Structural features of residue 110 in chain A

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Electrostatic Interactions:
GLU A 43 OE1	LYS A 110 NZ	-1.136	INTRA-CHAIN
GLU A 43 OE2	LYS A 110 NZ	-1.337	INTRA-CHAIN
LYS A 49 NZ	LYS A 110 NZ	0.681	INTRA-CHAIN
GLU A 52 OE1	LYS A 110 NZ	-1.736	INTRA-CHAIN
GLU A 52 OE2	LYS A 110 NZ	-1.554	INTRA-CHAIN
LYS A 53 NZ	LYS A 110 NZ	0.499	INTRA-CHAIN
GLU A 57 OE1	LYS A 110 NZ	-1.083	INTRA-CHAIN
LYS A 110 NZ	GLU A 43 OE2	-1.337	INTRA-CHAIN
LYS A 110 NZ	LYS A 49 NZ	0.681	INTRA-CHAIN
LYS A 110 NZ	GLU A 52 OE2	-1.554	INTRA-CHAIN
LYS A 110 NZ	LYS A 53 NZ	0.499	INTRA-CHAIN
LYS A 110 NZ	GLU B 122 OE2	-1.088	INTER-CHAIN
LYS A 110 NZ	LYS B 133 NZ	0.705	INTER-CHAIN
GLU B 122 OE1	LYS A 110 NZ	-1.075	INTER-CHAIN
GLU B 122 OE2	LYS A 110 NZ	-1.088	INTER-CHAIN
LYS B 133 NZ	LYS A 110 NZ	0.705	INTER-CHAIN

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Protrusion Index:
LYS A 110 N	0.16
LYS A 110 CA	0.20
LYS A 110 C	0.23
LYS A 110 O	0.21
LYS A 110 CB	0.52
LYS A 110 CG	0.51
LYS A 110 CD	0.86
LYS A 110 CE	0.97
LYS A 110 NZ	1.51

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Salt bridges:
ASP A 40	LYS A 110	2.942	INTRA-CHAIN

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Van der Waal's Interactions:
LYS A 110 NZ 820	TRP B 140 CH2 2057	-0.063	INTER-CHAIN