Structural features of residue 109 in chain B

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Electrostatic Interactions:
GLU A 68 OE1	LYS B 109 NZ	-1.067	INTER-CHAIN
LYS A 71 NZ	LYS B 109 NZ	0.442	INTER-CHAIN
GLU A 86 OE1	LYS B 109 NZ	-1.602	INTER-CHAIN
GLU A 86 OE2	LYS B 109 NZ	-1.397	INTER-CHAIN
GLU A 88 OE1	LYS B 109 NZ	-5.920	INTER-CHAIN
GLU A 88 OE2	LYS B 109 NZ	-3.720	INTER-CHAIN
LYS B 109 NZ	LYS A 71 NZ	0.442	INTER-CHAIN
LYS B 109 NZ	GLU A 86 OE2	-1.397	INTER-CHAIN
LYS B 109 NZ	GLU A 88 OE2	-3.720	INTER-CHAIN
LYS B 109 NZ	LYS B 113 NZ	0.677	INTRA-CHAIN
LYS B 109 NZ	GLU B 117 OE2	-1.342	INTRA-CHAIN
LYS B 113 NZ	LYS B 109 NZ	0.677	INTRA-CHAIN
GLU B 117 OE1	LYS B 109 NZ	-1.260	INTRA-CHAIN
GLU B 117 OE2	LYS B 109 NZ	-1.342	INTRA-CHAIN

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Protrusion Index:
LYS B 109 N	0.37
LYS B 109 CA	0.33
LYS B 109 C	0.46
LYS B 109 O	0.41
LYS B 109 CB	0.36
LYS B 109 CG	0.26
LYS B 109 CD	0.29
LYS B 109 CE	0.43
LYS B 109 NZ	0.53

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Salt bridges:
GLU A 88	LYS B 109	2.675	INTER-CHAIN

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Van der Waal's Interactions:
THR A 85 CG2 1152	LYS B 109 NZ 1353	-0.283	INTER-CHAIN
GLU A 88 OE2 1179	LYS B 109 NZ 1353	-0.141	INTER-CHAIN
SER B 106 OG 1329	LYS B 109 NZ 1353	-0.009	INTRA-CHAIN