Structural features of residue 109 in chain A

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Electrostatic Interactions:
LYS A 101 NZ	LYS A 109 NZ	0.510	INTRA-CHAIN
LYS A 109 NZ	LYS A 101 NZ	0.510	INTRA-CHAIN
LYS A 109 NZ	GLU A 142 OE2	-1.644	INTRA-CHAIN
LYS A 109 NZ	GLU D 417 OE2	-1.409	INTER-CHAIN
LYS A 109 NZ	GLU D 420 OE2	-5.335	INTER-CHAIN
GLU A 142 OE1	LYS A 109 NZ	-1.377	INTRA-CHAIN
GLU A 142 OE2	LYS A 109 NZ	-1.644	INTRA-CHAIN
GLU D 417 OE1	LYS A 109 NZ	-1.614	INTER-CHAIN
GLU D 417 OE2	LYS A 109 NZ	-1.409	INTER-CHAIN
GLU D 420 OE1	LYS A 109 NZ	-4.980	INTER-CHAIN
GLU D 420 OE2	LYS A 109 NZ	-5.335	INTER-CHAIN

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Protrusion Index:
LYS A 109 N	0.06
LYS A 109 CA	0.00
LYS A 109 C	0.02
LYS A 109 O	-0.03
LYS A 109 CB	0.09
LYS A 109 CG	0.18
LYS A 109 CD	0.26
LYS A 109 CE	0.36
LYS A 109 NZ	0.60

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Salt bridges:
LYS A 109	GLU D 420	3.180	INTER-CHAIN

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Van der Waal's Interactions:
TRP A 105 CH2 802	LYS A 109 NZ 835	-0.013	INTRA-CHAIN
LYS A 109 NZ 835	VAL D 414 CG2 3214	-0.010	INTER-CHAIN
LYS A 109 NZ 835	LEU D 416 CD2 3234	-0.008	INTER-CHAIN
LYS A 109 NZ 835	GLU D 420 OE2 3268	-1.319	INTER-CHAIN
LYS A 109 NZ 835	ILE D 422 CD1 3281	-0.015	INTER-CHAIN