TABLE 1.
Crystallographic data for Gla-domainless prothrombin mutant S525A
NAG, n-acetylglucosamine.
| Buffer | 100 mm Tris, pH 8.5 |
| PEG | 8000 (25%) |
| PDB ID | 4HZH |
| Data collection | |
| Wavelength (Å) | 1.5418 |
| Space group | P212121 |
| Unit cell dimensions (Å) | a = 82.6, b = 103.1, c = 149.5 |
| Molecules/asymmetric unit | 2 |
| Resolution range (Å) | 40-3.3 |
| Observations | 74,483 |
| Unique observations | 19,155 |
| Completeness (%) | 96.9 (93.1) |
| Rsym (%) | 18.0 (44.9) |
| I/σ(I) | 5.4 (2.1) |
| Refinement | |
| Resolution (Å) | 40-3.3 |
| Rcryst, Rfree | 0.294, 0.329 |
| Reflections (working/test) | 18,011/980 |
| Protein atoms | 6880 |
| NAG molecules | 4 |
| r.m.s.d. bond lengthsa (Å) | 0.007 |
| r.m.s.d. anglesa (°) | 1.2 |
| r.m.s.d. ΔB (Å2) (mm/ms/ss)b | 0.74/0.06/0.28 |
| 〈B〉 protein (Å2) | 58.4 |
| 〈B〉 NAG (Å2) | 54.5 |
| Ramachandran plot | |
| Most favored(%) | 95.0 |
| Generously allowed (%) | 3.3 |
| Disallowed (%) | 1.6 |
a Root mean squared deviation (r.m.s.d.) from ideal bond lengths and angles and r.m.s.d. in B-factors of bonded atoms.
b mm, main chain-main chain; ms, main chain-side chain; ss, side chain-side chain.