Structural features of residue 110 in chain B

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Electrostatic Interactions:
LYS A 18 NZ	LYS B 110 NZ	0.438	INTER-CHAIN
GLU A 25 OE2	LYS B 110 NZ	-1.085	INTER-CHAIN
GLU B 56 OE1	LYS B 110 NZ	-1.269	INTRA-CHAIN
GLU B 56 OE2	LYS B 110 NZ	-1.141	INTRA-CHAIN
GLU B 57 OE2	LYS B 110 NZ	-1.097	INTRA-CHAIN
GLU B 101 OE2	LYS B 110 NZ	-1.107	INTRA-CHAIN
GLU B 103 OE1	LYS B 110 NZ	-2.999	INTRA-CHAIN
GLU B 103 OE2	LYS B 110 NZ	-2.738	INTRA-CHAIN
GLU B 107 OE1	LYS B 110 NZ	-3.146	INTRA-CHAIN
GLU B 107 OE2	LYS B 110 NZ	-5.266	INTRA-CHAIN
LYS B 110 NZ	LYS A 18 NZ	0.438	INTER-CHAIN
LYS B 110 NZ	GLU A 25 OE2	-1.085	INTER-CHAIN
LYS B 110 NZ	GLU B 56 OE2	-1.141	INTRA-CHAIN
LYS B 110 NZ	GLU B 57 OE2	-1.097	INTRA-CHAIN
LYS B 110 NZ	GLU B 101 OE2	-1.107	INTRA-CHAIN
LYS B 110 NZ	GLU B 103 OE2	-2.738	INTRA-CHAIN
LYS B 110 NZ	GLU B 107 OE2	-5.266	INTRA-CHAIN
LYS B 110 NZ	GLU B 114 OE2	-1.395	INTRA-CHAIN
GLU B 114 OE1	LYS B 110 NZ	-1.654	INTRA-CHAIN
GLU B 114 OE2	LYS B 110 NZ	-1.395	INTRA-CHAIN

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Protrusion Index:
LYS B 110 N	0.36
LYS B 110 CA	0.59
LYS B 110 C	0.71
LYS B 110 O	0.67
LYS B 110 CB	0.74
LYS B 110 CG	0.72
LYS B 110 CD	1.02
LYS B 110 CE	1.11
LYS B 110 NZ	1.57

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Salt bridges:
GLU B 107	LYS B 110	3.007	INTRA-CHAIN

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Van der Waal's Interactions:
GLU B 103 OE2 1936	LYS B 110 NZ 1993	-0.023	INTRA-CHAIN
SER B 106 OG 1961	LYS B 110 NZ 1993	-0.126	INTRA-CHAIN
GLU B 107 OE2 1970	LYS B 110 NZ 1993	-1.057	INTRA-CHAIN