2O4N

Crystal Structure of HIV-1 Protease (TRM Mutant) in Complex with Tipranavir

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP		298	0.75-2.0 M NaCl, 100 mM acetate or citrate buffer pH 4.8-5.8 , VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.74	55.09

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 59.076	α = 90
b = 86.487	β = 90
c = 46.439	γ = 90

Symmetry
Space Group	P 21 21 2

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	IMAGE PLATE	RIGAKU RAXIS IV	osmic mirrors	2004-05-30	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RU200	1.54

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym I (Observed)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	2	19.6	94.7	0.086	0.086	10.7	3.9		15839

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2	2.07	84.2		0.308	0.308	3.07	3.1	1379

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	2	19.6	15710	1587	99.32	0.189	0.185	0.227	RANDOM	25.099

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]
0.01			-1.42		1.42

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.596
r_dihedral_angle_4_deg	17.593
r_dihedral_angle_3_deg	13.614
r_dihedral_angle_1_deg	5.79
r_scangle_it	3.358
r_scbond_it	2.312
r_angle_refined_deg	1.602
r_mcangle_it	1.348
r_mcbond_it	0.944
r_nbtor_refined	0.304

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.596
r_dihedral_angle_4_deg	17.593
r_dihedral_angle_3_deg	13.614
r_dihedral_angle_1_deg	5.79
r_scangle_it	3.358
r_scbond_it	2.312
r_angle_refined_deg	1.602
r_mcangle_it	1.348
r_mcbond_it	0.944
r_nbtor_refined	0.304
r_nbd_refined	0.197
r_symmetry_vdw_refined	0.167
r_xyhbond_nbd_refined	0.155
r_symmetry_hbond_refined	0.151
r_chiral_restr	0.106
r_bond_refined_d	0.017
r_gen_planes_refined	0.007

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1520
Nucleic Acid Atoms
Solvent Atoms	191
Heterogen Atoms	48

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
CNS	phasing

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.