Table 1.
Crystallographic data for the thrombin-protein C fragment complex
| Buffer | 0.1M Tris, pH 8.5, 0.2M CH3COONa |
| PEG | 4000 (30%) |
| PDB ID | 4DT7 |
| Data collection | Raxis IV++ |
| Wavelength, Å | 1.5418 |
| Space group | P21 |
| Unit cell dimensions, Å | a = 46.4, b = 84.3, c = 66.4 β = 94.6° |
| Molecules/asymmetric unit | 2 |
| Resolution range, Å | 40-1.9 |
| Observations | 140 938 |
| Unique observations | 38 884 |
| Completeness, % | 97.8 (81.1) |
| Rsym, % | 8.3 (34.0) |
| I/σ(I) | 13.4 (2.4) |
| Refinement | |
| Resolution, Å | 40-1.9 |
| Rcryst, Rfree | 0.175, 0.218 |
| Reflections (working/test) | 34 903/1953 |
| Protein atoms | 4755 |
| Na+ | 2 |
| Solvent molecules | 326 |
| Rmsd bond lengths, Å | 0.010 |
| Rmsd angles, degrees | 1.2 |
| Rmsd ΔB (Å2), mm/ms/ssb | 2.11/1.32/2.28 |
| protein, Å2 | 30.0 |
| Na+, Å2 | 26.3 |
| solvent, Å2 | 36.9 |
| Ramachandran plot | |
| Most favored, % | 99.2 |
| Generously allowed, % | 0.2 |
| Disallowed, % | 0.6 |
Rmsd indicates root-mean-squared deviation from ideal bond lengths and angles and Rmsd in B-factors of bonded atoms; mm, main chain-main chain; ms, main chain-side chain; and ss, side chain-side chain.