Table 4. Statistics of Reflection Data and Structure Refinements. a.
| Ligand | 5a | 6b | 17 |
| Space Group | P41212 | P41212 | P212121 |
| Unit Cell Dimension (Å) | 64.0, 64.0. 47.6 | 63.5, 63.5, 48.3 | 45.7, 47.4, 90.3 |
| Unit Cell Angles(°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Resolution Range (Å) | 47.56 – 1.53 | 38.43 – 1.59 | 33.30 – 1.74 |
| Reflections Observed | 74,444 (10,810) | 97,324 (4,162) | 82,661 (3,111) |
| Unique Reflections | 15,494 (2,197) | 13,794 (663) | 20,971 (951) |
| Reflections Rfree Set | 1,546 | 1,376 | 1,994 |
| Completeness (%) | 99.8 (99.6) | 99.9 (99.3) | 98.7 (83.4) |
| Redundancy | 4.8 (4.9) | 7.1 (6.3) | 3.9 (3.3) |
| <I/σ> | 26.1 (3.8) | 23.3 (1.5) | 11.8 (1.2) |
| CC1/2 (%) | 99.9 (90.5) | 99.9 (51.7) | 99.7 (68.2) |
| Rsymb | 0.048 (0.347) | 0.046 (1.28) | 0.055 (0.693) |
| Rcrysb | 0.195 | 0.207 | 0.209 |
| Rfreeb | 0.216 | 0.230 | 0.247 |
| No. of Amino Acids | 91 | 91 | 179 |
| No. of Protein Atoms | 747 | 743 | 1,457 |
| No. of Hetero Atoms | 33 | 33 | 33 |
| No. of Waters | 89 | 108 | 172 |
| RMSDc Bond Lengths (Å) | 0.012 | 0.006 | 0.013 |
| Angles (°) | 0.937 | 0.971 | 1.217 |
| Mean B Factor | 18.59 | 31.69 | 30.20 |
| Protein Atoms (Å2) | 17.18 | 30.32 | 29.13 |
| Hetero Atoms (Å2) | 21.54 | 38.29 | 31.58 |
| Water Atoms (Å2) | 25.92 | 39.05 | 39.03 |
| Ramachandran Outliers (%) | 0.0 | 0.0 | 0.0 |
| Ramachandran Favored (%) | 100.0 | 100.0 | 100.0 |
a
The numbers in parentheses represent values from the highest resolution shell: caS100B•5a (1.61-1.53Å), CaS100B•6b (1.62-1.59Å), and CaS100B•17 (1.77-1.59Å).
b
Rsym = Σ h(Σ j|Ihj - <Ih>|/ Σ Ihj), where h=set of Miller indices, j=set of observations of reflection h, and <Ih>=the mean intensity. Rcrys= Σh||Fo,h| – |Fc,h||/ Σh|Fo,h|. Rfree was calculated using a percentage of the complete data set excluded from refinement.
c
RMSD values are deviation from ideal values