Structural features of residue 348 in chain B

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Electrostatic Interactions:
LYS A 37 NZ	LYS B 348 NZ	0.456	INTER-CHAIN
GLU A 59 OE2	LYS B 348 NZ	-1.101	INTER-CHAIN
GLU B 190 OE1	LYS B 348 NZ	-1.506	INTRA-CHAIN
GLU B 190 OE2	LYS B 348 NZ	-1.359	INTRA-CHAIN
LYS B 300 NZ	LYS B 348 NZ	0.481	INTRA-CHAIN
LYS B 348 NZ	LYS A 37 NZ	0.456	INTER-CHAIN
LYS B 348 NZ	GLU A 59 OE2	-1.101	INTER-CHAIN
LYS B 348 NZ	GLU B 190 OE2	-1.359	INTRA-CHAIN
LYS B 348 NZ	LYS B 300 NZ	0.481	INTRA-CHAIN

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Protrusion Index:
LYS B 348 N	0.06
LYS B 348 CA	0.04
LYS B 348 C	0.05
LYS B 348 O	0.09
LYS B 348 CB	-0.02
LYS B 348 CG	-0.05
LYS B 348 CD	-0.04
LYS B 348 CE	0.05
LYS B 348 NZ	0.09

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Salt bridges:
ASP B 347	LYS B 348	2.247	INTRA-CHAIN

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Van der Waal's Interactions:
ASN A 39 ND2 284	LYS B 348 NZ 6777	-0.073	INTER-CHAIN
SER A 40 OG 290	LYS B 348 NZ 6777	-0.012	INTER-CHAIN
THR A 42 CG2 305	LYS B 348 NZ 6777	-0.060	INTER-CHAIN
GLY A 44 O 316	LYS B 348 NZ 6777	-0.017	INTER-CHAIN
GLY A 47 O 338	LYS B 348 NZ 6777	-0.010	INTER-CHAIN
ASP B 156 OD2 5219	LYS B 348 NZ 6777	-0.010	INTRA-CHAIN
LYS B 348 NZ 6777	SER B 433 OG 7465	-0.238	INTRA-CHAIN