SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 3D_13C-separated_NOESY | G311 mutant protein | 0.1 M KPi, pH7.0, ~0.6 M GuHCl. | 0.1M | 7.0 | ambient | 275 | |
| 2 | 3D_15N-separated_NOESY | G311 mutant protein | 0.1 M KPi, pH7.0, ~0.6 M GuHCl. | 0.1M | 7.0 | ambient | 275 | |
| 3 | 3D HNCACB, 3D HNCO, 3DCBCACONH, 3D HBHA(CBCACO)NH, 3D (H)C(CO)NH-TOCSY, H(CCO)NH-TOCSY, 2D TOCSY, 2D-CBHD, 2DCBHE, 2D TOCSY | G311 mutant protein | 0.1 M KPi, pH7.0, ~0.6 M GuHCl. | 0.1M | 7.0 | ambient | 275 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DRX | 600 |
| 2 | Bruker | DRX | 500 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| CNS 1.1 | simulated annealing | XwinNMR |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | The submitted conformer models are those with the fewest number of constraint violations. |
| Conformers Calculated Total Number | 50 |
| Conformers Submitted Total Number | 20 |
| Representative Model | 1 (lowest energy) |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | collection | XwinNMR | 2.5 | Bruker Co. |
| 2 | processing | NMRPipe | Frank Delaglio Stephan Grzeiek, Guang Zhu, Geerten W. Vuister, John Pfeifer, and Ad Bax | |
| 3 | data analysis | Sparky | 3 | T. D. Goddard and D. G. Kneller |
| 4 | structure solution | CNS | 1.1 | A.T.Brunger, P.D.Adams, G.M.Clore, W.L.Delano, P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang, J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren |
| 5 | refinement | CNS | 1.1 | A.T.Brunger, P.D.Adams, G.M.Clore, W.L.Delano, P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang, J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren |
