Structural features of residue 108 in chain B

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

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

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