2K3Q
Solution structure of the n-terminal domain (TUSP1-N) of the egg case silk from Nephila antipodiana
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 2D 1H-15N HSQC | 1 mM [U-99% 13C; U-99% 15N] Tusp1-n | 90% H2O/10% D2O | 5 | 6.1 | ambient | 303 | |
| 2 | 2D 1H-13C HSQC | 1 mM [U-99% 13C; U-99% 15N] Tusp1-n | 90% H2O/10% D2O | 5 | 6.1 | ambient | 303 | |
| 3 | 3D HNCA | 1 mM [U-99% 13C; U-99% 15N] Tusp1-n | 90% H2O/10% D2O | 5 | 6.1 | ambient | 303 | |
| 4 | 3D CBCA(CO)NH | 1 mM [U-99% 13C; U-99% 15N] Tusp1-n | 90% H2O/10% D2O | 5 | 6.1 | ambient | 303 | |
| 5 | 3D CCH-TOCSY | 1 mM [U-99% 13C; U-99% 15N] Tusp1-n | 90% H2O/10% D2O | 5 | 6.1 | ambient | 303 | |
| 6 | 4D NOESY | 1 mM [U-99% 13C; U-99% 15N] Tusp1-n | 90% H2O/10% D2O | 5 | 6.1 | ambient | 303 | |
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | AVANCE | 800 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| torsion angle dynamics | Amber | |
| 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) |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | refinement | Amber | 7 | Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollm |
| 2 | processing | NMRPipe | Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax | |
| 3 | data analysis | NMRView | Johnson, One Moon Scientific | |
| 4 | refinement | CYANA | Guntert, Mumenthaler and Wuthrich | |
