Structural features of residue 108 in chain A

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Hydrophobic Interactions:
ILE A 105	VAL A 108	Dist=5.431	INTRA-CHAIN
LEU A 107	VAL A 108	Dist=5.208	INTRA-CHAIN
VAL A 108	PHE A 165	Dist=6.711	INTRA-CHAIN
TYR B 84	VAL A 108	Dist=6.937	INTER-CHAIN

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Protrusion Index:
VAL A 108 N	0.59
VAL A 108 CA	0.50
VAL A 108 C	0.52
VAL A 108 O	0.48
VAL A 108 CB	0.28
VAL A 108 CG1	0.27
VAL A 108 CG2	0.29

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Van der Waal's Interactions:
THR A 104 CG2 1207	VAL A 108 CG2 1233	-0.137	INTRA-CHAIN
ILE A 105 CD1 1215	VAL A 108 CG2 1233	-0.275	INTRA-CHAIN
LEU A 107 CB 1226	VAL A 108 CG2 1233	-0.096	INTRA-CHAIN
VAL A 108 CG2 1233	ARG A 111 CB 1252	-0.012	INTRA-CHAIN
VAL A 108 CG2 1233	PHE A 165 CZ 1637	-0.067	INTRA-CHAIN
VAL A 108 CG2 1233	LEU A 195 CD2 1878	-0.126	INTRA-CHAIN
TYR B 84 OH 1064	VAL A 108 CG2 1233	-0.009	INTER-CHAIN