Table 4.

Intermolecular hydrogen bonds (Å) involving the inhibitor atom(s) NH1, NH2, or Nζ, or the OW3 molecule in the anionic salmon trypsin structures

	AST-1BZA		AST-2BEA	AST-3PEA	AST-4PPA	AST-Free	AST-BPT1
Contacts to	NH1	NH2	NH1	NH1	NH1	OW3	Nζ
Asp 189 Oδ1	2.87	(3.73)	3.33	3.14	3.46	2.85	3.35
Asp 189 Oδ2	(3.55)	2.84	2.70	(3.55)	(3.73)	3.18	(3.73)
Ser 190 O	3.17	3.34	2.86	3.16	3.07	2.93	2.78
Ser 190 Oγ	3.04			3.15	3.01	3.40	3.07
Gly 219 O		2.87	3.13
OW1			2.97	2.79	2.75	2.72	2.96
OW2	2.95			2.94	3.08	3.45	3.05
Cys 191 C-Trp 215 C		7.83	8.05	8.46	8.23	8.10	8.28
Relative B-factor of inhibitor		1.03	0.71	1.48	1.74		0.48a

Distances longer than 3.5 Å are given in parentheses, and the width of the pocket is taken as the Cys 191 C to Trp 215 C distance. Relative B-factors the inhibitors (〈B-factor_inhib〉/〈B-factor_prot〉) are also included.

^a Side-chain atoms only.