| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 28095 |
2020-09-03 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of wild-type substrate-free beta-phosphoglucomutase from Lactococcus lactis with a cis K145-P146 peptide bond (conformer A) |
Allomorphy as a mechanism of post-translational control of enzyme activity
|
Andrea M Hounslow, Angus J Robertson, Clare R Trevitt, F Aaron Cruz-Navarrete, Henry P Wood, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Samuel R Dix |
| 28096 |
2020-09-03 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of wild-type substrate-free beta-phosphoglucomutase from Lactococcus lactis with a trans K145-P146 peptide bond (conformer B) |
Allomorphy as a mechanism of post-translational control of enzyme activity
|
Andrea M Hounslow, Angus J Robertson, Clare R Trevitt, F Aaron Cruz-Navarrete, Henry P Wood, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Samuel R Dix |
| 28097 |
2020-09-03 |
Chemical Shifts: 1 set
|
1H, 15N, 13C backbone resonance assignments of the P146A variant of beta-phosphoglucomutase in a transition state analogue complex with glucose 6-phosphate and trifluoromagnesate (MgF3-) |
Allomorphy as a mechanism of post-translational control of enzyme activity
|
Andrea M Hounslow, Angus J Robertson, Clare R Trevitt, F Aaron Cruz-Navarrete, Henry P Wood, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Samuel R Dix |
