4XUE

Synthesis and evaluation of heterocyclic catechol mimics as inhibitors of catechol-O-methyltransferase (COMT): Structure with Cmpd27b

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION		298	0.1M Tris, 0.2M Lithium Sulfate, 20% PEG 4000; MA000598 (PEGsII), drop c11 :100uM ligand, 7.5mg/ml protein

Crystal Properties
Matthews coefficient	Solvent content
3.71	66.81

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 55.043	�� = 90
b = 113.19	�� = 90
c = 113.818	�� = 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	ADSC QUANTUM 315		2008-08-24	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 17-ID	1.0	APS	17-ID

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	2.3	50	99.8	0.106	8.6	7		32406

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	2.3	2.34	98.3		0.489		5.7	1533

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	2.3	49.57	30705	1640	99.77	0.1996	0.1979	0.229	RANDOM	28.686

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]
1.13			-0.24		-0.89

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.553
r_dihedral_angle_4_deg	17.229
r_dihedral_angle_3_deg	14.004
r_dihedral_angle_1_deg	5.557
r_scangle_it	2.736
r_scbond_it	1.706
r_angle_refined_deg	1.309
r_mcangle_it	1.158
r_mcbond_it	0.662
r_nbtor_refined	0.3

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.553
r_dihedral_angle_4_deg	17.229
r_dihedral_angle_3_deg	14.004
r_dihedral_angle_1_deg	5.557
r_scangle_it	2.736
r_scbond_it	1.706
r_angle_refined_deg	1.309
r_mcangle_it	1.158
r_mcbond_it	0.662
r_nbtor_refined	0.3
r_symmetry_hbond_refined	0.206
r_nbd_refined	0.199
r_symmetry_vdw_refined	0.174
r_xyhbond_nbd_refined	0.123
r_chiral_restr	0.08
r_bond_refined_d	0.012
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3345
Nucleic Acid Atoms
Solvent Atoms	120
Heterogen Atoms	98

Software

Software
Software Name	Purpose
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
MOLREP	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 R01GM157729.