Structural features of residue 233 in chain A

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Electrostatic Interactions:
LYS A 226 NZ	LYS A 233 NZ	0.669	INTRA-CHAIN
GLU A 229 OE1	LYS A 233 NZ	-1.404	INTRA-CHAIN
GLU A 229 OE2	LYS A 233 NZ	-1.204	INTRA-CHAIN
LYS A 233 NZ	LYS A 226 NZ	0.669	INTRA-CHAIN
LYS A 233 NZ	GLU A 229 OE2	-1.204	INTRA-CHAIN
LYS A 233 NZ	GLU A 238 OE2	-1.712	INTRA-CHAIN
LYS A 233 NZ	GLU A 241 OE2	-1.367	INTRA-CHAIN
LYS A 233 NZ	GLU A 259 OE2	-1.469	INTRA-CHAIN
LYS A 233 NZ	LYS A 282 NZ	0.423	INTRA-CHAIN
GLU A 238 OE1	LYS A 233 NZ	-1.430	INTRA-CHAIN
GLU A 238 OE2	LYS A 233 NZ	-1.712	INTRA-CHAIN
GLU A 241 OE1	LYS A 233 NZ	-1.358	INTRA-CHAIN
GLU A 241 OE2	LYS A 233 NZ	-1.367	INTRA-CHAIN
GLU A 259 OE1	LYS A 233 NZ	-1.264	INTRA-CHAIN
GLU A 259 OE2	LYS A 233 NZ	-1.469	INTRA-CHAIN
LYS A 282 NZ	LYS A 233 NZ	0.423	INTRA-CHAIN

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Protrusion Index:
LYS A 233 N	-0.01
LYS A 233 CA	0.06
LYS A 233 C	0.16
LYS A 233 O	0.13
LYS A 233 CB	0.06
LYS A 233 CG	0.10
LYS A 233 CD	0.21
LYS A 233 CE	0.26
LYS A 233 NZ	0.47

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Salt bridges:
GLU A 229	LYS A 233	3.139	INTRA-CHAIN

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Van der Waal's Interactions:
HIS A 220 NE2 1782	LYS A 233 NZ 1884	-0.046	INTRA-CHAIN
GLY A 230 O 1859	LYS A 233 NZ 1884	-0.028	INTRA-CHAIN
LYS A 233 NZ 1884	TYR A 237 OH 1922	-0.012	INTRA-CHAIN
LYS A 233 NZ 1884	ASP A 283 OD2 2283	-0.067	INTRA-CHAIN
VAL B 98 CG2 4191	LYS A 233 NZ 1884	-0.062	INTER-CHAIN