Table 1.
Data collection and refinement statistics (molecular replacement)
| Mamu-B*098:lyso-PC16:0 | Mamu-B*098:lyso-PE16:0 | Mamu-B*098:MG16:0 | Mamu-B*05104:lyso-PC16:0 | |
|---|---|---|---|---|
| Data collection | ||||
| Space group | C2 | C2 | C2 | P21 21 21 |
| Cell dimensions | ||||
| a, b, c (Å) | 251.44, 46.44, 84.93 | 251.88, 46.73, 84.98 | 252.54, 46.90, 85.09 | 54.451, 81.028, 106.108 |
| α, β, γ (degrees) | 90.0, 90.9, 90.0 | 90.0, 90.8, 90.0 | 90.0, 90.8, 90.0 | 90, 90, 90 |
| Resolution (Å) | 50–1.87 (1.90–1.87)a | 50–1.87 (1.83–1.80) | 50–1.69 (1.73–1.69) | 50–2.15 (2.19–2.15) |
| Rmerge | 0.048 (0.362) | 0.054 (0.254) | 0.056 (0.403) | 0.061 (0.363) |
| I/σI | 33.4 (3.66) | 46.3 (5.94) | 39.0 (4.21) | 32.3 (4.83) |
| Completeness (%) | 99.5 (98.8) | 99.1 (98.0) | 98.5 (97.5) | 96.0 (92.5) |
| Redundancy | 3.9 (3.5) | 6.2 (5.7) | 4.4 (4.2) | 7.7 (7.7) |
| Refinement | ||||
| Resolution (Å) | 1.87 (1.90–1.87) | 1.80 (1.82–1.80) | 1.69 (1.71–1.69) | 2.150 (2.23−2.15) |
| No. of reflections | 76,941 (2451) | 86,953 (2687) | 103,819 (2992) | 25,216 (2417) |
| Rwork/Rfree (%) | 19.4 (26.3)/23.0 (34.4) | 19.1 (23.9)/22.9 (29.0) | 19.5 (27.1)/22.7 (33.6) | 18.19 (22.63)/23.15 (33.38) |
| No. of atoms | ||||
| Protein | 6219 | 6266 | 6377 | 3131 |
| EKG/metal ion/EDO/buffer molecule | 46/6/128/0 | 69/9/104/16 | 69/8/172/0 | 23/1/32/0 |
| Water | 412 | 505 | 587 | 209 |
| B-Factors (Å2) | ||||
| Protein | 33.8 | 29.1 | 28.5 | 35.51 |
| Ligand and ion | 42.1 | 38.1 | 39.9 | 47.16 |
| Water | 36.2 | 33.8 | 33.9 | 37.15 |
| RMSDs | ||||
| Bond lengths (Å) | 0.009 | 0.007 | 0.008 | 0.008 |
| Bond angles (degrees) | 1.012 | 0.937 | 1.201 | 0.96 |
| Ramachandran plot | ||||
| Favored (%) | 98.53 | 98.79 | 98.39 | 98.12 |
| Outliers (%) | 0.0 | 0.0 | 0 | 0.0 |
a The highest-resolution shell is shown in parentheses.