Table 2.
Crystal data, X-ray diffraction, and structures
| HPPK•17 | HPPK•18 | HPPK•19 | |
|---|---|---|---|
|
| |||
| PDB Entry Code | 3UD5 | 3UDE | 3UDV |
| Crystal | |||
| Space group | C2 | P21212 | P21212 |
| Unit cell parameters: a (Å) | 79.98 | 52.91 | 53.00 |
| b (Å) | 52.77 | 70.98 | 70.64 |
| c (Å) | 36.69 | 36.38 | 36.25 |
| β (°) | 102.70 | 90 | 90 |
| Matthews coefficient (Å3/Da) | 2.1 | 1.9 | 1.9 |
|
| |||
| Data | Overall (last shell) | Overall (last shell) | Overall (last shell) |
| Resolution (Å) | 30.00–1.90 (1.97–1.90) | 30.00–1.82 (1.89–1.82) | 30.00–1.79 (1.85–1.79) |
| Unique reflections | 10236 (717) | 11525 (650) | 11716 (658) |
| Redundancy | 6.5 (5.3) | 6.1 (2.5) | 6.0 (2.8) |
| Completeness (%) | 87.0 (61.7) | 89.7 (51.9) | 87.6 (50.4) |
| Rmergea | 0.089 (0.320) | 0.084 (0.561) | 0.074 (0.322) |
| I/σ | 16.2 (3.8) | 16.7 (1.3) | 19.1 (2.3) |
|
| |||
| Refinement | Overall (last shell) | Overall (last shell) | Overall (last shell) |
| Resolution (Å) | 29.84–2.00 (2.13–2.00) | 29.48–1.88 (1.98–1.88) | 29.92–1.88 (1.98–1.88) |
| Unique reflections | 9252 (1203) | 10902 (1180) | 10754 (1150) |
| Completeness (%) | 90.7 (72.0) | 93.5 (73.0) | 92.8 (72.0) |
| Data in the test set | 824 (107) | 949 (104) | 920 (98) |
| R-work | 0.158 (0.164) | 0.178 (0.243) | 0.210 (0.253) |
| R-free | 0.205 (0.262) | 0.237 (0.309) | 0.275 (0.288) |
|
| |||
| Structure | |||
| Protein non-H atoms/B (Å2) | 1448/30.0 | 1389/28.1 | 1399/26.4 |
| Ligand atoms/B (Å2) | 49/44.4 | 47/31.3 | 48/40.7 |
| Water oxygen atoms/B (Å2) | 106/38.3 | 88/36.1 | 91/32.8 |
| Rmsd | |||
| Bond lengths (Å) | 0.012 | 0.012 | 0.013 |
| Bond angles (°) | 1.302 | 1.382 | 1.376 |
| Coordinate error (Å) | 0.54 | 0.50 | 0.48 |
| Ramachandran plotb | |||
| Favored regions (%) | 98.7 | 97.3 | 97.3 |
| Disallowed regions (%) | 0.0 | 0.0 | 0.0 |
a
Rmerge = Σ|(I-<I>)|/Σ(I), where I is the observed intensity.
b
Obtained using Ramachandran data by Lovell and coworkers.52