Table 3. Data collection and refinement statistics for structures reported in this publication (see also Table 4).
| pdb id | 5E2L | 5E40 | 5E4N |
|---|---|---|---|
| A. Data collection | |||
| Crystal system | Trigonal | Trigonal | Trigonal |
| Space group | P3221 | P3221 | P3221 |
| Unit cell parameters | |||
| a (Å) | 203.99 | 205.45 | 205.74 |
| b (Å) | 203.99 | 205.45 | 205.74 |
| c (Å) | 66.90 | 66.80 | 66.64 |
| Resolution range (Å)a | 49.00–2.50 (2.57–2.50) | 19.85–2.05 (2.09–2.05) | 47.37–2.05 (2.09–2.05) |
| Resolution where I/σ(I) = 2.0 | 3.00 | 2.48 | 2.61 |
| CC1/2 outer shell | 0.770 | 0.608 | 0.625 |
| Measurements | 620384 | 762663 | 1152805 |
| Unique reflections | 55365 | 101083 | 101243 |
| Redundancy | 11.2 (11.5) | 7.5 (7.5) | 11.4 (11.3) |
| Completeness (%) | 100.0 (100.0) | 99.9 (100.0) | 100.0 (100.0) |
| I/σ(I) | 4.0 (0.9) | 5.4 (0.8) | 4.7 (0.7) |
| Rmerge (%) | 19.0 (85.0) | 14.3 (102.6) | 16.5 (123.3) |
| Wilson B-value (Å2) | 35.6 | 27.5 | 31.5 |
| B. Refinement | |||
| Resolution (Å) | 49.00–2.50 (2.57–2.50) | 19.85–2.05 (2.10–2.05) | 47.37–2.05 (2.10–2.05) |
| Rcryst (%) | 15.6b | 19.4 | 19.9 |
| Rfree (%) | 17.4b | 20.7 | 22.9 |
| Amino acids (chain length 464 residues) | 462 + 458, 7196 atom sites | 462 + 456, 7641 atom sites | 459 + 454, 7606 atom sites |
| Water molecules | 82 | 537 | 541 |
| Other | 2 D-Phe ligands, 2 Mn2+, 5 Cl-, 5 SO42-, 2 glycerol | 2 D-Tyr ligands, 2 Mn2+, 5 SO42-, 1 glycerol | 3 D-Tyr ligands, 2 Mn2+, 4 Cl-, 4 SO42- |
| Mean B (Å2) | |||
| Protein | 36.2 | 27.4 | 31.8 |
| Water | 30.3 | 38.7 | 35.2 |
| Other | 36.1 | 39.2 | 35.3 |
| r.m.s.d. from target values | |||
| Bond lengths (Å) | 0.007 | 0.006 | 0.011 |
| Bond angles (°) | 1.105 | 1.115 | 1.452 |
| Dihedral angles (°) | 5.684 | 5.242 | 5.597 |
| Ramachandran | |||
| Most favoured (%) | 97.6 | 98.0 | 97.0 |
| Allowed (%) | 2.2 | 2.0 | 2.9 |
| Disallowed (%) | 0.2 | 0.0 | 0.1 |
a according to CC1/2>0.5 cutoff;
b intensity-based twin refinement was used.