1RI9
Structure of a helically extended SH3 domain of the T cell adapter protein ADAP
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 2D NOESY | 1.8mM ADAP-hSH3 domain "[U-95% 13C; U-90% 15N]" | 90% H2O/10% D2O | 0.05 | 6.3 | ambient | 300 | |
| 2 | 2D TOCSY | 1.8mM ADAP-hSH3 domain "[U-95% 13C; U-90% 15N]" | 90% H2O/10% D2O | 0.05 | 6.3 | ambient | 300 | |
| 3 | 3D_13C-separated_NOESY | 1.8mM ADAP-hSH3 domain "[U-95% 13C; U-90% 15N]" | 90% H2O/10% D2O | 0.05 | 6.3 | ambient | 300 | |
| 4 | 3D_15N-separated_NOESY | 1.8mM ADAP-hSH3 domain "[U-95% 13C; U-90% 15N]" | 90% H2O/10% D2O | 0.05 | 6.3 | ambient | 300 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DRX | 600 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| torsion angle dynamics | the structures are based on a total of 1136 restraints, 718 are NOE-derived distance constraints, 388 dihedral angle restraints,30 distance restraints from hydrogen bonds. | XwinNMR |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | The submitted conformer models are the 20 structures with the lowest energy. |
| Conformers Calculated Total Number | 51 |
| Conformers Submitted Total Number | 20 |
| Representative Model | 1 (fewest violations,lowest energy) |
| Additional NMR Experimental Information | |
|---|---|
| Details | This structure was determined using standard 2D homonuclear and 3D heteronuclear techniques. |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | collection | XwinNMR | 2.6 | Bruker GmbH |
| 2 | data analysis | XEASY | 1.3.13 | Bartels, C., Xia, T.H., Billeter, M., Guentert, P. and Wuethrich, K. |
| 3 | structure solution | CYANA | 1.0.6 | Guentert, P. |
| 4 | refinement | CYANA | 1.0.6 | Guentert, P. |
