1BDD
STAPHYLOCOCCUS AUREUS PROTEIN A, IMMUNOGLOBULIN-BINDING B DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | DQF-COSY | 5.0 | 303 | |||||
| 2 | HOHAHA | 5.0 | 303 | |||||
| 3 | NOESY | 5.0 | 303 | |||||
| 4 | PE-COSY; 1H-15N HSQC | 5.0 | 303 | |||||
| 5 | DOUBLE-DEPT | 5.0 | 303 | |||||
| 6 | 2D-HMQC-HOHAHA | 5.0 | 303 | |||||
| 7 | 2D-HMQC-NOESY | 5.0 | 303 | |||||
| 8 | HMQC-J | 5.0 | 303 | |||||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | JEOL | JNM-GSX | 500 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD | X-PLOR | |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | AT FIRST, THE DEPOSITORS CARRIED OUT THE DISTANCE GEOMETRY CALCULATION BY STARTING FROM 55 INITIAL STRUCTURES. THIS CALCULATION RESULTED IN 41 SOLUTIONS, WHICH HAD CORRECT POLYPEPTIDE FOLDS EXCLUDING 14 MIRROR-IMAGE SUBSTRUCTURES. NEXT, THE DYNAMICAL SIMULATED ANNEALING CALCULATIONS WERE PERFORMED BY USING THESE 41 SUBSTRUCTURES. THE DISTANCE AND TORSION ANGLE VIOLATIONS OF THE 41 SOLUTIONS OBTAINED BY THE DYNAMICAL SIMULATED ANNEALING CALCULATIONS WERE SMALLER THAN 0.6 ANGSTROMS AND 27 DEGREES, RESPECTIVELY. THE DEPOSITORS SELECTED 10 SOLUTIONS THAT HAD THE DISTANCE AND TORSION ANGLE VIOLATIONS OF SMALLER THAN 0.5 ANGSTROMS AND 10 DEGREES, RESPECTIVELY. |
| Conformers Calculated Total Number | 55 |
| Conformers Submitted Total Number | 1 |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | refinement | X-PLOR | BRUNGER | |
| 2 | structure solution | EMBOSS | ||
| 3 | structure solution | X-PLOR | ||
