6U7P
HIV-1 wild type protease with GRL-03119A, with phenyl-boronic-acid as P2'-ligand and with a hexahydro-4H-furo-pyran as the P2-ligand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-08-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 58.491, 86.097, 46.086 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.690 - 1.130 |
| R-factor | 0.1258 |
| Rwork | 0.125 |
| R-free | 0.14050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3nu3 |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.517 |
| Data reduction software | HKL-2000 (0.716.1) |
| Data scaling software | HKL-2000 (0.716.1) |
| Phasing software | PHASER (4.064 Datablock id: mmcif_pdbx.dic) |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.170 |
| High resolution limit [Å] | 1.130 | 2.430 | 1.130 |
| Rmerge | 0.061 | 0.053 | 0.445 |
| Rmeas | 0.066 | 0.058 | 0.564 |
| Rpim | 0.026 | 0.023 | 0.341 |
| Total number of observations | 456362 | ||
| Number of reflections | 79649 | 9081 | 4384 |
| <I/σ(I)> | 14.8 | ||
| Completeness [%] | 90.8 | 98.8 | 50.7 |
| Redundancy | 5.7 | 6.3 | 2 |
| CC(1/2) | 0.996 | 0.735 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 298 | 1.3 M sodium chloride, 0.1 M sodium acetate pH 6.2 |
