| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 51990 |
2024-07-30 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of the D10N,P146A variant of beta-phosphoglucomutase (trans K145-A146 peptide bond) in a Mg-bound complex with beta-glucose 1,6-bisphosphate |
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase
|
Adam J Flinders, Anamaria Buzioanu, F A Cruz-Navarrete, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Patrick J Baker |
| 51986 |
2024-07-30 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of the D10N,P146A variant of beta-phosphoglucomutase (trans K145-A146 peptide bond) in a Mg-bound complex with fructose 1,6-bisphosphate and an additional Mg ion bound in the active site |
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase
|
Adam J Flinders, Anamaria Buzoianu, F A Cruz-Navarrete, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Patrick J Baker |
| 51987 |
2024-07-30 |
Chemical Shifts: 1 set
|
1H and 15N backbone resonance assignments of the D10N,P146A variant of beta-phosphoglucomutase (trans K145-A146 peptide bond) in a Mg-bound complex with fructose 1,6-bisphosphate |
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase
|
Adam J Flinders, Anamaria Buzoianu, F A Cruz-Navarrete, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Patrick J Baker |
| 51988 |
2024-07-30 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of the D10N,P146A variant of beta-phosphoglucomutase (trans K145-A146 peptide bond) in a Mg-bound complex with beta-glucose 1,6-bisphosphate and an additional Mg ion bound in the active site |
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase
|
Adam J Flinders, Anamaria Buzoianu, F A Cruz-Navarrete, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Patrick J Baker |
| 51989 |
2024-07-30 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of the D10N,P146A variant of beta-phosphoglucomutase (cis K145-A146 peptide bond) in a Mg-bound complex with beta-glucose 1,6-bisphosphate |
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase
|
Adam J Flinders, Anamaria Buzioanu, F A Cruz-Navarrete, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Patrick J Baker |
| 51985 |
2024-07-30 |
Chemical Shifts: 1 set
|
1H, 15N and 13C backbone resonance assignments of the D10N variant of beta-phosphoglucomutase (cis K145-P146 peptide bond) in a Mg-bound complex with fructose 1,6-bisphosphate |
Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase
|
Adam J Flinders, Anamaria Buzoianu, F A Cruz-Navarrete, Jonathan P Waltho, Matthew J Cliff, Nicola J Baxter, Patrick J Baker |
| 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 |
| 27920 |
2019-08-14 |
Chemical Shifts: 1 set
|
1H, 15N, 13C backbone resonance assignments of the P146A variant of beta-phosphoglucomutase |
1H, 15N and 13C backbone resonance assignments of the P146A variant of beta-phosphoglucomutase from Lactococcus lactis in its substrate-free form
|
Andrea M Hounslow, F Aaron Cruz-Navarrete, Henry P Wood, Jonathan P Waltho, Nicola J Baxter |
