Table 1.

Summary statistics describing the structures used in this report.

Protein	Source	PDBID	Resol.1	# Res.	# HB	Avg HB E2	RMSD3	Seq Id4
Oxidized structures
TRX	E. coli	2TRX	1.7 Å	108	141	−2.6	0.0 Å	100 %
TRX	S. aureus	2O7K	2.2 Å	103	142	−2.3	1.3 Å	51 %
TRX-m	Spinach cholorplast	1FB6	2.1 Å	104	130	−2.4	1.0 Å	48 %
TRX-2	Anabaena sp.	1THX	1.6 Å	108	142	−2.6	1.0 Å	43 %
TRX-2	Human mitochondria	1W4V	1.8 Å	107	142	−2.5	1.2 Å	38 %
TRX-h	C. reinhardtii cytosol	1EP7	2.1 Å	112	142	−2.5	1.4 Å	36 %
TRX-f	Spinach cholorplast	1F9M	1.9 Å	112	148	−2.5	1.4 Å	32 %
TRX	Fruit fly cytosol	1XWA	2.2 Å	106	145	−2.4	1.2 Å	31 %
TRX	Human cytosol	1ERU	2.1 Å	105	146	−2.4	1.3 Å	27 %
Reduced structures
TRX-2	Human mitochondria	1UVZ	2.0 Å	107	140	−2.3	0.2 Å	100 %
TRX	Fruit fly cytosol	1XWC	2.3 Å	106	141	−2.3	0.5 Å	100 %
TRX	Human cytosol	1ERT	1.7 Å	105	155	−2.2	0.2 Å	100 %

¹The x-ray crystallographic resolution.

²The average hydrogen bond energy (kcal/mol).

³The α-carbon root mean square deviation comparing each structure to the E. coli homolog. In the case of the reduced TRXs, the comparison is to the oxidized state of the same homolog.

⁴The pairwise percent residue identity comparing each sequence to the E. coli homolog. In the case of the reduced TRXs, the comparison is to its oxidized state.