Table 4.

Residues involved in the hydrogen bond interactions between natriuretic receptors and their ligands (L2 and BNP).

	hNPR-A	hNPR-B	hNPR-C
L2	GLY1-GLU119 (A) LYS4-GLU162 (B) LYS7-ASP192 (B) LYS7-ASP191(B) LYS8-GLU187 (B) GLY13-GLU187 (B) PHE15-HSD185 (B) LYS18-ASP177 (A) ARG21-GLU162 (A) ARG21-GLU162 (B) GLY23-GLU162 (B) ASP34-LYS132 (B) ASP34-ARG174 (B) ASP34-ARG178 (B)	GLY1-PHE419 (A) ASP2-ARG143 (A) ASP2-ARG200 (A) LYS7-GLU189 (C) PRO11-GLN177 (A) GLY13-GLU184 (C) LYS18-GLU163 (A) ASP20-ARG183 (C) ARG21-GLU55 (C) GLY23-ASP155 (C) SER24-GLU55 (C) LYS32-GLU55 (A) ASN36-HSD92 (C) LYS37-GLU337 (C) LYS37-ASP338 (C) GLY38-ARG1 (C)	GLY1-GLU180 (A) GLY1-GLU181 (A) LYS4-GLU180 (A) LYS7-ASP197 (B) LYS7-ASP200 (B) LYS18-GLU176 (A) LYS18-GLU180 (A) ASP20-LYS162 (B) ASP20-LYS194 (B) ARG21-GLU172 (A) ARG21-GLU176 (A) LYS37-ASP105 (B)
BNP	LYS3-ARG178 (A) ARG13-ASP177 (A) LYS14-GLU169 (A) ARG17-GLU162 (B) SER21-GLU162 (A) SER22-TYR156 (A) SER22-GLU169 (B) GLY25-GLU187 (A) LYS27-GLU187 (A) ARG31-GLU169 (B)	SER1-THR116 (A) SER1-GLN347 (A) ARG13-GLU129 (A) ARG13-GLU393 (A) MET15-GLU167 (A) ARG17-ASP155 (C) SER19-GLU55 (C) SER22-TYR56 (A) SER21-ARG88 (C) ARG30-GLU184 (C) ARG31-ASP155 (C)	ARG13-GLU180 (A) LYS14-HSD120 (A) LYS14-GLU176 (A) LYS14-GLU180 (A) ASP16-ARG99 (A) ASP16-SER123 (A) ARG17-GLU176 (A) SER22-GLY117 (B) LYS27-GLU172 (B) LYS27-GLU176 (B) LEU29-TYR168 (B) HSD32-ARG165 (B)

Residues in L2 and BNP (annotated in bold) involved in the H-bond interactions allowing the best receptor–ligand stability were specifically determined using VMD software and visualized by PyMol at 3 Å. BNP, B-type natriuretic peptide; L2, Lebetin 2; NPR-A, natriuretic peptide receptor A; NPR-B, natriuretic peptide receptor B; NPR-C, natriuretic peptide receptor C. (A), chain A; (B) chain B; (C) chain C of natriuretic receptors.