SOLUTION NMR
| NMR Spectrometer Information | |||
|---|---|---|---|
| Spectrometer | Manufacturer | Model | Field Strength |
| 1 | Bruker | AMX | 500 |
| 2 | Bruker | AVANCE | 600 |
| 3 | Bruker | AVANCE | 800 |
| NMR Refinement | ||
|---|---|---|
| Method | Details | Software |
| REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. STRUCTURE WAS GENERATED FROM EXPERIMENTS CARRIED OUT AT 303-308K WITH PH 7.5-8.0 | CNS | |
| NMR Ensemble Information | |
|---|---|
| Conformer Selection Criteria | LEAST NOE VIOLATION ENERGY |
| Conformers Calculated Total Number | 35 |
| Conformers Submitted Total Number | 16 |
| Representative Model | 1 (n/a) |
| Additional NMR Experimental Information | |
|---|---|
| Details | THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. DOUBLE-HALF FILTERED 2D NOESY AND HALF-FILTERED HSQC-NOESY ON A MIXED LABELED/UNLABELED SAMPLE WERE USED TO DISTINGUISH INTRA- AND INTER-MONOMER NOES. RESIDUES 102-109 AND 171 ARE INSUFFICIENTLY CONSTRAINED BY THE INPUT DATA AND SHOULD BE CONSIDERED OF UNKNOWN STRUCTURE. THUS THE STRUCTURE IS ONLY DEFINED FOR RESIDUES 110 - 170. |
| Computation: NMR Software | ||||
|---|---|---|---|---|
| # | Classification | Version | Software Name | Author |
| 1 | refinement | CNS | 0.9 | BRUNGER ET AL |
| 2 | structure solution | Azara | ||
| 3 | structure solution | ANSIG | ||
| 4 | structure solution | CNS | ||
| 5 | structure solution | ARIA | ||
