Table 1.
Experimental Data and Structural Statistics of the 30 conformers representing the solution structure of M-Rep2-95.
| A. NMR-derived constraints | ||||
|---|---|---|---|---|
| Total interproton | 1248 | |||
| Intraresidue | 177 | |||
| Sequential (i-j=l) | 340 | |||
| Short range (l<i-j<5) | 168 | |||
| Long range (i-j>4) | 563 | |||
| Total dihedral angles | 110 | |||
| φ | 52 | |||
| ϕ | 52 | |||
| χ1 | 6 | |||
| Total number of constraints | 1358 | |||
| Total number of constraints per residue | 14.8 | |||
| B. Structural Quality
| ||||
| 1. Residual violationsa
| ||||
| Upper limits | Lower limits | Van der Waals | Torsions | |
|
| ||||
| Number of violationsb | 19±6 (8;33) | 0±0 (0;0) | 11±2(7;15) | 0±0 (0;1) |
| Maximum violation | 0.27 ±0.06 (0.17;0.39) | 0.02 ±0.01 (0.01;0.04) | 0.21 ±0.03 (0.17;0.31) | 3.76±1.08 (2.62;8.12) |
|
| ||||
| CYANA target function (Å2) | 1.77±0.23 (1.32;2.17) | |||
|
| ||||
| 2. Ramachandran statisticsc
| ||||
| 30-conformer ensemble | Regularized mean structure | |||
|
| ||||
| Residues in most favoured regions | 75.5/81.7 | 76.3/82.1 | ||
| Residues in additional allowed regions | 19.9/16.5 | 19.7/16.1 | ||
| Residues in generously allowed regions | 3.3/1.8 | 2.6/1.8 | ||
| Residues in disallowed regions | 1.3/0.0 | 1.3/0.0 | ||
|
| ||||
| C. Coordinate precision (Å, mean/pairwise)d
| ||||
| Folded domaine | Well-defined residuese | |||
|
| ||||
| N, Cα, C′ | 0.50±0.13/0.75±0.17 (0.32;0.83)/(0.31;1.24) | 0.23±0.05/0.40±0.08 (0.16;0.33)/(0.19;0.67) | ||
| All heavy atoms | 0.95±0.13/1.37±0.17 (0.78;1.28)/(0.88;1.79) | 0.70±0.12/1.03±0.15 (0.52;0.97)/(0.66;1.41) | ||
Average values, standard deviation, and maximum and minimum values (in brackets) for the 30 conformer ensemble. Upper limit, lower limit, and van der Waals violations are given in Å, and torsion violations in degrees.
Number of distance constraint violations larger than 0.1 Å (upper limits, lower limits, van der Waals), and torsional constraint violations larger than 5 degrees.
The 76/56 non-Gly, non-Pro residues in the folded/well-defined region 7–118/7–34,39–68,85–118 of the 30 conformers and those of the regularized mean structure are considered separately. Values are in percent.
Average r.m.s difference between the 30 conformer ensemble and the regularized mean structure/pairwise r.m.s difference between members of the ensemble.
The folded domain consists of 90 residues (5–94), excluding flexible N- and C-tails. The well-defined 70 residues include the folded domain except 20 residues (35–38 & 69–84) located in flexible loops.