TABLE 1.

Fluorescence anisotropy data

AmrZ protein	algD		amrZ1		amrZ2
	Avg Kd (nM) ± SDa	Fold over WTb	Avg Kd (nM) ± SDa	Fold over WTb	Avg Kd (nM) ± SDa	Fold over WTb
WT	107 ± 17	1.0	4.34 ± 0.74	1.0	59 ± 9.7	1.0
D2	143 ± 17	1.33	3.87 ± 0.76	0.89	89 ± 15	1.52
Δ5	140 ± 21	1.30	9.77 ± 1.92	2.25	134 ± 13	2.28
Δ11	170 ± 25	1.58	17.9 ± 5.70	4.12	106 ± 25	1.81
R14A	613 ± 86	5.72	3.96 ± 0.73	0.91	306 ± 28	5.21
K18A	2,300 ± 472	21.46	1,190 ± 210	274.2	306 ± 78	5.22
V20A	474 ± 97	4.42	45.4 ± 10.6	10.46	988 ± 98	16.83
R22A	1,347 ± 133	12.57	192 ± 26	44.24	875 ± 89	14.91

^aThe K_d was calculated based on the averages of data from three independent experiments. The data were graphed with SigmaPlot (a representative experiment is graphed in Fig. 3 and 4C and D) and analyzed based on a single-ligand-binding model with saturation.

^bFold over the wild type (WT) is defined as (calculated K_d of sample)/(calculated K_d of the wild type) for each binding site.