Structural features of residue 123 in chain B

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Electrostatic Interactions:
GLU A 321 OE1	LYS B 123 NZ	-1.276	INTER-CHAIN
GLU A 321 OE2	LYS B 123 NZ	-1.429	INTER-CHAIN
LYS B 123 NZ	LYS B 126 NZ	0.721	INTRA-CHAIN
LYS B 123 NZ	LYS B 131 NZ	0.738	INTRA-CHAIN
LYS B 123 NZ	GLU B 133 OE2	-1.117	INTRA-CHAIN
LYS B 123 NZ	GLU B 134 OE2	-1.552	INTRA-CHAIN
LYS B 123 NZ	LYS B 138 NZ	0.419	INTRA-CHAIN
LYS B 123 NZ	GLU A 321 OE2	-1.429	INTER-CHAIN
LYS B 126 NZ	LYS B 123 NZ	0.721	INTRA-CHAIN
LYS B 131 NZ	LYS B 123 NZ	0.738	INTRA-CHAIN
GLU B 133 OE1	LYS B 123 NZ	-1.320	INTRA-CHAIN
GLU B 133 OE2	LYS B 123 NZ	-1.117	INTRA-CHAIN
GLU B 134 OE1	LYS B 123 NZ	-1.875	INTRA-CHAIN
GLU B 134 OE2	LYS B 123 NZ	-1.552	INTRA-CHAIN
LYS B 138 NZ	LYS B 123 NZ	0.419	INTRA-CHAIN

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Protrusion Index:
LYS B 123 N	1.24
LYS B 123 CA	1.17
LYS B 123 C	1.13
LYS B 123 O	1.19
LYS B 123 CB	0.97
LYS B 123 CG	1.22
LYS B 123 CD	1.04
LYS B 123 CE	1.51
LYS B 123 NZ	1.45

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Salt bridges:
ASP B 120	LYS B 123	3.021	INTRA-CHAIN

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Van der Waal's Interactions:
ASP B 120 OD2 871	LYS B 123 NZ 892	-0.073	INTRA-CHAIN
LYS B 123 NZ 892	ALA A 322 OXT 2359	-0.054	INTER-CHAIN