1NH0

1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site

X-RAY DIFFRACTION

Crystallization

Crystal Properties
Matthews coefficient	Solvent content
1.94	36.64

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 28.913	α = 90
b = 66.562	β = 90
c = 93.147	γ = 90

Symmetry
Space Group	P 21 21 21

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	ADSC QUANTUM 4		2001-11-12	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID14-2		ESRF	ID14-2

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge 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	1.03	54.1	99	0.089	10.5	9.8	89657	88784			7.9

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.03	1.06	93.3		0.595	1.85	5.2

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	FREE R	1VIK	1.03	6	88225	88225	2205	99	0.1305	0.1305	0.1301	0.1654	RANDOM

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]

Coordinate Error
Structure Solution Method	Refinement High Resolution	Refinement Low Resolution
20	1670	1839.62

RMS Deviations
Key	Refinement Restraint Deviation
s_non_zero_chiral_vol	0.175
s_zero_chiral_vol	0.144
s_approx_iso_adps	0.085
s_anti_bump_dis_restr	0.054
s_similar_adp_cmpnt	0.054
s_angle_d	0.036
s_from_restr_planes	0.0304
s_bond_d	0.016
s_rigid_bond_adp_cmpnt	0.01
s_similar_dist

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1616
Nucleic Acid Atoms
Solvent Atoms	233
Heterogen Atoms	15

Software

Software
Software Name	Purpose
XDS	data scaling
XSCALE	data scaling
EPMR	phasing
SHELXL-97	refinement
XDS	data reduction

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.