Table 1.
Structure Determination and Refinement Statistics
| Data Collection and processing | ||
|---|---|---|
| SEK | SEK–hVβ5.1 | |
| Space group | P21 | P212121 |
| Resolution (Å) | 1.56 | 2.40 |
| Molecules/asymmetric unit | 2 SEK | 1 SEK/1 hVβ5.1 |
| Observations | 226,878 | 176,078 |
| Unique reflections | 63,074 | 21,526 |
| Completeness (%)a | 99.8 (99.0) | 99.9 (100.0) |
| Redundancya | 3.6 (2.8) | 8.2 (7.9) |
| Rsym (%)b | 8.6 (17.9) | 8.7 (34.1) |
| Mean I/σ(I) | 30.9 (5.9) | 25.9 (6.1) |
| Refinement | ||
| Rcryst (%)c | 16.3 | 21.9 |
| Rfree (%)d | 20.2 | 24.0 |
| Protein residues | 434 | 462 |
| Average B values | ||
| SEK | 9.9 | 32.8 |
| hVβ5.1 | 37.7 | |
| Water molecules | 655 | 152 |
| Ramachandran plot | ||
| Core (%) | 87.0 | 84.5 |
| Allowed (%) | 12.2 | 13.5 |
| Generous (%) | 0.8 | 0.7 |
| Disallowed (%) | 0 | 1.2e |
| RMS deviations from ideality | ||
| Bonds (Å) | 0.008 | 0.007 |
| Angles (°) | 1.23 | 1.69 |
| Molecular Characterization | ||
| Intermolecular contacts | ||
| Hydrogen Bonds | 14 | |
| van der Waals interactions | 75 | |
| Buried surface areas | ||
| ΔASAtotal (Å) | 1572 | |
| ΔASApolar (Å) | 920 | |
| ΔASAapolar (Å) | 658 | |
| ΔASAapolar/ΔASApolar (%) | 42 | |
| Shape complementarity | ||
| SC | 0.70 | |
a
Values in parentheses are for the highest resolution shell (1.62-1.56 Å for SEK; 2.49-2.40 Å for SEK-hVβ5.1).
b
Rsym = Σ|((Ihkl − I(hkl))|/(ΣIhkl), where I(hkl) is the mean intensity of all reflections equivalent to hkl by symmetry
c
Rcryst = Σ∥FO| − |FC|/Σ|FO∥, where FC is the calculated structure factor
d
Rfree is calculated as Rcryst using 5.1% (SEK) and 4.7% (SEK-hVβ5.1) of the reflections chosen randomly and omitted from the refinement calculations.
e
Residues in the disallowed region include: Ser134hVβ5.1; Ala136hVβ5.1; Thr202hVβ5.1; Glu225hVβ5.1; and Ser73SEK;