Table 1.

Structural statistics for the 20 lowest energy solution structures of ASPB and ASPC as determined by PSVS (protein structure validation suite).

	ASPBa	ASPCb
Experimental constraints
Total NOE	639	552
Intra-residue [i = j]	94	114
Sequential [|i – j| = 1]	199	197
Medium range [1 < |i – j| < 5]	91	56
Long range [|i – j| ≥ 5]	255	185
Dihedral angles	18	18
Hydrogen bonds	18	20
Violations
Distance (>0.1 Å)	0	0
Dihedral angle (>1°)	0	0
Van der Waals (<1.6 Å)	0	0
RMSD from idealized geometryc
Bond lengths (Å)	0.009	0.011
Bond angles (°)	0.6	0.8
RMS of distance violation (Å)	0.01	0.01
RMS of dihedral angle violation (°)	0	0.008
Average pairwise RMSD values (Å)c
All backbone atoms	0.02	0.13
All heavy atoms	0.47	0.46
Ramachandran plot statistics from Richardson’s lab (%)
Most favored regions	91.3	84.4
Allowed regions	8.7	15.6
Disallowed regions	0	0

^aAnalyzed for residues 2 to 37.

^bAnalyzed for residues 2 to 35.

^cRMSD values are mean values.