In silico insight into Amurensinine - an N-Methyl-D-Aspartate receptor antagonist

Table 1 Chemical bonds of the GluN1A/GluN2B N-methyl-D-Aspartate receptor/Amurensinine complex

Non protonated Amurensinine: Receptor1	Distance (Å)	Bond type
Aromatic ring (A): ARG347	4.1	π-alky1
Aromatic ring (A): TYR 287	4.8	π-π T-shaped
Aromatic ring (B): LYS361	2.9	Hydrogen bond
Aromatic ring (B): LYS361	4.8	π-alky1
Aromatic ring (B): PRO360	5.4	π-alky1
C-12: ARG347	4.2	Alky1
C-12: LEU349	5.2	Alky1
C-12: TYR287	5.1	π-alky1
C-22: ASP348	3.6	Carbon-hydrogen bond
C-9: PHE146	3.4	Carbon-hydrogen bond
Cycloheptane: LYS361	4.8	Alky1
Cyclopentane: LYS361	3.3	Hydrogen bond
Cyclopentane: PRO360	5	π-alky1
N-1: HIS359	3.3	Hydrogen bond
O-3: ASP295	3.5	Hydrogen bond
Protonated Amurensinine: Receptor*	Distance (Å)	Bond type
Aromatic ring (B): ASP477	4.4	π-anion
Aromatic ring (B): TRP166	5.7	Alky1
CH-19: TYR476	3.1	Carbon-hydrogen bond
Cyclopentane: VAL390	4.9	π- alky1
NH-1: ASP477	2	Carbon-hydrogen bond
O1: ASP165	3.3	Hydrogen bond

¹Atom: Residue.

Amino acid residues are shown in the three-letter code and the number represents the position of the residue in the polypeptide chain. (A) and (B) indicate the different aromatic rings of Amurensinine.

Table 2 Chemical bonds in the GLUN1A/GLUN2B N-methyl-D-Aspartate receptor/Ifenprodil complex

Ifenprodil: Receptor1	Distance (Å)	Bond type
Aromatic ring: ARG393	3.8	π-sigma
Aromatic ring: VAL390	4.6	Alky1
Aromatic ring: LYS454	4.9	π- alky1
N-1: TYR164	3.5	Hydrogen bond
OH-2: THR255	2.6	Hydrogen bond
OH-1: ASP477	2.6	Hydrogen bond

¹Atom: Residue.

Amino acid residues are shown in the three-letter code and the number represents the position of the residue in the polypeptide chain.