. Author manuscript; available in PMC: 2023 Nov 23.

Published in final edited form as: Org Biomol Chem. 2022 Nov 23;20(45):8932–8943. doi: 10.1039/d2ob01545e

Table 3. Calculated interaction energies (ΔE_I-E, in kcal mol^-1) for different ionized forms of the inhibitor 17 in a complex with either dGMII or JBMan enzymes at the MP2//BP86 level.

Also overall interaction energies between the enzyme and inhibitor fragment [the pyrrolidine core (ΔE_ring-E) or the N-2-naphtylmethyl linker (ΔE_linker-E)] are also compiled.

dGMII	conform	ΔE_I-E	ΔE_ring-E	ΔE_linker-E
inh⁰-Asp341^-	E3/²E	-591.68	-561.01	-30.67
inh⁰-Ash341⁰	² E	-571.61	-543.95	-27.66
inh⁺-Asp341^-	² E	-795.53	-765.93	-29.61
inh⁺-Ash341⁰	² E	-742.24	-718.44	-23.80
JBMan
inh⁰-Asp268^-	E3	-604.14	-586.80	-17.34
inh⁰-Ash268⁰	² E	-536.59	-526.59	-9.50
inh⁺ -Asp268^-	² E	-789.23	-773.32	-15.91
inh⁺ -Ash268⁰	² E	-673.16	-662.44	-10.72

Table 3. Calculated interaction energies (ΔEI-E, in kcal mol-1) for different ionized forms of the inhibitor 17 in a complex with either dGMII or JBMan enzymes at the MP2//BP86 level.

Table 3. Calculated interaction energies (ΔE_I-E, in kcal mol^-1) for different ionized forms of the inhibitor 17 in a complex with either dGMII or JBMan enzymes at the MP2//BP86 level.