. 2012 Jul;2(7):120087. doi: 10.1098/rsob.120087

Table 2.

Key structural parameters and quality checks of the starting structure, a single denatured structure and refolded structures.

structure	total cavity volume (Å³)^a	average area (Å²)^b	average volume (Å³)^b	% helix^c	% 3_10^c	% strand^c	% turn^c	% coil^c	BBCCHK^d	QUACHK^d	RAMCHK^d	HNDCHK^d	r.m.s. comparison^e
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
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
5 ns refold	171.01	2061.87	3288.21	26.28	0.96	5.13	33.65	33.97	−2.63	−2.15	−5.41	2.45	6.18
7.833 ns	136.29	1845.42	3061.50	25.96	3.85	6.73	31.73	31.73	−2.56	−2.06	−5.17	2.56	5.95

^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.