Structural features of residue 425 in chain A

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Hydrophobic Interactions:
TYR A 399	VAL A 425	Dist=6.207	INTRA-CHAIN
ALA A 424	VAL A 425	Dist=4.843	INTRA-CHAIN
VAL A 425	LEU A 427	Dist=6.279	INTRA-CHAIN
ALA B 382	VAL A 425	Dist=4.985	INTER-CHAIN
LEU B 392	VAL A 425	Dist=6.786	INTER-CHAIN

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Protrusion Index:
VAL A 425 N	-0.05
VAL A 425 CA	-0.04
VAL A 425 C	0.01
VAL A 425 O	0.03
VAL A 425 CB	-0.03
VAL A 425 CG1	-0.02
VAL A 425 CG2	-0.07

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Van der Waal's Interactions:
GLY A 394 O 3020	VAL A 425 CG2 3251	-0.105	INTRA-CHAIN
ASN A 395 ND2 3028	VAL A 425 CG2 3251	-0.014	INTRA-CHAIN
SER A 423 OG 3239	VAL A 425 CG2 3251	-0.013	INTRA-CHAIN
ALA A 424 CB 3244	VAL A 425 CG2 3251	-0.161	INTRA-CHAIN
VAL A 425 CG2 3251	PRO A 426 CD 3258	-0.072	INTRA-CHAIN
VAL A 425 CG2 3251	LEU A 427 CD2 3266	-0.011	INTRA-CHAIN
ALA B 382 CB 2918	VAL A 425 CG2 3251	-0.031	INTER-CHAIN
ASP B 384 OD2 2937	VAL A 425 CG2 3251	-0.008	INTER-CHAIN
LEU B 392 CD2 3004	VAL A 425 CG2 3251	-0.055	INTER-CHAIN
GLN B 422 NE2 3233	VAL A 425 CG2 3251	-0.015	INTER-CHAIN