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. 2005 Nov 3;33(19):6287–6295. doi: 10.1093/nar/gki939

Table 2.

Thermodynamics of LexA binding to recA operator mutants

Inhibitor sequencea Kd(app) (nM) Kd(calc) (nM)b ΔG (kJ/mol) |ΔΔG|c (kJ/mol)
5′-CGAACATATGTTCG-3′ 993 0.17 −34.2 0
5′-CGAACATGCGTTCG-3′ 767 0.22 −34.9 0.7
5′-AGAACATGCGTTCG-3′ 391 0.42 −36.6 2.4
5′-CGAACTTGCGTTCG-3′ 337 0.49 −36.9 2.7
5′-CGAACCTGCGTTCG-3′ 299 0.56 −37.2 3.3
5′-CGAACAAGCGTTCG-3′ 268 0.62 −37.5 3.4
5′-GGAACATGCGTTCG-3′ 166 1.0 −38.6 4.4
5′-CGAATATGCGTTCG-3′(wt) 40.3 4.6 −42.2 8.0
5′-CAAACATGCGTTCG-3′ 36.3 5.2 −42.4 8.2
5′-CGAATGTGCGTTCG-3′ 30.4 6.4 −42.9 8.7
5′-CGAATACGCGTTCG-3′ 25.6 7.8 −43.4 9.1
5′-AGAATATGCGTTCG-3′ 19.0 11.4 −44.0 9.8
5′-CGAATTTGCGTTCG-3′ 18.9 11.5 −44.1 9.9
5′-CGAATAAGCGTTCG-3′ 14.2 17.1 −44.8 10.6
5′-CGAATCTGCGTTCG-3′ 12.8 20.0 −45.0 10.8
5′-GGAATATGCGTTCG-3′ 7.7 53.0 −46.3 12.1
recA operator base substitutions that prevent LexA binding

5′-TGAATATGCGTTCG-3′ 5′-CTAATATGCGTTCG-3′
5′-CCAATATGCGTTCG-3′ 5′-CGTATATGCGTTCG-3′
5′-CGCATATGCGTTCG-3′ 5′-CGGATATGCGTTCG-3′
5′-CGATTATGCGTTCG-3′ 5′-CGACTATGCGTTCG-3′
5′-CGAGTATGCGTTCG-3′ 5′-CGAAGATGCGTTCG-3′
5′-CGAAAATGCGTTCG-3′ 5′-CGAATAGGCGTTCG-3′
5′-CTAACATGCGTTCG-3′ 5′-CCAACATGCGTTCG-3′
5′-CGAATATGCATTCG-3′ 5′-CGAATATGCGTTTG-3′
5′-CAAACATGCATTCG-3′ 5′-CAAACATGCGTTTG-3′

aBases in boldface are changes relative to the wild-type recA operator.

bKd values were determined by calculating KI from the relationship Kd(app) = Kd(recA) (1 + [I]/KI) and then multiplying the KI values by the ratio Kd(recA)/KI (wt).

cΔΔG values are given as absolute values.