Table I.
Codea | Resb (Å) | Lenc | pHd | Compound | Timee (s) | Atomsf | Agreeg (%) |
---|---|---|---|---|---|---|---|
1EJG26 | 0.54 | 46 | 7.0 | Crambin | 0.9 | 31 | 87 |
1GCI27 | 0.78 | 269 | 5.9 | Subtilisin | 11.3 | 185 | 99 |
1GDN28 | 0.81 | 242 | 6.0 | Trypsin | 19.0 | 167 | 85 |
1P9G29 | 0.84 | 41 | 5.5 | Antifungal protein | 0.9 | 20 | 90 |
1UCS30 | 0.62 | 64 | 7.5 | Antifreeze protein RD1 | 1.3 | 76 | 91 |
1YK431 | 0.69 | 53 | 6.0 | Rubredoxin | 1.5 | 56 | 88 |
2B9732 | 0.75 | 140 | 7.4 | Hydrophobin II | 2.2 | 128 | 89 |
2H5C33 | 0.82 | 198 | 4.3 | Alphalytic protease | 9.0 | 163 | 85 |
3PYP34 | 0.85 | 125 | 4.8 | Photoactive yellow protein | 4.1 | 119 | 95 |
Superscripts denote manuscript references.
Resolution (Å) of the X-ray diffraction.
Number of residues of the main macromolecular chain.
pH is taken from the PDB header (crystallization conditions).
Run time of Protonate3D in seconds on a 2 GHz Pentium IV.
Number of –;OH, –SH, –NHi, –CH3, –CO2, N(his) atoms with hydrogen occupancy ≥0.8.
The percentage agreement of hydrogen placement to within 15° dihedral angle of experiment.