Table 1.
Crystallographic Statistics for Human Carboxylesterase 1 Structures
| Coenzyme A | Homatropine/Palmitate/Coenzme A | Cholate/Palmitate | Taurocholate | |
|---|---|---|---|---|
| Resolution (Å; highest shell) | 30-2.0 (2.0-2.13) | 50-2.8 (3.0-2.8) | 20-3.0 (3.2-3.0) | 31-3.2 (3.4-3.2) |
| Space Group | P21 | P212121 | P212121 | P212121 |
| Asymmetric Unit | One hexamer | One trimer | One trimer | One trimer |
| Cell Constants (Å, °) | a = 88.99 | a=55.56 | a=55.29 | a=55.42 |
| b = 115.37 | b=181.02 | b=179.88 | b=179.95 | |
| c = 175.53 | c=202.56 | c=201.32 | c=201.09 | |
| β = 90.05 | ||||
| Data Collection Facilities | SSRL | SSRL | UNC | SSRL |
| Total Reflections | 1798533 | 238528 | 499077 | 125478 |
| Unique Reflections | 233023 | 50837 | 38284 | 34194 |
| Mean Redundancy | 7.7 | 4.7 | 13.0 | 3.7 |
| Rsym1 (%; highest shell) | 8.2 (33.5) | 12.3 (34.1) | 11.0 (34.1) | 14.4 (40.8) |
| Wilson B factor (Å2) | 21.6 | 48.4 | 47.8 | 45.6 |
| Completeness (%; highest shell) | 97.1 (88.1) | 99.1 (99.7) | 93.0 (83.6) | 98.6 (97.6) |
| Mean I/σ ( highest shell) | 12.7 (2.9) | 8.5 (2.8) | 7.8 (2.4) | 8.5 (3.0) |
| Rcryst2 (%; highest shell) | 18.4 (24.1) | 19.3 (28.9) | 22.6 (30.2)4 | 21.9 (28.6)4 |
| Rfree3 (%; highest shell) | 22.0 (27.4) | 24.4 (35.5) | 27.1 (35.3)4 | 25.5 (31.5)4 |
| Number Protein Atoms5 | 24726 | 12390 | 12390 | 12390 |
| Number Solvent Sites5 | 2715 | 508 | 269 | 253 |
| Number Carbohydrate | 154 | 105 | 105 | 105 |
| Atoms5 | ||||
| Number Ligand Atoms5 | 288 | 120 | 174 | 210 |
| Number Ion Atoms5 | 60 | 33 | 30 | 30 |
| Bound Ligands | One CoA in each active site | One palmitate in two active sites, One CoA in one active site; One homatropine in each Z site; One palmitate in side door | One palmitate in each active site; One cholate in each Z site | One taurocholate in each active site and each Z site |
1
Rsym = ∑|I−<I>| / ∑I, where I is the observed intensity and <I> is the average intensity of multiple symmetry-related observations of that reflection.
2
Rcryst = ∑||Fobs|−|Fcalc|| / ∑|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively.
3
Rfree = ∑||Fobs|−|Fcalc|| / ∑|Fobs| for 7% of the data not used at any stage of structural refinement.
4
Non-crystallographic symmetry restraints were applied throughout the trimeric complexes except areas (4–6 Å sphere) in contact with ligands.
5
Number of atoms per asymmetric unit.