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	-1.650	INTRA-CHAIN
LYS A 109 NZ	GLU D 417 OE2	-1.583	INTER-CHAIN
LYS A 109 NZ	GLU D 420 OE2	-5.441	INTER-CHAIN
GLU A 142 OE1	LYS A 109 NZ	-1.390	INTRA-CHAIN
GLU A 142 OE2	LYS A 109 NZ	-1.650	INTRA-CHAIN
GLU D 417 OE1	LYS A 109 NZ	-1.485	INTER-CHAIN
GLU D 417 OE2	LYS A 109 NZ	-1.583	INTER-CHAIN
GLU D 420 OE1	LYS A 109 NZ	-5.055	INTER-CHAIN
GLU D 420 OE2	LYS A 109 NZ	-5.441	INTER-CHAIN

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Protrusion Index:
LYS A 109 N	0.09
LYS A 109 CA	0.02
LYS A 109 C	0.03
LYS A 109 O	-0.02
LYS A 109 CB	0.10
LYS A 109 CG	0.17
LYS A 109 CD	0.25
LYS A 109 CE	0.31
LYS A 109 NZ	0.62

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Salt bridges:
LYS A 109	GLU D 420	3.133	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 3214	-0.010	INTER-CHAIN
LYS A 109 NZ 835	LEU D 416 CD2 3234	-0.008	INTER-CHAIN
LYS A 109 NZ 835	GLN D 418 NE2 3252	-0.008	INTER-CHAIN
LYS A 109 NZ 835	GLU D 420 OE2 3268	-1.470	INTER-CHAIN