Table 1.

Statistics for PRE-based, Bound GlnBP Structures Calculated via Different Simulated Annealing Protocols^a

Optimization type	Simultaneousb		Sequentiac
Probe representation	1 conformer	3 conformers	3 conformers
Overall Q (163)d	0.25 ± 0.00	0.23 ± 0.00	0.22 ± 0.00
Intra-domain Q (86)d	0.25 ± 0.01	0.22 ± 0.01	0.20 ± 0.00
Inter-domain Q (67)d	0.24 ± 0.00	0.23 ± 0.01	0.23 ± 0.00
RMSD (Å)e	2.9 ± 0.6	6.5 ±0.9	2.5 ± 0.2
51–117 distance (6.6) (Å)f	8.3 ±0.4	10.4 ± 0.7	7.2 ±0.2
51–138 distance (7.7) (Å)f	9.0 ± 0.4	12.2 ±0.5	9.2 ±0.2
Rgyr(17.5)(Å)g	17.9 ±0.1	18.2 ±0.1	17.8 ±0.1

^aThe 10 lowest-PRE energy structures out of 200 are considered.

^bSimultaneous optimization of paramagnetic probe conformer(s) and protein backbone.

^cOptimization of paramagnetic probe conformations, followed by optimization of protein backbone.

^dAverage PRE Q-factor for corresponding data set (number of restraints indicated in parenthesis).

^eAverage pairwise backbone (N, C^α, C’) RMSD of the small domain relative to the X-ray coordinates of the bound conformation (PDB ID: 1WDN), after superimposition of the large domain. RMSD calculation excludes residue segment 98–110 (see text).

^fAverage H^N–H^N separation distance of indicated residues (target value from 1WDN coordinates indicated in parenthesis).

^gAverage radius of gyration calculated from backbone (N, C^α, C’) atoms (target value from 1WDN coordinates indicated in parenthesis).