Structural features of residue 109 in chain A

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Electrostatic Interactions:
LYS A 101 NZ	LYS A 109 NZ	0.511	INTRA-CHAIN
LYS A 109 NZ	LYS A 101 NZ	0.511	INTRA-CHAIN
LYS A 109 NZ	GLU A 142 OE2	-1.649	INTRA-CHAIN
LYS A 109 NZ	GLU D 417 OE2	-1.460	INTER-CHAIN
LYS A 109 NZ	GLU D 420 OE2	-4.334	INTER-CHAIN
GLU A 142 OE1	LYS A 109 NZ	-1.392	INTRA-CHAIN
GLU A 142 OE2	LYS A 109 NZ	-1.649	INTRA-CHAIN
GLU D 417 OE1	LYS A 109 NZ	-1.715	INTER-CHAIN
GLU D 417 OE2	LYS A 109 NZ	-1.460	INTER-CHAIN
GLU D 420 OE1	LYS A 109 NZ	-5.591	INTER-CHAIN
GLU D 420 OE2	LYS A 109 NZ	-4.334	INTER-CHAIN

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Protrusion Index:
LYS A 109 N	0.09
LYS A 109 CA	0.04
LYS A 109 C	0.04
LYS A 109 O	-0.02
LYS A 109 CB	0.13
LYS A 109 CG	0.22
LYS A 109 CD	0.33
LYS A 109 CE	0.36
LYS A 109 NZ	0.68

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Salt bridges:
LYS A 109	GLU D 420	2.832	INTER-CHAIN

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Van der Waal's Interactions:
TRP A 105 CH2 802	LYS A 109 NZ 835	-0.015	INTRA-CHAIN
LYS A 109 NZ 835	VAL D 414 CG2 3215	-0.010	INTER-CHAIN
LYS A 109 NZ 835	LEU D 416 CD2 3235	-0.008	INTER-CHAIN
LYS A 109 NZ 835	GLU D 420 OE2 3269	-0.400	INTER-CHAIN
LYS A 109 NZ 835	ILE D 422 CD1 3282	-0.014	INTER-CHAIN