5N5O
Structure of SARS coronavirus main protease in complex with the alpha-ketoamide (S)-N-benzyl-3-((S)-2-cinnamamido-3-cyclopropylpropanamido)-2-oxo-4-((S)-2-oxopyrrolidin-3-yl)butanamide (Cinnamoyl-cyclopropylalanine-GlnLactam-CO-CO-NH-benzyl)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PETRA III, DESY BEAMLINE P11 |
Synchrotron site | PETRA III, DESY |
Beamline | P11 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-05-25 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9919 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 109.165, 81.873, 53.499 |
Unit cell angles | 90.00, 104.34, 90.00 |
Refinement procedure
Resolution | 43.830 - 2.000 |
R-factor | 0.19512 |
Rwork | 0.192 |
R-free | 0.25152 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | SARS-CoV main protease |
RMSD bond length | 0.018 |
RMSD bond angle | 1.908 |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.830 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.060 | 0.507 |
Rpim | 0.039 | 0.331 |
Number of reflections | 30329 | 4358 |
<I/σ(I)> | 10.5 | 2.4 |
Completeness [%] | 98.3 | 97.4 |
Redundancy | 3.3 | 3.3 |
CC(1/2) | 0.997 | 0.804 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 6 - 8% polyethylene glycol 6000, 0.1 M MES, pH 6.0 |