3HVJ

Rat catechol O-methyltransferase in complex with a catechol-type, N6-propyladenine-containing bisubstrate inhibitor

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.5	298	25% PEG 8000, 0.1M BT pH 5.5, 0.1M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.27	45.88

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 55.346	�� = 90
b = 61.414	�� = 90
c = 132.5	�� = 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	MARMOSAIC 225 mm CCD		2009-04-03	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X10SA	1.0075	SLS	X10SA

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	1.79	45.04	97.5	0.109	9.6	6.2		42379			20.4

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.8	1.82	62.2		0.529	2	4.4	867

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	MOLECULAR REPLACEMENT	THROUGHOUT	1.79	45.04	39165	2078	95.12	0.18603	0.18346	0.2354	RANDOM	18.328

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			-1.08		0.66

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.626
r_dihedral_angle_4_deg	22.135
r_dihedral_angle_3_deg	14.221
r_dihedral_angle_1_deg	5.353
r_scangle_it	3.873
r_scbond_it	2.52
r_mcangle_it	1.54
r_angle_refined_deg	1.53
r_angle_other_deg	0.959
r_mcbond_it	0.886

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.626
r_dihedral_angle_4_deg	22.135
r_dihedral_angle_3_deg	14.221
r_dihedral_angle_1_deg	5.353
r_scangle_it	3.873
r_scbond_it	2.52
r_mcangle_it	1.54
r_angle_refined_deg	1.53
r_angle_other_deg	0.959
r_mcbond_it	0.886
r_mcbond_other	0.246
r_chiral_restr	0.098
r_bond_refined_d	0.016
r_gen_planes_refined	0.007
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3362
Nucleic Acid Atoms
Solvent Atoms	406
Heterogen Atoms	99

Software

Software
Software Name	Purpose
COMO	phasing
REFMAC	refinement
XDS	data reduction
SADABS	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 R01GM157729.