Table 1.

Structural properties of the proteins after five chaperone cycles

						RG		SASA
PDBID	Nres	Exp.Nα	Exp.Nβ	RMSD	HB	Exp.	Model	Exp.	Model
1vcc	77	11	25	0.59 (0.59)	6 (8)	1.23	1.20 (1.30)	24.7/27.6	24.2/32.0 (29.4/32.3)
1alz	83	62	0	0.46 (0.55)	17 (13)	1.21	1.20 (1.33)	22.9/38.1	25.0/31.7 (31.4/29.5)
1sro	76	4	27	0.55 (0.87)	8 (11)	1.22	1.24 (1.31)	24.2/32.5	25.0/30.6 (27.8/32.1)

PDBID indicates Protein Data Bank identifier; N_res, number of residues; N_α, the number of helical residues; N_β, the number of strand residues; the backbone root mean squared deviation (RMSD) in nm with respect to the experimental structure after 50-nsec molecular dynamics (MD) simulation using five chaperone cycles starting from different initial configurations (the values in parentheses correspond to the RMSD of the starting model with respect to the experimental structure); HB, the number of native hydrogen bonds in a certain conformation while the native hydrogen bonds were defined as that occur with a frequency >0.9 during the last 1 nsec of the MD simulations started from the experimental structure; RG, radius of gyration; RG exp., RG of experimental structure; RG model, RG of predicted model structure (the value in parentheses correspond to the RG of the initial model); SASA, solvent-accessible surface area; SASA exp., hydrophobic and hydrophilic SASA of the experimental structure; and SASA model, hydrophobic and hydrophilic SASA of the predicted model structure (the value in parentheses correspond to the SASA of the initial model).