Structural features of residue 248 in chain B

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Electrostatic Interactions:
GLU A 325 OE1	LYS B 248 NZ	-1.068	INTER-CHAIN
GLU A 325 OE2	LYS B 248 NZ	-1.068	INTER-CHAIN
LYS B 238 NZ	LYS B 248 NZ	0.430	INTRA-CHAIN
GLU B 240 OE1	LYS B 248 NZ	-2.448	INTRA-CHAIN
GLU B 240 OE2	LYS B 248 NZ	-2.925	INTRA-CHAIN
GLU B 243 OE1	LYS B 248 NZ	-1.642	INTRA-CHAIN
GLU B 243 OE2	LYS B 248 NZ	-1.359	INTRA-CHAIN
LYS B 248 NZ	LYS B 238 NZ	0.430	INTRA-CHAIN
LYS B 248 NZ	GLU B 240 OE2	-2.925	INTRA-CHAIN
LYS B 248 NZ	GLU B 243 OE2	-1.359	INTRA-CHAIN
LYS B 248 NZ	LYS B 250 NZ	0.493	INTRA-CHAIN
LYS B 248 NZ	GLU B 251 OE2	-2.688	INTRA-CHAIN
LYS B 248 NZ	GLU A 325 OE2	-1.068	INTER-CHAIN
LYS B 250 NZ	LYS B 248 NZ	0.493	INTRA-CHAIN
GLU B 251 OE1	LYS B 248 NZ	-3.297	INTRA-CHAIN
GLU B 251 OE2	LYS B 248 NZ	-2.688	INTRA-CHAIN

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Protrusion Index:
LYS B 248 N	0.54
LYS B 248 CA	0.51
LYS B 248 C	0.59
LYS B 248 O	0.67
LYS B 248 CB	0.40
LYS B 248 CG	0.47
LYS B 248 CD	0.72
LYS B 248 CE	0.80
LYS B 248 NZ	0.89

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Salt bridges:
ASP B 244	LYS B 248	2.781	INTRA-CHAIN

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Van der Waal's Interactions:
GLU B 240 OE2 4107	LYS B 248 NZ 4167	-0.034	INTRA-CHAIN
ASP B 244 OD2 4138	LYS B 248 NZ 4167	-0.603	INTRA-CHAIN
ALA B 247 CB 4158	LYS B 248 NZ 4167	-0.072	INTRA-CHAIN
LYS B 248 NZ 4167	GLU B 251 OE2 4193	-0.023	INTRA-CHAIN