Peripheral-subunit binding domains from mesophilic, thermophilic, and hyperthermophilic bacteria fold by ultrafast, apparently two-state transitions
SOLUTION NMR
NMR Experiment | ||||||||
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Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
1 | DRX | 95% H2O/5% D2O, 3MM SAMPLE | 100 | 6.2 | 1.0 atm | 298.0 |
NMR Spectrometer Information | |||
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Spectrometer | Manufacturer | Model | Field Strength |
1 | Bruker | AVANCE | 800 |
NMR Refinement | ||
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Method | Details | Software |
REFINEMENT DETAILS CAN BE FOUND IN THE JRNL REFERENCE ABOVE | CNS |
NMR Ensemble Information | |
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Conformer Selection Criteria | NO VIOLATIONS > 0.25 |
Conformers Calculated Total Number | 21 |
Conformers Submitted Total Number | 20 |
Representative Model | 1 (n/a) |
Additional NMR Experimental Information | |
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Details | THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N LABELLED PROTEIN |
Computation: NMR Software | ||||
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# | Classification | Version | Software Name | Author |
1 | refinement | CNS | BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARREN | |
2 | structure solution | ANSIG | ||
3 | structure solution | CNS |