From: Structure of the catalytic domain of the colistin resistance enzyme MCR-1
cMCR-1 (PDB ID 5K4P) | |
---|---|
Data collection | |
Space group | P43212 |
Cell dimensions | |
a, b, c, Å | 59.1, 59.1, 186.7 |
α, β, γ, ° | 90, 90, 90 |
Wavelength, Å | 1.00 |
Resolution, Åa | 49.9–1.32 (1.39–1.32) |
R merge | 0.057 (0.491) |
R meas | 0.079 (0.892) |
R pim | 0.055 (0.552) |
I/s(I) | 9.6 (1.7) |
CC 1/2 | 0.996 (0.547) |
Completeness, % | 100 (100) |
Redundancy | 14.7 (11.7) |
Refinement | |
Resolution, Å | 49.9–1.32 (1.39–1.32) |
No. reflections | 78753 |
R work/R free | 0.1464/0.1732 |
No. atoms | 2935 |
Protein | 2541 |
Ligand/ion (D-sorbitol/zinc) | 12/10 |
Water | 368 |
B factors, Å2 | |
Protein | 12.1 |
Zinc | 10.8 |
D-sorbitol | 11.3 |
Water | 25.1 |
Root-mean-square deviations | |
Bond lengths, Å | 0.007 |
Bond angles, ° | 0.878 |
MolProbity clash score | 1.00 |