5P9Y

humanized rat catechol O-methyltransferase in complex with 6-(4-fluorophenyl)-8-hydroxy-3-(5-pyrrolo[3,2-c]pyridin-1-ylpentyl)quinazolin-4-one

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	9	295	AMMONIUM SULPHATE, CHES, PH 9

Crystal Properties
Matthews coefficient	Solvent content
2.24	44.98

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 49.967	α = 90
b = 54.212	β = 90
c = 81.524	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		2010-03-08	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X10SA	1.000000	SLS	X10SA

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	CC (Half)	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	1.2	33.5	97.9	0.058	0.067	0.999	11.99	4.17		68572		-3	16.968

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.2	1.23	97.5		0.889	1.024	0.656	1.66

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	inhouse model	1.2	33.5	59877	3167	90.05	0.1429	0.1411	0.1772	RANDOM	12.749

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]
0.12			0.27		-0.39

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.201
r_dihedral_angle_4_deg	21.477
r_rigid_bond_restr	15.624
r_sphericity_free	13.084
r_dihedral_angle_3_deg	11.991
r_sphericity_bonded	7.132
r_dihedral_angle_1_deg	5.153
r_angle_refined_deg	1.935
r_angle_other_deg	1.416
r_mcbond_it	0.156

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.201
r_dihedral_angle_4_deg	21.477
r_rigid_bond_restr	15.624
r_sphericity_free	13.084
r_dihedral_angle_3_deg	11.991
r_sphericity_bonded	7.132
r_dihedral_angle_1_deg	5.153
r_angle_refined_deg	1.935
r_angle_other_deg	1.416
r_mcbond_it	0.156
r_chiral_restr	0.124
r_mcbond_other	0.122
r_bond_refined_d	0.021
r_gen_planes_refined	0.01
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1673
Nucleic Acid Atoms
Solvent Atoms	230
Heterogen Atoms	75

Software

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

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.