1Q9P
Solution structure of the mature HIV-1 protease monomer
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 3D_13C-separated_NOESY | 0.5mM HIV-1 protease u-15N, 13C, 20mM phosphate buffer, 95% H2O, 5%D2O | 95% H2O/5% D2O | 20mM | 5.8 | ambient | 293 | |
| 2 | 3D_15N-separated_NOESY | 0.5mM HIV-1 protease u-15N, 13C, 20mM phosphate buffer, 95% H2O, 5%D2O | 95% H2O/5% D2O | 20mM | 5.8 | ambient | 293 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DMX | 500 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| simulated annealing | The structures are based on a total of 862 restraints, 752 are NOE-derived distance constraints, 47 dihedral angle restraints,30 distance restraints from hydrogen bonds, 63 dipolar coupling constraints. | XwinNMR |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the lowest energy |
| Conformers Calculated Total Number | 100 |
| Conformers Submitted Total Number | 20 |
| Representative Model | 1 (lowest energy) |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | collection | XwinNMR | 2.6 | Bruker |
| 2 | data analysis | NMRPipe | D.Garrett | |
| 3 | structure solution | X-PLOR | 1.0.6 | C.D.Schwieters, J.J.Kuszewski, N.Tjandra, and G.M.Clore |
| 4 | refinement | X-PLOR | 1.0.6 | C.D.Schwieters, J.J.Kuszewski, N.Tjandra, and G.M.Clore |
