Table 1. Crystallographic data and refinement statistics.
| Data set | Thrombin:s-variegin complex | |
| Crystal | ||
| Space Group | P1 | C2 |
| Unit Cell Parameters (Å, °) | a = 50.8 | A = 124.7 |
| b = 61.58 | B = 50.8 | |
| c = 67.3 Å | C = 61.5 Å | |
| α = 98.1 | AL = 90 | |
| β = 112.2 | BE = 98.7 | |
| γ = 89.9° | GA = 90° | |
| Data collection | ||
| Resolution range (Å) | 50−2.4 | |
| Wavelength (Å) | 0.9795 | |
| Total number of reflections | 52,825 | |
| Unique reflections | 29,154 | 15,137 |
| Completeness (%) | 88.1 (56.8) | 98.1 (97.0) |
| I/σI | 25.1 (7.0) | 20.0 (5.4) |
| Redundancy | 1.9 (1.7) | 3.6 (3.1) |
| Rmerge (%) | 2.4 (8.5) | 5.3 (15.4) |
| Refinement and quality | ||
| Resolution range (Å) I>σ(I) | 8−2.4 | |
| Rwork | 0.208 | |
| Rfree | 0.259 | |
| RMSD bond lengths (Å) | 0.01 | |
| RMSD bond angles(°) | 1.22 | |
| Average B-factors (Å2) | ||
| Protein atoms (2450 atoms) | 67.4 | |
| Water molecules (51 atoms) | 66.2 | |
| Ramachandran plot | ||
| Most favored regions (%) | 86.1 | |
| Additional allowed regions (%) | 13.9 | |
| Generously allowed regions (%) | 0 | |
| Disallowed regions (%) | 0 | |
Values in parentheses are for the last resolution shell (2.46−2.40 Å). The diffraction data were processed under the space group P1 and transformed to the space group C2 using the transformation A = 2c+a, B = a and C = b, where a,b,c and A,B,C are the P1 and C2 unit-cell vectors, respectively.