Structural features of residue 108 in chain A

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Hydrophobic Interactions:
VAL A 104	VAL A 108	Dist=6.227	INTRA-CHAIN
TYR A 107	VAL A 108	Dist=5.200	INTRA-CHAIN
VAL A 108	PHE A 111	Dist=5.678	INTRA-CHAIN
LEU B 32	VAL A 108	Dist=5.451	INTER-CHAIN

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Protrusion Index:
VAL A 108 N	0.38
VAL A 108 CA	0.25
VAL A 108 C	0.33
VAL A 108 O	0.23
VAL A 108 CB	0.13
VAL A 108 CG1	0.07
VAL A 108 CG2	0.04

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Van der Waal's Interactions:
LEU A 89 CD2 579	VAL A 108 CG2 721	-0.009	INTRA-CHAIN
VAL A 104 CG2 689	VAL A 108 CG2 721	-0.017	INTRA-CHAIN
GLY A 106 O 702	VAL A 108 CG2 721	-0.015	INTRA-CHAIN
CYS B 31 SG 937	VAL A 108 CG2 721	-0.243	INTER-CHAIN
LEU B 32 CD2 945	VAL A 108 CG2 721	-0.115	INTER-CHAIN
ILE B 35 CD1 973	VAL A 108 CG2 721	-0.171	INTER-CHAIN
ILE B 61 CD1 1178	VAL A 108 CG2 721	-0.035	INTER-CHAIN