Table 2.
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.