Table 1.
Crystallographic data.
| Dataset | Kgp·KYT-36 |
|---|---|
| Data processing | |
| Space group | P212121 |
| Cell constants (a, b, c, in Å) | 86.67, 87.05, 129.21 |
| Wavelength (Å) | 0.97949 |
| No. of measurements/unique reflections | 2,922,120/290,672 |
| Resolution range (Å) | 72.2 – 1.20 (1.27 – 1.20)a |
| Completeness (%) | 95.8 (75.2) |
| Rmerge | 0.065 (0.726) |
| Rmeas/CC1/2 | 0.068 (0.800)/1.000 (0.843) |
| <I/σ(I)> of unique reflections after merging | 19.6 (2.9) |
| B-Factor (Wilson) (Å2)/Aver. Multiplicity | 15.9/10.1 (5.2) |
| Structure refinement | |
| Resolution range used for refinement (Å) | 72.2 – 1.20 |
| No. of reflections used (test set) | 289,551 (1120) |
| Crystallographic Rfactor (free Rfactor) | 0.146 (0.148)b |
| No. of protein residues + atoms/solvent molecules/ligandsc | 906 + 7,048/1,580/2 K36, 4 Ca2+, 4 Na+, 4 UNK, 1 DTT, 6 GOL, 2 EPE |
| Correlation coefficient Fobs-Fcalc | 0.962b |
| Rmsd from target valuesb | |
| bonds (Å)/angles (°) | 0.012/1.17 |
| Average B-factors (Å2) (all// molec. A/B) | 16.3//13.2/13.3 |
| Overall anisotropic B-value (B11, B22, B33, in Å2) | 1.04, −3.67, 2.64 |
| All-atom contacts and geometry analysisd | |
| Protein residues in favored regions/outliers/all residues | 915e (97%)/6f/947e |
| Protein residues with outlying rotamers/bonds/angles/chirality/planarity | 2/0/0/0/0 |
| All-atom clashscore | 2.7 |
aData processing values in parenthesis are for the outermost resolution shell. bAccording to the final BUSTER/TNT refinement step. cK36, KYT-36; DTT, (2S,3S)-1,4-bis(sulfanyl)butane-2,3-diol; GOL, glycerol; UNK, unknown atoms/ions; and EPE, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES.). dwwPDB X-ray Structure Validation Report. eIncluding residues with atoms in two positions. fAll outliers are unambiguously resolved in the final Fourier map.