Table 2.

Mutations in Mokola virus phosphoprotein that prevent binding to Mokola virus N are compared with corresponding residues in rabies virus P and placed in the structure of rabies virus P_186-297

RABa	MOKb	Position in structure	Effect on structure
A. Mutations that likely lead to destabilisation of the structure
S196	D→G	α1	Helix destabilisation
V197	I→L, V	α1	Core packing destabilisation
F209	F→L	Loop	Core packing destabilisation
Y213	Y→C	β1	Core packing destabilisation
F215	F→Y	β1	Core packing destabilisation
M232	M→T	Loop	Core packing destabilisation
D235	D→G	α2	Helix destabilisation
R260	R→G	α4	Loss of H-bond between α4/α6
L276	L→P	α5	Helix destabilisation
N292	N→S	α6	Helix destabilisation
Y294	Y→C	α	Core packing destabilisation
B. Mutations that are located on the surface of P but not in clusters 1 and 2
K239	K→Q	α2
K256	K→E	loop
K272	K→A	α5
K282	K→N, E	α6
C. Mutations that are located on the surface of P and grouped in clusters 1 and 2
K211	K→E	Loop	Cluster 1
K212	K→E, R	Loop	Cluster 1
K214	K→E	β1	Cluster 1
L224	L→S	β2	Cluster 1
C261	C→R, S	α4	Cluster 2 (W-hole)
W265	F→L	α4	Cluster 2 (W-hole)
M287	I→T	α6	Cluster 2 (W-hole)

^aRabies virus phosphoprotein residue type and number.

^bCorresponding residue in Mokola virus phosphoprotein that, when mutated to the residue indicated, no longer binds to Mokola virus N in a yeast two-hybrid assay.²²