Table 1.
Data collection and refinement statistics for SeCcmP
Values in parentheses are for the outer resolution shell.
| SeCcmP_P2 1 3 | SeCcmP_I2 1 3 | |
|---|---|---|
| Protein Data Bank id | 5LT5 | 5LSR |
| Data collection | ||
| Beam line | ID29 | ID29 |
| Wavelength (Å) | 0.97239 | 0.97625 |
| Space group | P213 | I213 |
| Unit cell parameters (Å) | a, b, c=107.2; α, β, γ=90° | a, b, c=178.7; α, β, γ=90° |
| V M (Å3 Da–1) | 2.1 | 3.4 |
| Solvent content (%) | 42 | 64 |
| Resolution (Å) | 47.9–1.45 (1.47–1.45) | 44.7–1.65 (1.68–1.65) |
| No. of observations | 721 918 (34 433) | 2 272 675 (98 426) |
| No. of unique reflections | 72 625 (3579) | 113 271 (5592) |
| R meas a | 0.061 (0.943) | 0.095 (1.445) |
| <I/(σI)> | 21.7 (2.6) | 18.9 (2.3) |
| Completeness (%) | 100.0 (100.0) | 100.0 (100.0) |
| Multiplicity | 9.9 (9.6) | 20.1 (17.6) |
| Refinement | ||
| Resolution range (Å) | 47.9–1.45 (1.49–1.45) | 44.7–1.65 (1.69–1.65) |
| No. of reflections | 72 565 | 113 268 |
| R work b | 0.165 | 0.181 |
| R free c | 0.184 | 0.191 |
| No. of atoms | ||
| Protein | 3246 | 4774 |
| Ligands | 13 | 6 |
| Waters | 325 | 357 |
| Average B-values (Å2) | ||
| Estimated from Wilson plot | 19.2 | 29.2 |
| Protein | 20.1 | 32.1 |
| Ligands | 26.1 | 37.2 |
| Waters | 33.1 | 39.8 |
| Rms deviations from ideal values | ||
| Bond lengths (Å) | 0.010 | 0.010 |
| Bond angles (°) | 1.05 | 1.03 |
| Ramachandran analysisd | ||
| Outliers (%) | 0 | 0 |
a R meas=∑h ∑l (nh/nh−1)1/2|Ihl−<Ih>|/∑h ∑l<Ih> (Evans, 2006; Evans and Murshudov, 2013).
b R work=∑hkl||Fo|−|Fc||/∑hkl |Fo| where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
c R free calculated from a randomly chosen 5% of all unique reflections.
dFrom MolProbity (Chen et al., 2010).