Table 1.

Summary of the crystal structures of EfFIC determined in this study

EfFIC	Space group	Cell parameters a, b, c (Å)	Ligand	Resolution	PDB
WT	P41212	65.13, 65.13, 248.06	PO42−	2.29	6ER8
WT	I222	121.54, 131.00, 136.94	—	2.40	5NV5
WT	P41212	64.98, 64.98, 246.24	AMP-Ca2+	2.35	6EP0
WT	P43212	125.35, 125.35, 362.8	ATPγSa-Ca2+	2.15	6EP2
WT	P43212	87.84, 87.84, 364.94	ATPγSa	1.93	6EP5
H111A	P21221	76.67, 77.11, 103.15	—	2.60	5NWF
H111A	I222	121.93, 131.16, 136.71	SO42−	2.20	5NVQ

All crystals have cell angles of α, β, and γ = 90°. Crystallographic statistics are given in Supplementary Table 1

EfFIC FIC protein from Enterococcus faecalis, WT wild type

^aOnly the ADP moiety is visible