. 2012 Mar;86(5):2809–2816. doi: 10.1128/JVI.05549-11

Table 2.

Van der Waals contacts and hydrogen bonds formed between Fab 14G7 and GP

Peptide epitope	Fab residue	Distance (Å)
Van der Waals contacts
Lys^Q478	Tyr^H52, Thr^H55
Gly^Q480	Thr^H30, Asp^H31
Leu^Q481	Asp^H31
Ile^Q482	Asp^H31, Tyr^H32
Asn^Q484	Tyr^L53, Leu^L54 Asp^H101
Thr^Q485	Tyr^L36, His^L38, Leu^L50, Tyr^L53, Ala^L95, Ala^H99, Phe^H100, Asp^H101
Ile^Q486	Tyr^L36, Val^H33
Ala^Q487	Tyr^L36
Gly^Q488	Arg^L100
Val^Q489	Glu^H50, Tyr^H52
Ala^Q490	Leu^L98, Tyr^H59, Glu^H50
Gly^Q491	Ser^H57
Hydrogen bond contacts
Thr^Q485 O	His^L38 Nϵ2	2.98
Gly^Q488 O	Arg^L100 Nη2	2.95
Ile ^Q482 N	Asp^H31 O	2.87
Ala^Q490 N	Glu^H50 Oϵ2	2.75
Thr^Q485 Oγ1	Ala^H99 O	2.30
Thr^Q485 Oγ1	Asp^H101 Oδ1	2.83
Lys^Q478 N	Tyr^H52 Oη	3.34

H, L, and Q denote the heavy, light, and peptide chains, respectively.