Structural features of residue 289 in chain A

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Hydrophobic Interactions:
PHE A 286	VAL A 289	Dist=5.037	INTRA-CHAIN
LEU A 288	VAL A 289	Dist=5.491	INTRA-CHAIN
VAL A 289	ALA A 292	Dist=5.971	INTRA-CHAIN

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Protrusion Index:
VAL A 289 N	0.22
VAL A 289 CA	0.20
VAL A 289 C	0.17
VAL A 289 O	0.13
VAL A 289 CB	0.20
VAL A 289 CG1	0.17
VAL A 289 CG2	0.29

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Van der Waal's Interactions:
PHE A 109 CZ 835	VAL A 289 CG2 2205	-0.175	INTRA-CHAIN
ALA A 285 CB 2173	VAL A 289 CG2 2205	-0.014	INTRA-CHAIN
PHE A 286 CZ 2184	VAL A 289 CG2 2205	-0.043	INTRA-CHAIN
LEU A 288 CD2 2198	VAL A 289 CG2 2205	-0.015	INTRA-CHAIN
VAL A 289 CG2 2205	ALA A 292 CB 2226	-0.014	INTRA-CHAIN
VAL A 289 CG2 2205	THR A 293 CG2 2233	-0.014	INTRA-CHAIN
ASN B 14 ND2 2660	VAL A 289 CG2 2205	-0.016	INTER-CHAIN
TYR B 16 OH 2677	VAL A 289 CG2 2205	-0.011	INTER-CHAIN
GLN B 17 NE2 2686	VAL A 289 CG2 2205	-0.329	INTER-CHAIN