7N6V

Crystal structure of HIV-1 Protease multiple mutants PRS17 with Revertant mutation V48G bound to inhibitor Amprenavir

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	2020-02-22
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.0
Spacegroup name	P 61
Unit cell lengths	62.804, 62.804, 82.450
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	32.880 - 1.390
R-factor	0.1623
Rwork	0.160
R-free	0.19810
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5t2z
RMSD bond length	0.018
RMSD bond angle	2.127
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.440
High resolution limit [Å]	1.390	2.990	1.390
Rmerge	0.086	0.075	1.114
Rmeas	0.091	0.079	1.189
Rpim	0.029	0.025	0.409
Total number of observations	338553
Number of reflections	36885	3752	3652
<I/σ(I)>	15.9
Completeness [%]	100.0	99.8	100
Redundancy	9.2	9.9	7.9
CC(1/2)		0.994	0.766

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.7	298	26% PEG 8000, 0.1 M sodium cacodylate pH 6.7, 0.2 M sodium acetate