3EWU

D312N mutant of human orotidyl-5'-monophosphate decarboxylase in complex with 6-acetyl-UMP, covalent adduct

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8	300	0.1 M Tris-HCl pH 8.0, 1.8 M (NH4)2SO4, VAPOR DIFFUSION, SITTING DROP, temperature 300.0K

Crystal Properties
Matthews coefficient	Solvent content
2.47	50.17

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 69.41	�� = 90
b = 61.69	�� = 112.86
c = 70.81	�� = 90

Symmetry
Space Group	P 1 21 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	MARMOSAIC 225 mm CCD		2008-07-09	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X10SA	1.0000	SLS	X10SA

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	1.6	44.3	99.9	0.083	9	3.6		72838

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	1.6	1.63	99.1		0.531	1.5	2.8	2657

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	1.6	38.78	67721	3553	97.86	0.16465	0.16299	0.19614	RANDOM	15.955

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]
0.68		2.03	-0.75		1.65

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.925
r_dihedral_angle_4_deg	16.608
r_dihedral_angle_3_deg	13.205
r_dihedral_angle_1_deg	5.928
r_scangle_it	4.679
r_scbond_it	2.861
r_mcangle_it	1.72
r_angle_refined_deg	1.592
r_angle_other_deg	0.982
r_mcbond_it	0.966

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.925
r_dihedral_angle_4_deg	16.608
r_dihedral_angle_3_deg	13.205
r_dihedral_angle_1_deg	5.928
r_scangle_it	4.679
r_scbond_it	2.861
r_mcangle_it	1.72
r_angle_refined_deg	1.592
r_angle_other_deg	0.982
r_mcbond_it	0.966
r_mcbond_other	0.295
r_chiral_restr	0.097
r_bond_refined_d	0.018
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	3932
Nucleic Acid Atoms
Solvent Atoms	513
Heterogen Atoms	57

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.