Structural features of residue 108 in chain A

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Hydrophobic Interactions:
VAL A 53	TYR A 108	Dist=5.808	INTRA-CHAIN
LEU A 62	TYR A 108	Dist=5.497	INTRA-CHAIN
TYR A 108	PHE A 110	Dist=6.569	INTRA-CHAIN

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Protrusion Index:
TYR A 108 N	-0.39
TYR A 108 CA	-0.41
TYR A 108 C	-0.39
TYR A 108 O	-0.36
TYR A 108 CB	-0.45
TYR A 108 CG	-0.46
TYR A 108 CD1	-0.45
TYR A 108 CD2	-0.44
TYR A 108 CE1	-0.41
TYR A 108 CE2	-0.39
TYR A 108 CZ	-0.38
TYR A 108 OH	-0.32
TYR A 108 H	-0.40
TYR A 108 HA	-0.41
TYR A 108 HB2	-0.47
TYR A 108 HB3	-0.46
TYR A 108 HD1	-0.44
TYR A 108 HD2	-0.44
TYR A 108 HE1	-0.38
TYR A 108 HE2	-0.36
TYR A 108 HH	-0.33

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Short Contacts:
TYR A 108 O	HIS B 131 H	-0.351	INTER-CHAIN
TYR A 108 H	HIS B 131 O	-0.438	INTER-CHAIN

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Van der Waal's Interactions:
SER A 55 HG 871	TYR A 108 HH 1664	-0.000	INTRA-CHAIN
LEU A 62 HD23 988	TYR A 108 HH 1664	-0.000	INTRA-CHAIN
ILE A 103 HD13 1597	TYR A 108 HH 1664	-0.001	INTRA-CHAIN
ALA A 104 HB3 1607	TYR A 108 HH 1664	-0.004	INTRA-CHAIN
PRO A 105 HD3 1621	TYR A 108 HH 1664	-0.000	INTRA-CHAIN
TYR A 108 HH 1664	HIS B 133 HE2 4150	-0.000	INTER-CHAIN