Structural features of residue 233 in chain A

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Electrostatic Interactions:
LYS A 233 NZ	GLU B 170 OE2	-1.267	INTER-CHAIN
LYS A 233 NZ	LYS B 202 NZ	0.462	INTER-CHAIN
LYS A 233 NZ	GLU A 241 OE2	-1.590	INTRA-CHAIN
LYS A 233 NZ	GLU B 241 OE2	-1.137	INTER-CHAIN
LYS A 233 NZ	GLU B 340 OE2	-1.130	INTER-CHAIN
GLU A 241 OE1	LYS A 233 NZ	-1.943	INTRA-CHAIN
GLU A 241 OE2	LYS A 233 NZ	-1.590	INTRA-CHAIN
GLU B 160 OE1	LYS A 233 NZ	-1.092	INTER-CHAIN
GLU B 170 OE1	LYS A 233 NZ	-1.346	INTER-CHAIN
GLU B 170 OE2	LYS A 233 NZ	-1.267	INTER-CHAIN
LYS B 202 NZ	LYS A 233 NZ	0.462	INTER-CHAIN
GLU B 241 OE2	LYS A 233 NZ	-1.137	INTER-CHAIN
GLU B 340 OE1	LYS A 233 NZ	-1.070	INTER-CHAIN
GLU B 340 OE2	LYS A 233 NZ	-1.130	INTER-CHAIN

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Protrusion Index:
LYS A 233 N	0.03
LYS A 233 CA	0.11
LYS A 233 C	0.16
LYS A 233 O	0.18
LYS A 233 CB	0.05
LYS A 233 CG	0.15
LYS A 233 CD	0.20
LYS A 233 CE	0.21
LYS A 233 NZ	0.23

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Van der Waal's Interactions:
LYS A 233 NZ 1769	ILE A 236 CD1 1789	-0.057	INTRA-CHAIN
LYS A 233 NZ 1769	ILE A 285 CD1 2199	-0.027	INTRA-CHAIN
LYS A 233 NZ 1769	ASP B 315 OD2 5759	-0.022	INTER-CHAIN
ARG B 159 NH2 4488	LYS A 233 NZ 1769	-0.008	INTER-CHAIN
TYR B 166 OH 4548	LYS A 233 NZ 1769	-0.145	INTER-CHAIN