2A51
Structure of the (13-51) domain of the nucleocapsid protein NCp8 from SIVlhoest
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 2D NOESY | 1mM (13-51)NCp7 | 90% H2O/10% D2O | 6.0 | ambient | 293 | ||
| 2 | 2D TOCSY | 1mM (13-51)NCp7 | 90% H2O/10% D2O | 6.0 | ambient | 293 | ||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DRX | 600 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| simulated annealing | the structures are based on a total of 474 NOE-derived distance 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 (closest to the average) |
| Additional NMR Experimental Information | |
|---|---|
| Details | This structure was determined using standard 2D homonuclear techniques |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | collection | XwinNMR | 3.0 | bruker |
| 2 | data analysis | XwinNMR | 3.0 | bruker |
| 3 | refinement | Discover | 98 | Accelrys |
