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)