Structural features of residue 123 in chain B

*********************************
Electrostatic Interactions:
LYS A 121 NZ	LYS B 123 NZ	0.452	INTER-CHAIN
LYS A 127 NZ	LYS B 123 NZ	0.624	INTER-CHAIN
GLU A 135 OE1	LYS B 123 NZ	-1.301	INTER-CHAIN
GLU A 135 OE2	LYS B 123 NZ	-1.298	INTER-CHAIN
LYS B 123 NZ	LYS A 121 NZ	0.452	INTER-CHAIN
LYS B 123 NZ	LYS A 127 NZ	0.624	INTER-CHAIN
LYS B 123 NZ	LYS B 127 NZ	1.230	INTRA-CHAIN
LYS B 123 NZ	GLU A 135 OE2	-1.298	INTER-CHAIN
LYS B 123 NZ	GLU B 135 OE2	-2.096	INTRA-CHAIN
LYS B 123 NZ	GLU B 136 OE2	-1.204	INTRA-CHAIN
LYS B 123 NZ	LYS B 169 NZ	0.433	INTRA-CHAIN
LYS B 127 NZ	LYS B 123 NZ	1.230	INTRA-CHAIN
GLU B 135 OE1	LYS B 123 NZ	-1.943	INTRA-CHAIN
GLU B 135 OE2	LYS B 123 NZ	-2.096	INTRA-CHAIN
GLU B 136 OE1	LYS B 123 NZ	-1.085	INTRA-CHAIN
GLU B 136 OE2	LYS B 123 NZ	-1.204	INTRA-CHAIN
LYS B 169 NZ	LYS B 123 NZ	0.433	INTRA-CHAIN

*********************************
Protrusion Index:
LYS B 123 N	0.27
LYS B 123 CA	0.30
LYS B 123 C	0.43
LYS B 123 O	0.37
LYS B 123 CB	0.32
LYS B 123 CG	0.15
LYS B 123 CD	0.18
LYS B 123 CE	0.36
LYS B 123 NZ	0.45

*********************************
Salt bridges:
ASP B 120	LYS B 123	3.180	INTRA-CHAIN

*********************************
Van der Waal's Interactions:
ASP B 120 OD2 1233	LYS B 123 NZ 1259	-0.015	INTRA-CHAIN
LYS B 123 NZ 1259	LYS B 127 NZ 1290	-0.051	INTRA-CHAIN
LYS B 123 NZ 1259	PHE B 134 CZ 1350	-0.017	INTRA-CHAIN
LYS B 123 NZ 1259	TYR B 162 OH 1596	-0.030	INTRA-CHAIN