Structural features of residue 253 in chain A

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Hydrophobic Interactions:
ILE A 219	VAL A 253	Dist=6.799	INTRA-CHAIN
VAL A 249	VAL A 253	Dist=6.107	INTRA-CHAIN
LEU A 250	VAL A 253	Dist=5.606	INTRA-CHAIN
TYR A 252	VAL A 253	Dist=5.479	INTRA-CHAIN
VAL A 253	LEU D 268	Dist=4.801	INTER-CHAIN
VAL A 253	ALA D 272	Dist=4.726	INTER-CHAIN

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Protrusion Index:
VAL A 253 N	0.08
VAL A 253 CA	0.11
VAL A 253 C	0.30
VAL A 253 O	0.29
VAL A 253 CB	0.14
VAL A 253 CG1	0.25
VAL A 253 CG2	0.02

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Van der Waal's Interactions:
SER A 223 OG 1698	VAL A 253 CG2 1956	-0.189	INTRA-CHAIN
VAL A 249 CG2 1918	VAL A 253 CG2 1956	-0.179	INTRA-CHAIN
LEU A 250 CD2 1926	VAL A 253 CG2 1956	-0.030	INTRA-CHAIN
VAL A 253 CG2 1956	SER A 256 OG 1975	-0.013	INTRA-CHAIN
VAL A 253 CG2 1956	ARG A 257 NH2 1986	-0.016	INTRA-CHAIN
VAL A 253 CG2 1956	LEU D 268 CD2 2057	-0.118	INTER-CHAIN
VAL A 253 CG2 1956	ALA D 272 CB 2085	-0.120	INTER-CHAIN