Structural features of residue 125 in chain A

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Electrostatic Interactions:
LYS A 100 NZ	LYS A 125 NZ	0.442	INTRA-CHAIN
LYS A 124 NZ	LYS A 125 NZ	1.635	INTRA-CHAIN
LYS A 125 NZ	LYS A 100 NZ	0.442	INTRA-CHAIN
LYS A 125 NZ	LYS A 124 NZ	1.635	INTRA-CHAIN
LYS A 125 NZ	LYS B 161 NZ	0.664	INTER-CHAIN
LYS A 125 NZ	GLU B 162 OE2	-1.623	INTER-CHAIN
LYS A 125 NZ	GLU B 171 OE2	-1.824	INTER-CHAIN
LYS B 161 NZ	LYS A 125 NZ	0.664	INTER-CHAIN
GLU B 162 OE1	LYS A 125 NZ	-1.342	INTER-CHAIN
GLU B 162 OE2	LYS A 125 NZ	-1.623	INTER-CHAIN
GLU B 171 OE1	LYS A 125 NZ	-1.502	INTER-CHAIN
GLU B 171 OE2	LYS A 125 NZ	-1.824	INTER-CHAIN

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Protrusion Index:
LYS A 125 N	0.68
LYS A 125 CA	0.50
LYS A 125 C	0.38
LYS A 125 O	0.35
LYS A 125 CB	0.57
LYS A 125 CG	0.77
LYS A 125 CD	0.75
LYS A 125 CE	1.08
LYS A 125 NZ	1.06

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Salt bridges:
ASP A 122	LYS A 125	2.695	INTRA-CHAIN
LYS A 124	LYS A 125	2.813	INTRA-CHAIN

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Van der Waal's Interactions:
ASP A 122 OD2 911	LYS A 125 NZ 933	-0.111	INTRA-CHAIN
LYS A 124 NZ 924	LYS A 125 NZ 933	-0.279	INTRA-CHAIN