP SYNTHASE (SUBUNIT C) | ||||||
![]() | MEMBRANE PROTEIN | ||||||
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 | ||||||
![]() | Girvin, M.E. / Fillingame, R.H. | ||||||
![]() | ![]() Title: Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of subunit c of the F1F0 ATP synthase. Authors: Girvin, M.E. / Fillingame, R.H. #1: ![]() Title: Hairpin Folding of Subunit C of F1Fo ATP Synthase: 1H Distance Measurements to Nitroxide-Derivatized Aspartyl-61 Authors: Girvin, M.E. / Fillingame, R.H. #2: ![]() Title: Helical Structure and Folding of Subunit C of F1Fo ATP Synthase: 1H NMR Resonance Assignments and Noe Analysis Authors: Girvin, M.E. / Fillingame, R.H. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127.1 KB | Display | ![]() |
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PDB format | ![]() | 102.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 354 KB | Display | ![]() |
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Full document | ![]() | 473.6 KB | Display | |
Data in XML | ![]() | 38.4 KB | Display | |
Data in CIF | ![]() | 51.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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 | Mass: 8291.129 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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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 9 |