1IYT
Solution structure of the Alzheimer's disease amyloid beta-peptide (1-42)
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 2D NOESY | 2mM amyloid beta-peptide (TFA pretreated); 20% H2O, 80% hexafluoroisopropanol-d2 | 20% H2O, 80% hexafluoroisopropanol-d2 (v/v) | ambient | 300 | |||
| 2 | 2D NOESY | 2.5mM amyloid beta-peptide (TFA pretreated); 20% D2O, 80% hexafluoroisopropanol-d2 | 20% D2O, 80% hexafluoroisopropanol-d2 (v/v) | ambient | 300 | |||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DRX | 600 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| torsion angle dynamics and restrained minimization | the structures are based on a total of 413 NOE-derived, non-redundant restraints (130 intra-residue, 283 inter-residue) | XwinNMR |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the least restraint violations |
| Conformers Calculated Total Number | 20 |
| Conformers Submitted Total Number | 10 |
| Additional NMR Experimental Information | |
|---|---|
| Details | The structure was determined using standard 2D homonuclear techniques |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | collection | XwinNMR | 1.3 | |
| 2 | processing | NMRPipe | 1.5 | Delaglio |
| 3 | data analysis | NMRView | 4.0.3 | Johnson |
| 4 | structure solution | DYANA | 1.5 | Guentert |
| 5 | refinement | Amber | 6 | Case, Pearlman et al. |
