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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