TABLE 2. The pseudo-atomic models identified residues of HPV16 predicted to interact with Fab and define the antigenic epitopes.

In the contact region, two or three L1 proteins of the capsomer interacted with each Fab. For each footprint the copy of the L1 protein that made the major contributions is designated with a blue X, and additional minor interactions were made by a second neighboring L1 (indicated by red X′). In only one case, mAb HPV.263.A2, there was a third copy of L1 involved in the conformational epitope (green X″). The H16.V5 result included here was from our previously published paper (16). The alternative mode of binding for the light chain facing out has been included as supplemental material.

L1 Protein Surface Loop			Fab
			V5*	1A	14J	263A2
BC	54	LYS			X′
	55	PRO			X′	X′
DE	135	TYR		X		X
	136	ALA		X		X
	137	ALA		X		X
	138	ASN	X	X	X	X
	139	ALA	X	X	X	X
	141	VAL	X			X′
	142	ASP	X			X′
	143	ASN	X
EF	181	GLN	X	X	X	X
	182	PRO			X	X
	184	ASP	X
FG	267	VAL	X
	269	GLN	X
	270	ASN	X	X
	273	ASP				X
	278	LYS		X		X
	280	SER	X		X	X
	282	SER	X	X	X	X
	283	THR	X			X
	284	ALA			X	X
	285	ASN	X	X	X	X
	286	LEU		X		X
	287	ALA		X
HI	348	ILE		X′	X′	X′
	354	THR			X′	X″
	358	THR	X′	X′	X′	X′
	361	LYS	X′	X′	X′	X′