Structural features of residue 108 in chain B

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Electrostatic Interactions:
LYS A 80 NZ	LYS B 108 NZ	0.524	INTER-CHAIN
GLU A 133 OE1	LYS B 108 NZ	-1.174	INTER-CHAIN
GLU A 133 OE2	LYS B 108 NZ	-1.115	INTER-CHAIN
GLU B 84 OE1	LYS B 108 NZ	-2.075	INTRA-CHAIN
GLU B 84 OE2	LYS B 108 NZ	-1.646	INTRA-CHAIN
LYS B 108 NZ	LYS A 80 NZ	0.524	INTER-CHAIN
LYS B 108 NZ	GLU B 84 OE2	-1.646	INTRA-CHAIN
LYS B 108 NZ	GLU B 112 OE2	-3.042	INTRA-CHAIN
LYS B 108 NZ	GLU A 133 OE2	-1.115	INTER-CHAIN
LYS B 108 NZ	GLU B 141 OE2	-1.894	INTRA-CHAIN
GLU B 112 OE1	LYS B 108 NZ	-3.312	INTRA-CHAIN
GLU B 112 OE2	LYS B 108 NZ	-3.042	INTRA-CHAIN
GLU B 141 OE1	LYS B 108 NZ	-2.003	INTRA-CHAIN
GLU B 141 OE2	LYS B 108 NZ	-1.894	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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|        N|      134|      A|         K|      108|      B|
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|        F|      135|      A|         K|      108|      B|
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Protrusion Index:
LYS B 108 N	0.43
LYS B 108 CA	0.49
LYS B 108 C	0.42
LYS B 108 O	0.38
LYS B 108 CB	0.39
LYS B 108 CG	0.48
LYS B 108 CD	0.29
LYS B 108 CE	0.24
LYS B 108 NZ	0.35

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Salt bridges:
ASP B 107	LYS B 108	2.213	INTRA-CHAIN

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Van der Waal's Interactions:
LEU B 85 O 806	LYS B 108 NZ 1000	-0.070	INTRA-CHAIN
LYS B 108 NZ 1000	GLU B 112 OE2 1028	-0.049	INTRA-CHAIN
LYS B 108 NZ 1000	PRO B 113 CD 1035	-0.022	INTRA-CHAIN
LYS B 108 NZ 1000	VAL B 114 CG2 1042	-0.011	INTRA-CHAIN
LYS B 108 NZ 1000	ASP B 115 OD2 1050	-0.602	INTRA-CHAIN
LYS B 108 NZ 1000	ARG B 125 NH2 1126	-0.017	INTRA-CHAIN