Table 2.
Crystallographic statistics for BPTI complexes of rat trypsin and trypsinogen mutants
| ΔI16V17 trypsinogen | ΔI16V17/D194N trypsinogen | ΔI16V17/Q156K trypsinogen | K15A trypsinogen | |
| Data Collection | ||||
| Molecules per asymmetric unit | 1 | 1 | 1 | 1 |
| Space group | P3221 | P3221 | P3221 | P3221 |
| Unit cell | a = b = 92.60 | a = b = 92.53 | a = b = 92.57 | a = b = 92.70 |
| Dimensions (Å) | c = 62.06 | c = 62.07 | c = 62.13 | c = 62.08 |
| Resolution range (Å) | 10–1.7 | 10–1.7 | 22–1.65 | 20–1.55 |
| Reflections observed | 160,328 | 181,142 | 195,481 | 172,527 |
| Unique reflections | 32,489 | 32,654 | 34897 | 44,058 |
| Rmergea (%) | 5.9 | 5.7 | 5.0 | 5.6 |
| Completeness (%) | 95.2 | 95.8 | 93.7 | 95.7 |
| Refinement | ||||
| Resolution range (Å) | 10–1.7 | 10–1.7 | 22–1.65 | 30–1.55 |
| Reflections used | 29240/3249 | 29389/3265 | 31408/3489 | 38611/4305 |
| (Working/free; F/σ(F) > 0)) | no cutoff | no cutoff | no cutoff | no cutoff |
| Final R factorb (%) | 18.4 | 18.4 | 19.0 | 19.9 |
| Final R free (%) | 21.3 | 21.8 | 22.0 | 20.9 |
| Number of nonhydrogen | 2072 | 2105 | 2071 | 2042 |
| Protein atoms | ||||
| Number of Ca+2 ions | 1 | 1 | 1 | 1 |
| Number of H2O | 232 | 213 | 270 | 153 |
| Number of SO4−2 | 3 | 3 | 0 | 2 |
| Temperature factor model | individual | individual | individual | individual |
| Rms deviations from ideal geometry | ||||
| Bond lengths (Å) | 0.01 | 0.01 | 0.005 | 0.0049 |
| Bonds angles (deg) | 1.5 | 1.6 | 1.3 | 1.3 |
| Improper angles (deg) | 0.82 | 0.89 | 0.78 | 0.76 |
| Dihedral angles (deg) | 26.8 | 27.0 | 25.3 | 25.4 |
a Rmerge = ∑/Ii − 〈I〉 I/∑Ii, where Ii is the scaled intensity of the ith measurement; and 〈I〉 is the mean intensity for that reflection.
b R factor = ∑/Fobs − Fcalc I/∑Fobs for all reflections.