. Author manuscript; available in PMC: 2015 Jul 8.

Published in final edited form as: Structure. 2014 Jun 12;22(7):974–984. doi: 10.1016/j.str.2014.05.001

Table 1.

Glycoforms observed in SOSIP.664 trimers.

Glycosylation sites^*	KNH1144	BG505 (293S)	BG505 (293F)
N88	Man₅	Man₅	Man₅ & Complex
N156	Man_8,9	-	-
N188/190 & N190c	Man₅^a	Man₅^a,^b	Complex
N197	Man_5–9	Man_5–9	Man_5–9
N234	Man_6–9^a	Man_8,9	Man_8,9
N241	Man_6–9^a	-	-
N262	Man_8,9	Man_8,9	Man_8,9
N276	Man_7,8	Man_5–8	Man_5–8
N295	-	Man₈^b	Man₈^a
N301	Man_7–8	Man₈^b	Man₈^a
N332 & N339	Man_8,9^a	-	-
N356 & N363	Man₇^a	-	-
N448	Man_8,9	Man_8,9	Man_8,9
N463/462	Man₅	Man₅	Complex
N611 & N616/618	Man₅^a,^b	Man₅^b	Complex
N625	Man₅^b	Man₅^b	Man₅^b
N637	Man_5,6	Man_5–8	Man_5–8

N-linked glycosylation site(s) where some peptides contained more than one glycan (denoted by +); KNH1144/BG505 position

Data were obtained from peptides bearing two glycans; therefore, only the average for the total combined glycosylation is reported.

Glycan occupancy was observed at less than 90% as assessed by the relative abundance of non-glycosylated and deglycosylated signal after PNGaseF digestion (see Tables S1 and S2).