4PIE

Crystal structure of human adenovirus 2 protease a substrate based nitrile inhibitor

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	4.6	293	1mM peptide-nitrile inhibitor was added to the protein and incubated for 30 minutes. 0.8M lithium sulphate, 0.1 M sodium acetate, pH 4.6

Crystal Properties
Matthews coefficient	Solvent content
1.86	33.71

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 41.312	α = 90
b = 44.437	β = 90
c = 98.921	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	PIXEL	PSI PILATUS 6M		2011-12-13	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X10SA	1.000	SLS	X10SA

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	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	1.94	44.4	99.9	0.054	0.059	19.48	6.4		14072		-3	34.286

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.94	1.99	99.7		0.407	0.442	4.57

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	PDB entry 1NLN	1.94	40.53	14072	704	99.95	0.2096	0.2069	0.2603	RANDOM	31.634

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]
-2.49			5.01		-2.52

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.728
r_dihedral_angle_3_deg	17.297
r_dihedral_angle_4_deg	13.089
r_dihedral_angle_1_deg	7.102
r_scangle_it	4.829
r_scbond_it	3.272
r_angle_refined_deg	2.049
r_mcangle_it	1.903
r_mcbond_it	1.113
r_chiral_restr	0.138

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.728
r_dihedral_angle_3_deg	17.297
r_dihedral_angle_4_deg	13.089
r_dihedral_angle_1_deg	7.102
r_scangle_it	4.829
r_scbond_it	3.272
r_angle_refined_deg	2.049
r_mcangle_it	1.903
r_mcbond_it	1.113
r_chiral_restr	0.138
r_bond_refined_d	0.024
r_gen_planes_refined	0.011

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1685
Nucleic Acid Atoms
Solvent Atoms	33
Heterogen Atoms	49

Software

Software
Software Name	Purpose
XDS	data reduction
REFMAC	refinement
PDB_EXTRACT	data extraction
XSCALE	data scaling

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.