3F9H

Crystal Structure of the F140A mutant of SARS-Coronovirus 3C-like Protease at pH 7.6

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.6	277	0.1M Tris pH 7.6, 10% PEG 6000, 1mM DTT, 5% DMSO, vapor diffusion, hanging drop, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.28	46.13

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 61.111	α = 90
b = 68.144	β = 90
c = 148.903	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	IMAGE PLATE	RIGAKU RAXIS IV++		2008-03-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU	1.5418

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	2.9	15	98.4	0.189		3.47		14073

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)
	2.9	3	99.9		0.366	1.9	3.59	1402

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		THROUGHOUT	2.9	14.97	14059	704	98.26	0.235	0.232	0.294	RANDOM	22.86

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]
0.53			-3.64		3.11

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.646
r_dihedral_angle_3_deg	15.76
r_dihedral_angle_4_deg	15.074
r_dihedral_angle_1_deg	4.944
r_angle_refined_deg	0.932
r_scangle_it	0.581
r_mcangle_it	0.471
r_scbond_it	0.352
r_nbtor_refined	0.3
r_mcbond_it	0.262

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.646
r_dihedral_angle_3_deg	15.76
r_dihedral_angle_4_deg	15.074
r_dihedral_angle_1_deg	4.944
r_angle_refined_deg	0.932
r_scangle_it	0.581
r_mcangle_it	0.471
r_scbond_it	0.352
r_nbtor_refined	0.3
r_mcbond_it	0.262
r_nbd_refined	0.184
r_symmetry_vdw_refined	0.163
r_symmetry_hbond_refined	0.16
r_xyhbond_nbd_refined	0.136
r_chiral_restr	0.062
r_bond_refined_d	0.006
r_gen_planes_refined	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4634
Nucleic Acid Atoms
Solvent Atoms	21
Heterogen Atoms

Software

Software
Software Name	Purpose
d*TREK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
d*TREK	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.