Table 3.

Ligand-free structures and their corresponding ligand-bound complexes used in testing the minimal rotation hypothesis

	PDB code			Resolution (Å)		Best ligand RMSD (Å)
No.	Free	Bound	Protein/ligand complex	Free	Bound	Flexible docking	Rigid docking	Template size
1M	1ahc	1ahb	Alpha-momorcharin/Formycin 5′-monophosphate	2.0	2.2	0.94	—	88
2M	1ajz	1aj2	Dihydropteroate synthase/Dihydropterine-diphosphate	2.0	2.0	0.75	—	79
3	3cox	1coy	Cholesterol oxidase/3-beta-hydroxy-5-androsten-17-one	1.8	1.8	1.61	—	74
4	1gmq	1gmr	RNAse SA/Guanosine-2′-monophosphate	1.8	1.8	1.28	1.63	87
5	3grs	1gra	Glutathione reductase/Glutathione disulfide	1.5	2.0	0.69	1.88	139
6	1kem	1kel	Catalytic antibody 28B4 FAB Fragment/AAHa	2.2	1.9	0.46	—	74
7M	2hvm	1llo	Hevamine(endochitinase)/N-Acetyl-d-allosamine	1.8	1.9	0.67	—	150
8	1nsb	1nsc	Neuraminidase/N-acetyl neuraminic acid(sialic acid)	2.2	1.7	0.40	0.67	74
9	1swa	1swd	Streptavidin/Biotin	2.0	1.9	0.62	0.67	37
10M	2ptn	1tps	Trypsin/Inhibitor A90720A	1.5	1.9	0.93	—	143
11	1xib	1xid	D-Xylose isomerase/L-Ascorbic acid	1.6	1.7	2.28	—	45
12M	1ydc	1ydb	Carbonic anhydrase II/Acetazolamide	2.0	1.9	1.42	—	50
13	2chs	2cht	Chorismate mutase/Endo-oxabicyclic inhibitor	1.9	2.2	1.02	—	39
14	2apr	3apr	Acid proteinase/Reduced peptide inhibitor	1.8	1.8	0.54	—	153
15	1tli	3tmn	Thermolysin/VAL-TRP	2.0	1.7	0.99	0.99	75
16	2ctv	5cna	Concanavalin A/alpha-methyl-D-mannopyranoside	2.0	2.0	1.99	—	57
17	2sga	5sga	Proteinase A/Tetrapeptide ACE-PRO-ALA-PRO-TYR	1.5	1.8	0.59	1.90	126
18M	6taa	7taa	Fam. 13 alpha amylase/Modified acarbose hexasaccharide	2.1	2.0	0.82	—	133

The template sizes are given as the number of template points to indicate the differences in the sizes of the binding sites of the proteins.

^a AAH = 1-[N-4′-nitrobenzyl-N-4′-carboxybutylaminomethylphosphonic acid.

^M Proteins existing as biological monomers both in their ligand-free and ligand-bound states.