Table 1.
Data reduction and refinement statistics of CBS p.P49L structure.
| p.P49L CBS variant | |
|---|---|
| PDB entry | 5MMS |
| Data collection | |
| Synchrotron | ESRF (Grenoble, France) |
| Beamline | ID30A-3 |
| Wavelength (Å) | 0.968 |
| Space group | P1 |
| Unit cell | |
| a, b, c (Å) | 86.2, 86.8, 97.8 |
| α, β, γ (°) | 102.7, 103.1, 111.2 |
| Resolution rangea (Å) | 76.35–2.80 (2.90–2.80) |
| Total number of reflections | 121227 (1141) |
| Number of unique reflections | 58862 (571) |
| Completeness (%) | 98.5 (95.6) |
| Multiplicity | 2.1 (2.0) |
| 〈I/σ(I)〉 | 4.8 (1.5) |
| R meas b (%) | 17.4 (68.7) |
| R pim c (%) | 11.2 (45.1) |
| CC 1/2 d (%) | 97.6 (62.1) |
| Wilson B-factor (Å2) | 41.8 |
|
| |
| Refinement | |
| R cryst e (%) | 18.2 (27.2) |
| R free f (%) | 22.1 (33.1) |
| Number of non-H atoms | 16452 |
| Protein | 15916 |
| Ligands | 351 |
| Waters | 185 |
| r.m.s.d bonds (Å) | 0.010 |
| r.m.s.d. angles (°) | 1.12 |
| Protein residues | 2077 |
| Ramachandran plot | |
| Most favoured (%) | 96.6 |
| Allowed (%) | 3.2 |
| Outliers (%) | 0.3 |
| Rotamer outliers (%) | 0.3 |
| Clashscore | 0.46 |
| MolProbity scoreg | 0.88 |
| B-factors (Å2) | 45.4 |
| Protein | 41.3 |
| Ligands | 29.7 |
aInformation in parenthesis refers to the last resolution shell. bRmeas = Σhkl(n/n − 1)1/2Σi | Ihkl,j − 〈Ihkl,j〉 | /ΣhklΣjIhkI,j, where nh denotes multiplicity and j thej-th reflection hkl. cRpim = Σhkl(1/n − 1)1/2Σi | Ihkl,j − 〈Ihkl, j〉 | /ΣhklΣiIhkI,j, where nh denotes multiplicity and j the j-th reflection hkl. dCC1/2 is as described previously [69]. eRcryst = ∑hkl‖Fobs(hkl) | −|Fcalc(hkl)‖/∑hkl|Fobs(hkl)|, where Fobs(hkl) and Fcalc(hkl) are the observed and calculated structure factors for reflection (hkl), respectively. fRfree was calculated as Rcryst but using only 5% of reflections randomly selected and omitted from refinement. gMolProbity score provides a single number that represents the central MolProbity protein quality statistics; it is a log-weighted combination of Clashscore, Ramachandran not favored, and bad side-chain rotamers, giving one number that reflects the crystallographic resolution at which those values would be expected.