3GEL

O-Methylphosphorylated Torpedo Acetylcholinesterase Obtained by Reaction with Methyl Paraoxon (AGED)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.8	277.15	18% Peg 200, 0.1 M MES, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K

Crystal Properties
Matthews coefficient	Solvent content
4.09	69.93

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 111.726	α = 90
b = 111.726	β = 90
c = 136.853	γ = 120

Symmetry
Space Group	P 31 2 1

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	BRUKER SMART 6000	Multilayer Mirrors	2008-08-15	M	SINGLE WAVELENGTH

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

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	2.39	28.53	94.64	0.139	23.75	21.27		35608	3	3	26.949

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2.39	2.48	100		6.36	20.67	4106

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	2ACE	2.39	27.93	35608	1872	94.64	0.21169	0.21021	0.23995	RANDOM	26.949

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]
0.41	0.21		0.41		-0.62

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.25
r_dihedral_angle_4_deg	21.102
r_dihedral_angle_3_deg	16.053
r_dihedral_angle_1_deg	6.35
r_scangle_it	3.53
r_scbond_it	2.705
r_mcangle_it	2.611
r_angle_refined_deg	1.914
r_mcbond_it	1.863
r_nbtor_refined	0.314

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.25
r_dihedral_angle_4_deg	21.102
r_dihedral_angle_3_deg	16.053
r_dihedral_angle_1_deg	6.35
r_scangle_it	3.53
r_scbond_it	2.705
r_mcangle_it	2.611
r_angle_refined_deg	1.914
r_mcbond_it	1.863
r_nbtor_refined	0.314
r_symmetry_vdw_refined	0.301
r_nbd_refined	0.242
r_xyhbond_nbd_refined	0.189
r_chiral_restr	0.126
r_symmetry_hbond_refined	0.115
r_bond_refined_d	0.024
r_gen_planes_refined	0.01

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4208
Nucleic Acid Atoms
Solvent Atoms	351
Heterogen Atoms

Software

Software
Software Name	Purpose
PROTEUM PLUS	data collection
AMoRE	phasing
REFMAC	refinement
SAINT	data reduction
SCALA	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.