Table 1. Input for the structure calculation and characterization of the energy-minimized NMR solution structures of tPrP(121–225), chPrP(121–225), and xlPrP(90–222).
| Quantity* | chPrP(121–225) | tPrP(121–225) | xlPrP(90–222) |
|---|---|---|---|
| NOE upper distance limits | 1,889 | 1,522 | 2,283 |
| Dihedral angle constraints | 123 | 110 | – |
| Residual target function value, Å2 | 1.62 ± 0.20 | 1.75 ± 0.18 | 1.99 ± 0,19 |
| Residual distance constraint violations | |||
| Number > 0.1 Å | 29 ± 2 | 30 ± 4 | 24 ± 4 |
| Maximum, Å | 0.16 ± 0.03 | 0.14 ± 0.01 | 0.14 ± 0.01 |
| Residual dihedral angle constraint violations | |||
| Number > 2.0° | 1 ± 1 | 0 | – |
| Maximum, ° | 2.13 ± 0.80 | 1.21 ± 0.71 | – |
| Amber energies, kcal/mol | |||
| Total | –4,633 ± 98 | –4,694 ± 69 | –5,215 ± 60 |
| van der Waals | –285 ± 17 | –309 ± 16 | –244 ± 17 |
| Electrostatic | –5,285 ± 94 | –5,265 ± 74 | –6,032 ± 59 |
| rms deviation to the averaged coordinates (Å)† | |||
| Backbone (N, Cα, C′) | 0.72 ± 0.14 | 0.85 ± 0.13 | 0.75 ± 0.13 |
| (135–200, 211–237) | (125–224) | (127–166, 172–225) | |
| All heavy atoms | 1.17 ± 0.13 | 1.33 ± 0.15 | 1.19 ± 0.12 |
*
Except for the top two entries, the average for the 20 conformers with the lowest residual dyana target function values and the standard deviation among them are given. NOE, nuclear Overhauser enhancement
†
The numbers in parentheses identify the polypeptide segments for which the rms deviation was calculated