TABLE 4.

Experimental and computational results of inhibition study with compound 6142342

Enzyme	Experimental % inhibition with 40 μM inhibitora	Computational result
		Binding energy (kcal/mol)b	Inhibitor-enzyme distance (Å)c
			O-1–Zn1	O-1–Zn2	O-3–Zn1	O-2–K224 N-ζ	N-3–K150a N-ζ
IMP-1-V67Ad	33 ± 10	−10.7 ± 0.5	2.3	1.9	2.1	2.9	3.4
IMP-1 (V67)	85 ± 5	−11.8 ± 0.8	2.1	1.9	2.0	3.1	3.2
IMP-1-V67I	58 ± 11	−11.4 ± 0.4	2.3	1.8	1.9	2.7	3.6
IMP-10 (F67)	49 ± 5	−11.0 ± 0.6	2.1	1.9	2.2	3.0	3.3

^aPercent inhibition values are the averages for three experiments ± standard deviations.

^bThe binding energies reported are the average binding energies of the highest-ranked clusters of docking conformations ± standard deviations.

^cThe distances reported are distances between inhibitor atoms and enzyme atoms found in the highest-ranked docking conformation (see Fig. 4B). O-1 is the nitro group oxygen coordinating the two Zn(II) ions, O-2 is the nitro group oxygen hydrogen bonding with K224, O-3 is the deprotonated phenol oxygen coordinating Zn1, and N-3 is the benzothiazole nitrogen that interacts electrostatically with K150a.

^dAmino acid identities are shown in bold.