1WQU
Solution structure of the human FES SH2 domain
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 3D_13C-separated_NOESY | 1.2mM uniformly 13C and 15N labeled protein; 20mM Tris-HCl buffer; 100mM NaCl; 1mM dithiothreitol; 0.02% NaN3 | 90% H2O/10% D2O | 7.0 | AMBIENT | 298 | ||
| 2 | 3D_15N-separated_NOESY | 1.2mM uniformly 13C and 15N labeled protein; 20mM Tris-HCl buffer; 100mM NaCl; 1mM dithiothreitol; 0.02% NaN3 | 90% H2O/10% D2O | 7.0 | AMBIENT | 298 | ||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DRX | 600 |
| 2 | Bruker | AVANCE | 800 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| automated NOESY assignment, torsion angle dynamics, energy minimization | NMRPipe | |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the least restraint violations |
| Conformers Calculated Total Number | 100 |
| Conformers Submitted Total Number | 20 |
| Representative Model | 1 (closest to the average) |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | processing | NMRPipe | 2.1 | Delaglio, F. |
| 2 | data analysis | NMRView | 5.0.4 | Johnson, B. |
| 3 | structure solution | CYANA | 2.0.32 | Guntert, P. |
| 4 | refinement | OPALp | 1.3 | Koradi, R., Billeter, M., Guntert, P. |
