1GH8
SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
SOLUTION NMR
| NMR Experiment | ||||||||
|---|---|---|---|---|---|---|---|---|
| Experiment | Type | Sample Contents | Solvent | Ionic Strength | pH | Pressure | Temperature (K) | Spectrometer |
| 1 | 3D_15N-SEPARATED_NOESY | 2.0-3.0 MM N15-LABELED PROTEIN | 0.15 M NACL | 6.3 | AMBIENT | 305 | ||
| 2 | 3D_13C-SEPARATED_NOESY | 2.0-3.0 MM N15,C13-LABELED PROTEIN | 0.15 M NACL | 6.3 | AMBIENT | 305 | ||
| 3 | 2D NOESY | 2.0-3.0 MM UNLABELED PROTEIN | 0.15 M NACL | 6.3 | AMBIENT | 305 | ||
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | DRX | 500 |
| 2 | Varian | UNITYPLUS | 750 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| simulated annealing | THE STRUCTURE IS BASED ON A TOTAL OF 1962 RESTRAINTS, 1854 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 82 DIHEDRAL ANGLE RESTRAINTS, 26 HYDROGEN BOND CONSTRAINTS. | XwinNMR |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | structures with the lowest energy |
| Conformers Calculated Total Number | 200 |
| Conformers Submitted Total Number | 30 |
| Representative Model | 1 (lowest energy) |
| Additional NMR Experimental Information | |
|---|---|
| Details | THE STRUCTURE WAS DETERMINED FOR THE PROTEIN WITH N-TERMINAL HIS-TAG ATTACHED TO IT. THE HIS-TAG SEQUENCE IS MGSSHHHHHHSSGLVPRGSH. |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | collection | XwinNMR | 2.1 | BRUKER |
| 2 | processing | Gifa | 4.0 | DELSUC |
| 3 | data analysis | XEASY | 1.3.13 | WUTHRICH |
| 4 | structure solution | CNS | 0.5 | BRUNGER |
| 5 | structure solution | ARIA | 0.1 | NILGES |
| 6 | refinement | ARIA | 0.1 | NILGES |
