Table 1.

Equilibrium binding affinities for VcGluP wildtype and binding site mutants

Variant	Glu Kd (µM)	FC	n	Gln Kd (mM)	FC	n	Pyroglu Kd (mM)	FC	n
WT	0.065 ± 0.031	-	5	0.011 ± 0.002	-	5	0.050 ± 0.016	-	10
Y45A	13.88 ± 1.576	213	5	5.135 ± 0.864	466	6	2.000 ± 0.094	40	5
S75A	0.915 ± 0.126	14	5	0.073 ± 0.028	6.5	7	0.499 ± 0.050	10	5
Q93A	64.39 ± 13.74	990	10	ND	ND	5	18.62 ± 4.566	372	5
E125A	0.083 ± 0.023	1.3	5	0.025 ± 0.008	2.3	9	0.147 ± 0.010	2.9	6
Y200A	0.228 ± 0.088	3.5	6	0.022 ± 0.008	2	8	0.104 ± 0.022	2.1	3
M201A	0.139 ± 0.032	2.1	4	0.040 ± 0.009	3.6	9	0.302 ± 0.010	6	4

FC is the fold change in Kd compared to wildtype, n indicates the number of technical replicates performed, and error indicated is the standard deviation. Values are color coded to indicate the extent of Kd change for a mutant compared to wildtype (red being most deleterious, blue being a mild effect, and orange being middling).