Structural features of residue 104 in chain A

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Electrostatic Interactions:
LYS A 104 NZ	GLU B 95 OE2	-5.583	INTER-CHAIN
LYS A 104 NZ	LYS A 105 NZ	0.437	INTRA-CHAIN
LYS A 104 NZ	GLU A 110 OE2	-1.604	INTRA-CHAIN
LYS A 104 NZ	GLU A 124 OE2	-1.554	INTRA-CHAIN
LYS A 105 NZ	LYS A 104 NZ	0.437	INTRA-CHAIN
GLU A 110 OE1	LYS A 104 NZ	-1.984	INTRA-CHAIN
GLU A 110 OE2	LYS A 104 NZ	-1.604	INTRA-CHAIN
GLU A 124 OE1	LYS A 104 NZ	-1.316	INTRA-CHAIN
GLU A 124 OE2	LYS A 104 NZ	-1.554	INTRA-CHAIN
GLU B 92 OE1	LYS A 104 NZ	-1.130	INTER-CHAIN
GLU B 95 OE1	LYS A 104 NZ	-3.777	INTER-CHAIN
GLU B 95 OE2	LYS A 104 NZ	-5.583	INTER-CHAIN

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Protrusion Index:
LYS A 104 N	0.10
LYS A 104 CA	0.07
LYS A 104 C	-0.01
LYS A 104 O	-0.03
LYS A 104 CB	0.10
LYS A 104 CG	0.17
LYS A 104 CD	0.22
LYS A 104 CE	0.32
LYS A 104 NZ	0.45

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Salt bridges:
LYS A 104	LYS A 105	2.947	INTRA-CHAIN
GLU B 95	LYS A 104	2.837	INTER-CHAIN

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Van der Waal's Interactions:
TYR A 69 OH 541	LYS A 104 NZ 822	-0.009	INTRA-CHAIN
LYS A 104 NZ 822	TYR A 121 OH 963	-0.008	INTRA-CHAIN
GLU B 95 OE2 1883	LYS A 104 NZ 822	-1.450	INTER-CHAIN