Table 3.

Conformational preferences of Asn and glyco-Asn residues at the (experimentally introduced) glycosylation sites in heptapeptide sequences, depicted as percent of conformers in α-helix, β-sheet, or turn/α_L conformations (see SI Text for definitions)

	Pseudo-WT				Glycosylated pseudo-WT
	α-Helix	β-Sheet	Turn/αL		α-Helix	β-Sheet	Turn/αL
N5	0.87 ± 0.03	0.06 ± 0.01	0.07 ± 0.02		0.66 ± 0.05	0.19 ± 0.03	0.14 ± 0.04
A13N	0.39 ± 0.03	0.06 ± 0.02	0.55 ± 0.01		0.34 ± 0.08	0.43 ± 0.07	0.19 ± 0.08
K20N	0.84 ± 0.05	0.07 ± 0.02	0.09 ± 0.05		0.59 ± 0.07	0.20 ± 0.04	0.19 ± 0.04
V27N	0.69 ± 0.04	0.07 ± 0.02	0.24 ± 0.02		0.43 ± 0.05	0.32 ± 0.03	0.23 ± 0.06
N60	0.88 ± 0.02	0.05 ± 0.01	0.07 ± 0.02		0.90 ± 0.02	0.06 ± 0.01	0.03 ± 0.02
K73N	0.81 ± 0.03	0.11 ± 0.03	0.08 ± 0.05		0.34 ± 0.04	0.64 ± 0.04	0.00 ± 0.00
A78N	0.90 ± 0.04	0.04 ± 0.01	0.06 ± 0.03		0.69 ± 0.05	0.25 ± 0.03	0.05 ± 0.02

Structures with dihedral angles not in one of these categories comprised < 0–4% of the conformational ensembles. The data were obtained from a backbone dihedral angle analysis of structures generated using REMD simulations of Im7 heptapeptide subsequences.