TABLE 6.

Comparison between experimentally determined and calculated percentages of naphthol isomers produced by wild-type ToMO and ToMO mutant proteins

ToMO variant or mutation	Binding energya (kcal/mol) for:			Calculated %b of:			Experimentally determined %c of:
	EN‡α	EN‡β1	EN‡β2	α-N	β-N produced by EN‡β1	β-N produced by EN‡β2	α-N	β-N
Wild type	−38.66	−31.08	−35.49	99.5	0.0	0.5	87	13
F176I	−36.32	−32.88	−34.10	97.4	0.3	2.3	57	43
F176L	−37.29	−28.65	−34.17	99.5	0.0	0.5	57	43
I100A	−38.58	−33.37	−36.10	98.5	0.02	1.5	53	47
I100V	−38.02	−30.30	−35.91	97.3	0.0	2.7	81	19

^aTotal binding energy for the complex ToMO variant-naphthalene analogue of CCI 10 (EN^‡_α), ToMO variant-naphthalene analogue of CCI 12 (EN^‡_β1), or ToMO variant-naphthalene analogue of CCI 13 (EN^‡_β2).

^bα- and β-N, α- and β-naphthol.

^cError, <1%.