3WQB

Crystal structure of aeromonas sobria serine protease (ASP) and the chaperone (ORF2) complex

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.5	277	7.5% PEG 3000, 0.05M HEPES, 0.05M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.15	42.9

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 152.062	α = 90
b = 152.062	β = 90
c = 51.625	γ = 120

Symmetry
Space Group	P 61

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 210r		2013-04-24	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	PHOTON FACTORY BEAMLINE AR-NW12A	1.0	Photon Factory	AR-NW12A

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	1.41	50	99.2	0.088	21	6.3		130476

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	1.41	1.43	97.9		0.381		2.5	6439

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	3HJR	1.41	28.74	130244	6544	98.84	0.1877	0.1867	0.2069	RANDOM	16.733

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]
-0.58	-0.29		-0.58		0.87

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.402
r_dihedral_angle_4_deg	17.571
r_dihedral_angle_3_deg	12.537
r_dihedral_angle_1_deg	6.088
r_scangle_it	3.161
r_scbond_it	2.109
r_mcangle_it	1.33
r_angle_refined_deg	1.148
r_rigid_bond_restr	0.866
r_mcbond_it	0.791

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.402
r_dihedral_angle_4_deg	17.571
r_dihedral_angle_3_deg	12.537
r_dihedral_angle_1_deg	6.088
r_scangle_it	3.161
r_scbond_it	2.109
r_mcangle_it	1.33
r_angle_refined_deg	1.148
r_rigid_bond_restr	0.866
r_mcbond_it	0.791
r_chiral_restr	0.075
r_bond_refined_d	0.007
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	5208
Nucleic Acid Atoms
Solvent Atoms	392
Heterogen Atoms	3

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
MOLREP	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.