Structural features of residue 108 in chain A

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Hydrophobic Interactions:
ILE A 105	VAL A 108	Dist=5.530	INTRA-CHAIN
LEU A 107	VAL A 108	Dist=5.290	INTRA-CHAIN
VAL A 108	LEU A 195	Dist=6.772	INTRA-CHAIN
TYR B 84	VAL A 108	Dist=6.423	INTER-CHAIN

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Protrusion Index:
VAL A 108 N	0.46
VAL A 108 CA	0.28
VAL A 108 C	0.30
VAL A 108 O	0.25
VAL A 108 CB	0.20
VAL A 108 CG1	0.14
VAL A 108 CG2	0.18

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Van der Waal's Interactions:
THR A 104 CG2 863	VAL A 108 CG2 892	-0.206	INTRA-CHAIN
ILE A 105 CD1 871	VAL A 108 CG2 892	-0.031	INTRA-CHAIN
LEU A 107 CD2 885	VAL A 108 CG2 892	-0.014	INTRA-CHAIN
VAL A 108 CG2 892	PHE A 165 CZ 1351	-0.040	INTRA-CHAIN
VAL A 108 CG2 892	LEU A 195 CD2 1598	-0.140	INTRA-CHAIN
TYR B 84 OH 693	VAL A 108 CG2 892	-0.011	INTER-CHAIN