TABLE 1.
Crystallographic statistics for PDB code 3UWS
Values in parentheses are for the highest resolution shell.
| Data collection | |
| Wavelength (Å) | 0.9793 |
| Space group | P21 |
| Unit cell dimensions a, b, c (Å); β° | 39.11, 108.68, 77.97; β = 94.32° |
| Resolution range (Å) | 28.73–1.70 (1.79–1.70) |
| Unique reflections | 70,913 |
| Rmergea on I (%) | 10.2 (49.0) |
| Rmeasb on I (%) | 11.0 (52.7) |
| Rpimc on I (%) | 4.1 (19.2) |
| I/σI | 15.6 (4.6) |
| Wilson B (Å2) | 15.9 |
| Completeness (%) | 99.6 (99.8) |
| Multiplicity | 7.3 (7.5) |
| Model and refinement | |
| Reflections (total/test) | 70,883/3,577 |
| Rcryst/Rfreed (%) | 14.3/17.5 |
| No. protein residues/atoms | 700/5612 |
| No. of water/EDO molecules | 690/7 |
| ESUe based on Rfree (Å) | 0.095 |
| B-values (Å2) | |
| Average isotropic B (overall) | 20.0 |
| Protein overall | 18.8 |
| All main/side chains | 16.7/20.8 |
| Solvent/EDO | 29.4/35.6 |
| RMSDg | |
| Bond lengths (Å) | 0.01 |
| Bond angles (°) | 1.6 |
| Ramachandran analysis (%) | |
| Favored regions | 97.0 |
| Allowed regions | 3.0 |
| Outliers | 0.0 |
a Rmerge = ΣhklΣi|Ii(hkl) − 〈I(hkl)〉|/Σhkl Σi(hkl).
b Rmeas = Σhkl[N/(N-1)]1/2Σi|Ii(hkl) − 〈I(hkl)〉|/ΣhklΣiIi(hkl).
c Rpim (precision-indicating Rmerge) = Σhkl[(1/(N-1)]1/2 Σi|Ii (hkl) − 〈I(hkl)〉|/ΣhklΣi Ii(hkl) (43), where n is the multiplicity of reflection hkl, and Ii(hkl) and 〈I(hkl)〉 are the intensity of the ith measurement and the average intensity of reflection hkl, respectively (44).
d Rcryst and Rfree = Σ‖Fobs| − |Fcalc‖/Σ|Fobs| for reflections in the working and test sets, respectively, where Fobs and Fcalc are the observed and calculated structure-factor amplitudes, respectively. Rfree is the same as Rcryst but for 5% of the total reflections chosen at random and omitted from structural refinement.
e ESU is the estimated standard uncertainties of atoms.
f The average isotropic B includes TLS and residual B components.
g RMSD, root-mean-square deviation.