Structural features of residue 253 in chain B

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Hydrophobic Interactions:
ALA A 109	TYR B 253	Dist=6.859	INTER-CHAIN
TYR B 253	PHE B 254	Dist=5.416	INTRA-CHAIN
TYR B 253	LEU B 256	Dist=5.312	INTRA-CHAIN
TYR B 253	PHE B 257	Dist=6.077	INTRA-CHAIN

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Protrusion Index:
TYR B 253 N	0.09
TYR B 253 CA	0.10
TYR B 253 C	0.14
TYR B 253 O	0.11
TYR B 253 CB	0.09
TYR B 253 CG	0.01
TYR B 253 CD1	-0.04
TYR B 253 CD2	-0.03
TYR B 253 CE1	-0.02
TYR B 253 CE2	-0.04
TYR B 253 CZ	0.01
TYR B 253 OH	0.05

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Van der Waal's Interactions:
ALA A 109 CB 908	TYR B 253 OH 1428	-0.277	INTER-CHAIN
ILE A 110 CD1 916	TYR B 253 OH 1428	-0.020	INTER-CHAIN
GLU A 112 OE2 933	TYR B 253 OH 1428	-0.009	INTER-CHAIN
LEU A 113 CD2 941	TYR B 253 OH 1428	-0.093	INTER-CHAIN
VAL A 116 CG2 965	TYR B 253 OH 1428	-0.503	INTER-CHAIN
LEU B 228 CD2 1213	TYR B 253 OH 1428	-0.031	INTRA-CHAIN
TYR B 253 OH 1428	LEU B 256 CD2 1456	-0.010	INTRA-CHAIN