1C17
A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE
SOLUTION NMR
NMR Experiment | ||||||||
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Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
1 | 3D_13C-SEPARATED_NOESY | 1 MM SUBUNIT C | 50 mM | 5.0 | AMBIENT | 300 | ||
2 | 3D_15N-SEPARATED_NOESY | 1 MM SUBUNIT C | 50 mM | 5.0 | AMBIENT | 300 | ||
3 | 3D_13C-SEPARATED_NOESY | 1 MM SUBUNIT C | 50 mM | 8.0 | AMBIENT | 300 | ||
4 | 3D_15N-SEPARATED_NOESY | 1 MM SUBUNIT C | 50 mM | 8.0 | AMBIENT | 300 |
NMR Spectrometer Information | |||
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Spectrometer | Manufacturer | Model | Field Strength |
1 | Bruker | DRX | 600 |
NMR Refinement | ||
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Method | Details | Software |
torsion angle dynamics | CNS |
NMR Ensemble Information | |
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Conformer Selection Criteria | structures with the least restraint violations |
Conformers Calculated Total Number | 20 |
Conformers Submitted Total Number | 1 |
Representative Model | 1 (fewest violations) |
Additional NMR Experimental Information | |
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Details | THE STRUCTURES OF SUBUNIT C MONOMERS WERE DETERMINED BY TRIPLE RESONANCE TECHNIQUES THE MODELS OF SUBUNIT A, THE C12 SUBCOMPLEX, AND THE AC12 SUBCOMPLEX USED DISLUFIDE CROSS-LINKS AS CONSTRAINTS IN CONJUCNTION WITH THE NMR SOLUTION STRUCTURES OF SUBUNIT C |
Computation: NMR Software | ||||
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# | Classification | Version | Software Name | Author |
1 | structure solution | CNS | 0.5 | BRUNGER |
2 | refinement | CNS | 0.5 | BRUNGER |