Structural features of residue 108 in chain C

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Hydrophobic Interactions:
PHE C 12	VAL C 108	Dist=3.973	INTRA-CHAIN
TYR C 13	VAL C 108	Dist=5.803	INTRA-CHAIN
VAL C 76	VAL C 108	Dist=5.359	INTRA-CHAIN
LEU C 106	VAL C 108	Dist=6.772	INTRA-CHAIN
VAL C 108	VAL C 111	Dist=6.591	INTRA-CHAIN
PHE B 104	VAL C 108	Dist=5.420	INTER-CHAIN
VAL B 105	VAL C 108	Dist=6.663	INTER-CHAIN
LEU B 106	VAL C 108	Dist=5.494	INTER-CHAIN

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Protrusion Index:
VAL A 108 C	0.02
VAL C 108 N	-0.03
VAL C 108 CA	-0.03
VAL C 108 C	0.03
VAL C 108 O	0.05
VAL C 108 CB	0.04
VAL C 108 CG1	0.01
VAL C 108 CG2	-0.02

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Van der Waal's Interactions:
LEU B 106 CD2 1497	VAL C 108 CG2 2377	-0.310	INTER-CHAIN
PRO B 107 CD 1504	VAL C 108 CG2 2377	-0.017	INTER-CHAIN
SER C 10 OG 1742	VAL C 108 CG2 2377	-0.014	INTRA-CHAIN
LYS C 14 NZ 1783	VAL C 108 CG2 2377	-0.015	INTRA-CHAIN
VAL C 76 CG2 2137	VAL C 108 CG2 2377	-0.160	INTRA-CHAIN
PRO C 107 CD 2370	VAL C 108 CG2 2377	-0.013	INTRA-CHAIN
VAL C 108 CG2 2377	VAL C 111 CG2 2398	-0.023	INTRA-CHAIN