Hydrogen bond networks determine emergent mechanical and thermodynamic properties across a protein family

BMC Chemistry

Table 2 Descriptions of the structures used in this report.¹

	LAOBP		HBP	GBP		PhBP
Source	S. typhimurium		E. coli	E. coli		E. coli
PDB ID	1LST	2LAO*	1HSL	1WDN	1GGG*	1IXH
Bound ligand²	Lysine	n/a	histidine	glutamine	n/a	phosphate
Number of residues	238	238	238	223	220	321
Large domain³	1–90, 191–240		1–90,191–238	4–88, 182–226		1–75,255–321
Small domain	91–190		91–190	89–181		76–254
Resolution (Å)	1.80	1.90	1.89	1.94	2.30	0.98
Number of H-bonds	352	357	327	327	293	504
Number of H-bonds to substrate	5	n/a	6	9	n/a	7
Total H-bond energy (Kcal/mol)⁴	-942.11	-875.20	-714.00	-757.28	-633.40	-1274.28
Avg. H-bond energy (kcal/mol)	-2.68	-2.45	-2.18	-2.32	-2.16	-2.53
Std. dev. H-bond energy (kcal/mol)	2.34	2.27	2.12	2.22	2.05	2.30

¹All four bPBP homologs have been crystallized in the ligated conformation. Additionally, two bPBP homologs (marked with asterisks) have been crystallized in the open apo conformation. ² Non-biologically relevant co-crystallized solutes (i.e., metal ions) are ignored. ³ Domain boundaries are identified from the ligated structures using PDP [40]. ⁴ Total H-bond energy is simply the sum of the energies for each H-bond observed within the structure.

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