Table 3.

Binding affinities and molecular interaction of the best lead molecules to target Brucella transcription termination factor rho protein was calculated from PyMOL software

S number	ZINC ID	Binding affinity (kcal/mol)	Protein-ligand interactions		Bond distance	Bond angle
			Protein	Ligand
1	ZINC24934545	−10.4	Arg180 CA-N	O57P55	2.80	107.38
			Arg180 C-O	N49C1	2.29	111.49
			Thr188 CB-OG1	O40P56	3.26	138.75
			Thr188 CB-OG1	O58P56	3.27	97.26
			Thr188 CB-OG1	O53C25	2.99	147.81
			Asp213 C-O	HN8N50	2.90	129.85
			Asp213 C-O	O38C42	3.18	139.40
			Asp213 CG-OD1	O38C42	3.35	88.25
			*Arg215 CZ-NH1	O52C16	3.24	110.96
			Glu218 CD-OE2	O58P56	3.12	106.91
			Phe358 C-O	O37C41	3.31	132.17
			Phe358 C-O	N3C41	3.30	133.70
2	ZINC72319544	−10.4	Thr185 CA-N	O38C42	2.80	105.05
			Thr185 CB-OG1	O38C42	2.97	113.79
			Gly186 CA-N	O38C42	2.84	122.00
			Lys187 CA-N	O38C42	3.11	119.29
			Asp213 C-O	O57P55	3.52	133.45
			*Arg215 CZ-NH2	O43P55	3.28	91.52
			*Arg215 CZ-NH2	O47P56	2.99	157.60
			*Arg215 CA-N	O57P55	3.00	135.60
			Phe235 C-O	N49C1	2.98	121.93
			Phe235 C-O	O37C41	3.45	139.39

Note:

^*The anchoring residue for the inhibitor interaction in rho.

Abbreviations: S, serial; ZINC, ZINC Is Not Commercial.