Table 4.

Interaction profile between PS and ATP in wild-type and alanine mutants after MD simulations.

Systems	No. of hydrogen bond	Participating residues in hydrogen bond with their bond length (Å)	Participating residues in hydrophobic bonding
Wild-type	16	Arg44(2.7 Å), Arg47(2.7 Å, 2.9 Å), Gly158(2.7 Å,), Lys160(2.5 Å, 2.9 Å), Val187(3.0 Å, 3.0 Å), Met195(2.9 Å), Ser196(2.7 Å), Ser197(3.1 Å, 2.8 Å, 2.6 Å), Arg198(2.8 Å, 2.7 Å, 2.5 Å)	Gly46, Leu50, Phe157, Pro185, Thr186
H44A	13	Arg47(2.6 Å), Lys160(2.5 Å, 3.0 Å), Asp161(2.5 Å), Val187(2.9 Å, 2.9 Å), Met195(2.9 Å), Ser196(2.7 Å), Ser197(2.9 Å, 3.0 Å), Arg198(3.2 Å, 2.6 Å, 2.5 Å)	Gly46, Phe157, Gly158, Pro185, Thr186
H47A	9	Arg44(2.8 Å), Gly158(2.9 Å,), Lys160(2.7 Å), Val187(2.9 Å, 3.1 Å), Met195(2.9 Å), Ser196(2.6 Å), Arg198(2.6 Å, 2.5 Å)	Gly46, His47, Leu50, Phe157, Pro185, Thr186
N69A	12	Arg44(2.6 Å), Lys160(2.9 Å, 2.6 Å, 2.9 Å), Val187(3.0 Å, 3.0 Å), Met195(3.0 Å), Ser196(2.6 Å), Ser197(2.7 Å), Arg198(2.8 Å, 2.6 Å, 2.5 Å)	Met40, Gly46, His47, Leu50, Phe157, Gly158, Thr186
Q72A	16	Arg44(2.7 Å), Arg47(2.6 Å), Gly158(3.0 Å), Lys160(2.5 Å, 2.9 Å), Asp161(2.9 Å),Val187(2.9 Å, 2.8 Å), Met195(3.0 Å), Ser196(2.6 Å), Ser197(2.9 Å, 2.9 Å, 3.1 Å), Arg198(2.7 Å, 2.7 Å, 3.1 Å)	His44, Leu50, Phe157, Pro185, Thr186
K160A	9	Arg44(2.6 Å), Val187(2.9 Å), Met195(2.8 Å, 3.3 Å), Ser197(3.2 Å, 2.8 Å), Arg198(2.9 Å, 2.9 Å, 2.9 Å)	Gly46, His47, Leu50, Phe157, Ala160, Pro185, Thr186
Q164A	15	Arg44(2.6 Å), Gly158(2.9 Å, 3.3 Å), Lys160(2.5 Å, 2.8 Å), Asp161(3.2 Å) Val187(2.9 Å, 2.7 Å), Met195(3.0 Å), Ser196(2.6 Å), Ser197(2.8 Å, 3.1 Å), Arg198(2.5 Å, 2.6 Å, 3.0 Å)	Met40, His47, Leu50, Phe157, Pro185, Thr186