Table 3.

Experimental restraints and structural statistics for the 20 lowest-energy structures of glutathionylated hHsp70 SBD (residues 386–641)

Distance restraints
Intraresidue	866
Sequential	477
Medium	158
Long-range	451
Ambiguous	1249
Total	3201
Hydrogen bond restraints	90
Dihedral angle restraints
ϕ	99
y	95
χ1	63
Total	257
Violations
NOE violations (>0.3 Å)	0
Torsion angle violation (>5°)	0
PROCHECK statistics (%)a
Most favored regions	86.8
Additional allowed regions	11.4
Generously allowed regions	0.8
Disallowed regions	0.9
r.m.s.d. from mean structure (Å)
Backbone heavy atoms
All residuesb	1.67 ± 0.28
Regular secondary structurec	0.42 ± 0.09
All heavy atoms
All residues	2.37 ± 0.32
Regular secondary structure	1.22 ± 0.15

^a Residues used to calculate PROCHECK statistics include 394–545.

^b Residues used to calculate the r.m.s.d. values of all residues include 394–545 in glutathionylated hHsp70(385–641).

^c Regular secondary structure regions used here include β-strand residues: 401–404, 410–415, 422–428, 438–444, 457–460, 474–480, 486–491, and 498–504 for glutathionylated hHsp70(385–641).