Structural features of residue 224 in chain A

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Electrostatic Interactions:
GLU A 24 OE1	LYS A 224 NZ	-1.206	INTRA-CHAIN
GLU A 24 OE2	LYS A 224 NZ	-1.089	INTRA-CHAIN
LYS A 27 NZ	LYS A 224 NZ	0.467	INTRA-CHAIN
GLU A 212 OE1	LYS A 224 NZ	-1.259	INTRA-CHAIN
GLU A 212 OE2	LYS A 224 NZ	-1.282	INTRA-CHAIN
LYS A 215 NZ	LYS A 224 NZ	1.134	INTRA-CHAIN
GLU A 220 OE1	LYS A 224 NZ	-3.219	INTRA-CHAIN
GLU A 220 OE2	LYS A 224 NZ	-3.129	INTRA-CHAIN
LYS A 224 NZ	GLU A 24 OE2	-1.089	INTRA-CHAIN
LYS A 224 NZ	LYS A 27 NZ	0.467	INTRA-CHAIN
LYS A 224 NZ	GLU A 212 OE2	-1.282	INTRA-CHAIN
LYS A 224 NZ	LYS A 215 NZ	1.134	INTRA-CHAIN
LYS A 224 NZ	GLU A 220 OE2	-3.129	INTRA-CHAIN
LYS A 224 NZ	GLU A 339 OE2	-1.235	INTRA-CHAIN
GLU A 339 OE1	LYS A 224 NZ	-1.163	INTRA-CHAIN
GLU A 339 OE2	LYS A 224 NZ	-1.235	INTRA-CHAIN

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Hydrogen bonds:

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|Res1 type| Res1 No.| Chain1| Res2 type| Res2 No.| Chain2|
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|        R|      116|      B|         K|      224|      A|
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Protrusion Index:
LYS A 224 N	0.67
LYS A 224 CA	0.53
LYS A 224 C	0.30
LYS A 224 O	0.29
LYS A 224 CB	0.41
LYS A 224 CG	0.50
LYS A 224 CD	0.71
LYS A 224 CE	0.74
LYS A 224 NZ	1.19

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Salt bridges:
GLU A 220	LYS A 224	3.045	INTRA-CHAIN
LYS A 224	HIS A 225	2.843	INTRA-CHAIN

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Van der Waal's Interactions:
TYR A 209 OH 1332	LYS A 224 NZ 1445	-0.195	INTRA-CHAIN
LYS A 215 NZ 1381	LYS A 224 NZ 1445	-0.032	INTRA-CHAIN
GLU A 220 OE2 1416	LYS A 224 NZ 1445	-0.050	INTRA-CHAIN
SER A 223 OG 1436	LYS A 224 NZ 1445	-0.034	INTRA-CHAIN