2FRW
Solution structure of the second SH3 domain of human adaptor protein NCK2
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 3D_13C-separated_NOESY | 50mM phosphate buffer, pH 6.8, 90% H2O, 10% D2O, 0.01% NaN3, DDT 10mM | 90% H2O/10% D2O | 6.8 | ambient | 298 | ||
| 2 | 3D_15N-separated_NOESY | 50mM phosphate buffer, pH 6.8, 90% H2O, 10% D2O, 0.01% NaN3, DDT 10mM | 90% H2O/10% D2O | 6.8 | ambient | 298 | ||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | AVANCE | 800 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| distance geometry, simulated annealing | the structures are based on a total of 974 restraints, 880 are NOE-derived distance constraints, 87 dihedral angle restraints,7 distance restraints from hydrogen bonds | CNS |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the lowest energy |
| Conformers Calculated Total Number | 100 |
| Conformers Submitted Total Number | 10 |
| Representative Model | 1 (lowest energy) |
| Additional NMR Experimental Information | |
|---|---|
| Details | The structure was determined using triple-resonance NMR spectroscopy |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | refinement | CNS | 1.1 | A.T.Brunger |
