Table 1.

Key structural parameters and quality checks of the starting structure, the denatured structure and its refolded counterpart.

structure	total cavity volume (Å3)a	average area (Å2)b	average volume (Å3)b	% helixc	% 3_10c	% strandc	% turnc	% coilc	BBCCHKd	QUACHKd	RAMCHKd	HNDCHKd	r.m.s. comparisone
crystal	148.36	1716.92	2521.74	37.18	1.92	15.71	19.23	25.96	0.14	−0.75	−2.42	0.59	0
ezrU1000	135.94	1875.24	3020.59	25.00	2.24	10.90	33.01	28.85	−3.14	−1.91	−6.59	4.81	1.56
ezrU2000	102.06	1846.57	2837.62	18.59	4.81	8.97	36.22	31.41	−3.95	−2.08	−7.72	6.52	1.92
ezrU3000	143.39	1870.54	2862.15	5.77	2.89	3.21	49.36	38.78	−3.51	−2.33	−7.97	7.88	2.51
ezrU4000	148.41	1926.01	3027.20	7.69	1.92	4.81	46.47	39.11	−4.48	−2.69	−8.39	8.78	2.77
ezrU5000	228.08	1856.60	2855.86	2.56	2.89	0	48.40	46.15	−3.90	−2.73	−8.91	10.11	2.98

^aCavity volume (Cavvol) analyses for the protein in starting, unfolded and refolded state.

^bdarvols areas and volumes, respectively.

^cThe secondary structure statistics.

^dBackbone conformation normality check (BBCCHK), packing quality control (QUACHK), Ramachandran z-score (RAMCHK) and checks for atoms with the wrong hand (HNDCHK), respectively.

^eResults of r.m.s. comparison of simulation structures compared with the starting crystal structure.