Table 1.
Crystallographic data for the thrombin mutants Y225F, Y2265P, and Y225I
| Y225F | Y225P | Y225I | |
|---|---|---|---|
| Data collection | |||
| Wavelength, Å | 1.03 | 1.03 | 1.03 |
| Resolution, Å | 30−2.1 | 30−2.1 | 30−2.1 |
| Reflections, observed/unique (I/σ(I) > 1) | 68,774/18,509 | 76,087/17,519 | 72.954/16,825 |
| Completeness*, % | 94.1/89.6 | 88.0/88.2 | 82.9/81.9 |
| Rsym,† % | 4.8/13.1‡ | 4.2/7.1‡ | 4.9/10.4‡ |
| Unit cell dimensions, Å | a = 53.1, b = 75.1, c = 81.4 | a = 53.1, b = 75.1, c = 82.4 | a = 50.6, b = 73.7, c = 89.9 |
| Refinement | |||
| Resolution, Å | 6.0−2.1 | 6.0−2.1 | 6.0−2.1 |
| R factor, % | 19.7 | 19.8 | 22.5 |
| Rfree,§ % | 26.3 | 27.2 | 28.2 |
| Completeness,‡ %, F/σ(F) > 2, working set only§ | 87.5/83.1 | 82.4/81.7 | 78.9/77.6 |
| Number of protein atoms | 2,239 | 2,262 | 2,115 |
| Number of solvent molecules | 141 | 168 | 147 |
| 〈B〉 main chain atoms | 20.9 | 15.7 | 17.8 |
| 〈B〉 side chain atoms and solvent | 24.2 | 20.1 | 20.3 |
| Rmsd bond lengths,¶ Å | 0.010 | 0.010 | 0.011 |
| Rmsd angles,¶ ° | 1.59 | 1.57 | 1.58 |
| Rmsd in B for bonded atoms main chaine | 1.4 | 1.3 | 1.6 |
| Rmsd in B for bonded atoms side chaine | 2.6 | 2.4 | 2.5 |
*
Percentage of: overall completeness/completeness in the last resolution shell (2.18−2.10 Å).
†
Defined as Σ |I − 〈I〉|/Σ I, where I is the observed intensity and 〈I〉 is the average intensity from multiple observations of symmetry related reflections.
‡
Rsym for: overall resolution range/last resolution shell (2.18−2.10 Å).
§
Calculated using 6.5% (Y225F and Y225P) and 4.0% (Y225I) data sets.
¶
rms deviation (Rmsd) from ideal bond lengths and angles (25) and Rmsd in B factors of bonded atoms.