Structural features of residue 125 in chain B

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Electrostatic Interactions:
LYS A 161 NZ	LYS B 125 NZ	0.497	INTER-CHAIN
GLU A 162 OE2	LYS B 125 NZ	-1.101	INTER-CHAIN
GLU A 171 OE1	LYS B 125 NZ	-1.439	INTER-CHAIN
GLU A 171 OE2	LYS B 125 NZ	-1.795	INTER-CHAIN
LYS B 100 NZ	LYS B 125 NZ	0.483	INTRA-CHAIN
LYS B 105 NZ	LYS B 125 NZ	0.450	INTRA-CHAIN
LYS B 124 NZ	LYS B 125 NZ	1.449	INTRA-CHAIN
LYS B 125 NZ	LYS B 100 NZ	0.483	INTRA-CHAIN
LYS B 125 NZ	LYS B 105 NZ	0.450	INTRA-CHAIN
LYS B 125 NZ	LYS B 124 NZ	1.449	INTRA-CHAIN
LYS B 125 NZ	LYS A 161 NZ	0.497	INTER-CHAIN
LYS B 125 NZ	GLU A 162 OE2	-1.101	INTER-CHAIN
LYS B 125 NZ	GLU A 171 OE2	-1.795	INTER-CHAIN

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Protrusion Index:
LYS B 125 N	0.71
LYS B 125 CA	0.53
LYS B 125 C	0.46
LYS B 125 O	0.42
LYS B 125 CB	0.63
LYS B 125 CG	0.80
LYS B 125 CD	0.91
LYS B 125 CE	1.24
LYS B 125 NZ	1.37

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Salt bridges:
ASP B 122	LYS B 125	2.657	INTRA-CHAIN

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Van der Waal's Interactions:
THR B 99 CG2 3059	LYS B 125 NZ 3237	-0.070	INTRA-CHAIN
ASP B 122 OD2 3215	LYS B 125 NZ 3237	-0.027	INTRA-CHAIN
LYS B 124 NZ 3228	LYS B 125 NZ 3237	-0.136	INTRA-CHAIN