1HVS
STRUCTURAL BASIS OF DRUG RESISTANCE FOR THE V82A MUTANT OF HIV-1 PROTEASE: BACKBONE FLEXIBILITY AND SUBSITE REPACKING
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.900, 59.600, 62.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 2.250 |
R-factor | 0.15 |
Rwork | 0.150 |
RMSD bond length | 0.015 |
RMSD bond angle | 3.100 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 7.000 * |
High resolution limit [Å] | 2.250 * |
Rmerge | 0.078 * |
Total number of observations | 20561 * |
Number of reflections | 7262 * |
Completeness [%] | 69.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | complex of V82A | 3 (mg/ml) | |
2 | 1 | drop | A-77003 | ||
3 | 1 | drop | sodium acetate | 50 (mM) | |
4 | 1 | drop | DTT | 10 (mM) | |
5 | 1 | drop | DMSO | 10 (%) | |
6 | 1 | reservoir | sodium citrate | 66 (mM) | |
7 | 1 | reservoir | sodium phosphate | 132 (mM) | |
8 | 1 | reservoir | ammonium sulfate | 34 (%sat) |