Table 3. Crystallographic Data and Refinement Statistics of TbPTR1−Ligand Complexesa.
| ligand complex | 4 | 5 | 9 | 12 |
|---|---|---|---|---|
| Details of Data Collection | ||||
| PDB code | 2WD7 | 3GN1 | 3GN2 | 2WD8 |
| space group | P21 | P21 | P21 | P21 |
| unit cell dimensions (Å) | a = 74.68 | a = 74.64 | a = 74.89 | a = 74.66 |
| b = 89.89 | b = 90.41 | b = 90.78 | b = 89.89 | |
| c = 82.70 | c = 82.64 | c = 82.86 | c = 83.05 | |
| β = 115.48 | β = 115.73 | β = 115.85 | β = 115.54 | |
| resolution range (Å) | 30.0−1.90 | 30.66−2.00 | 67.42−1.60 | 30.0−2.10 |
| (2.0−1.90) | (2.10−2.00) | (1.69−1.60) | (2.18−2.10) | |
| observations | 147241 | 341528 | 522950 | 118137 |
| unique observations | 71041 | 63246 | 124512 | 48991 |
| redundancy | 2.1 | 5.4 | 4.2 | 2.4 |
| completeness (%) | 91.6 (63.8) | 94.8 (89.9) | 94.9 (93.7) | 84.7 (84.9) |
| ⟨I/σ(I)⟩ | 13.0 (2.4) | 9.3 (5.1) | 8.3 (2.0) | 11.5 (2.43) |
| Rmergeb (%) | 5.4 (31.1) | 5.1 (13.6) | 6.7 (35.9) | 9.4 (56.9) |
| Refinement Statistics | ||||
| resolution range (Å) | 30.0−1.9 | 30.66−2.00 | 67.42−1.60 | 30.0−2.10 |
| R factorc % (Rwork/Rfree) | 15.5/20.2 | 15.5/21.6 | 14.6/17.8 | 15.8/22.6 |
| number of atomsd | 7545/195/88/687 | 7480/192/20/896 | 7568/192/95/1272 | 7453/144/100/733 |
| mean B factore (Å2) | 26/21/27/35 | 12/9/26/21 | 11/8/11/27 | 30/30/28/41 |
| rms bond length deviation (Å) | 0.016 | 0.014 | 0.009 | 0.012 |
| rms bond angle deviation (deg) | 1.627 | 1.473 | 1.293 | 1.419 |
a
Values between brackets are for the highest resolution shell.
b
Rmerge = ∑|I − ⟨I⟩|/∑⟨I⟩.
c
R factor = ∑ Fo− Fc|/∑ Fo.
d
Number of atoms of protein, cofactor, ligand, and water molecules, respectively.
e
Mean B factor for protein, cofactor, ligand, and water molecules, respectively