Table 1.

Main hydrogen-bonding interactions involved in antibodies binding with the RBD domain of SARS-CoV-2.

Hydrogen Bonda	Occupancyb
	WT	H:V106R	H:V106 R/H:P107Y
O@G447···O-H@H:Y27	86.14	87.13	93.07
O@H:S31⋯N-H@Y449	70.30	66.34	85.15
OD1@N450···NE2-HE2@H:H54	67.33	44.55	69.31
O@H:S30···ND2-HD21@N450	64.36	59.41	70.30
OE2@E484···NH1-HH12@H:R112	61.39	55.45	94.06
OE2@E484···NH2-HH22@H:R112	54.46	31.68	33.66
OE1@E484···NH2-HH22@H:R112	27.72	30.69	38.61
OE1@E484···NH1-HH12@H:R112	18.81	41.58
O@E484···ND2-HD22@L:N33	43.56	53.47	8.91
O-H@ L:Y34⋯N-H@E484	27.72	16.83	20.79
OD1@N450···NE2-HE2@H:Y53	21.78		11.88
OE2@E484···NH2-HH21@H:R106		44.55	4.95
OE1@E484···NH2-HH21@H:R106		53.47	86.14
OE1@E484···NE-HE@H:R106		38.61	13.86
OE2@E484···NE-HE@H:R106		37.62	65.35
O@T470···O-H@H:Y107			88.12

Residues of the antibody are shown in bold.

^aThe hydrogen bonds are determined by an acceptor···donor distance of <3.5 Å and an acceptor···H−donor angle of >120°.

^bOccupancy is defined as the percentage of simulation time that a specific hydrogen bond exists.