TABLE 3.
Data collection and refinement statistics
| Parametera | Value(s) for the peptideb |
|---|---|
| Data collection statistics | |
| Space group | P1 |
| Unit cell dimensions | |
| a, b, c (Å) | 54.97, 56.19, 77.15 |
| α, β, γ (°) | 90.34, 90.18, 94.98 |
| Resolution range (Å) | 25.0–1.98 |
| No. of molecules in the asymmetric unit | 2 |
| No. of unique observations | 59,746 |
| Multiplicity | 2.9 (1.9) |
| Completeness (%) | 93.0 (81.7) |
| Rmerge | 0.077 (0.476) |
| I/σ(I) | 15.9 (1.7) |
| Refinement statistics | |
| Resolution range (Å) | 15.0–19.8 |
| Rfactor/Rfreec | 0.224/0.267 |
| No. of protein/peptide atoms | 13,092 |
| No. of water molecules | 510 |
| RMSD from ideal structure | |
| Bond length (Å) | 0.0020 |
| Bond angle (°) | 1.30 |
a
Rmerge = ΣhklΣi|Ii(hkl) − <I(hkl)>|/ΣhklΣiIi(hkl), where Ii(hkl) is the intensity of an observation and <I(hkl)> is the mean value for its unique reflection; summations are over all reflections. Rfactor = Σh|Fo(h) − Fc(h)|/ΣhFo(h), where Fo and Fc are the observed and calculated structure-factor amplitudes, respectively.
b
Values in parentheses refer to the 2.05- to 1.98-Å-resolution shell.
c
Rfree was calculated with 5% of the data excluded from the refinement.