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. Author manuscript; available in PMC: 2017 Jan 1.
Published in final edited form as: Methods Mol Biol. 2017;1529:291–306. doi: 10.1007/978-1-4939-6637-0_15

Table 1.

K * resistance prediction (columns 1–5) and experimental characterization (columns 6–7) of wild type and mutant SaDHFR enzymes from (1).

Enzyme K* ratio rank K* positive-to-negative design ratio K* positive design (dihydrofolate) score K* negative design (compound 1) score kcat/KM Fold loss (Ki mut/Ki wt) compound 1
Sa(WT)DHFR 18 1.96 E + 06 7.16 E + 42 3.66 E + 36 6.1 ± 0.3 n/a
Sa(V31L)DHFR 1 7.11 E + 21 2.16 E + 41 3.04 E + 19 1.60 ± 0.06 58
Sa(V31l)DHFR 2 5.95 E + 21 4.87 E + 36 8.18 E+ 14 1.74 ± 0.07 36
Sa(L5l)DHFR 3 1.71 E + 15 6.06 E + 39 3.54 E+ 24 2.24 ± 0.1 4.4
Sa(L5V)DHFR 4 1.16 E + 14 4.01 E + 44 3.44 E + 30 1.8 ± 0.1 1.9