2KGJ
Solution structure of parvulin domain of PpiD from E.Coli
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 2D 1H-15N HSQC | 100 mM potassium phosphate-1, 5 mM [U-15N] protein | 90% H2O/10% D2O | 0.1 | 7.0 | ambient | 298 | |
| 2 | 3D 1H-15N NOESY | 100 mM potassium phosphate-1, 5 mM [U-15N] protein | 90% H2O/10% D2O | 0.1 | 7.0 | ambient | 298 | |
| 3 | 3D 1H-15N TOCSY | 100 mM potassium phosphate-1, 5 mM [U-15N] protein | 90% H2O/10% D2O | 0.1 | 7.0 | ambient | 298 | |
| 4 | 2D 1H-1H NOESY | 100 mM potassium phosphate-1, 5 mM [U-15N] protein | 90% H2O/10% D2O | 0.1 | 7.0 | ambient | 298 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | AVANCE | 800 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| simulated annealing | ARIA | |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the lowest energy |
| Conformers Calculated Total Number | 50 |
| Conformers Submitted Total Number | 10 |
| Representative Model | 1 (lowest energy) |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | structure solution | ARIA | 2.0 | Linge, O'Donoghue and Nilges |
| 2 | chemical shift assignment | ARIA | 2.0 | Linge, O'Donoghue and Nilges |
| 3 | refinement | ARIA | 2.0 | Linge, O'Donoghue and Nilges |
