TABLE 1 .

Distances of the salt bridge interactions at the chain A-chain B interface of P domain of Fab2D3/MNV1 final conformations from the MDFF simulations^a

Chain A; open conformation	Chain B; closed conformation	Cryo-EM reconstruction R (Å)	Open conformation R (Å)	Closed conformation fitted R (Å)	Closed conformation V339I mutation R (Å)
ASP313 [OD1]	ARG 238 [NH1]			3.57
ASP313 [OD2]	ARG 238 [NE]	3.14
ASP313 [OD2]	ARG 238 [NH1]	3.28
ASP313 [OD2]	ARG 238 [NH2]	3.93
GLU338 [OE1]	ARG396 [NE]			3.90
GLU338 [OE1]	ARG396 [NH1]	2.76
GLU338 [OE1]	ARG396 [NH2]	3.65		3.40
GLU338 [OE2]	ARG396 [NH1]	2.63
GLU338 [OE2]	ARG396 [NH2]	3.12			3.44
GLU338 [OE2]	ARG 437 [NH2]	2.75
ARG396 [NH1]	GLU338 [OE1]	2.85			3.92
ARG396 [NH1]	GLU338 [OE2]	3.16		3.91	3.31
ARG396 [NH2]	GLU338 [OE2]	2.58		3.57	3.57
ARG396 [NH2]	GLU338 [OE1]	3.81	2.98
ARG396 [NE]	GLU338 [OE2]			3.49

^aThe structures are identified by the conformation of the P domain, A, B, and V339I mutation. Empty cells indicate the lack of interactions.