3R9E

Crystal structure of Microcin C7 self immunity acetyltransferase MccE in complex with coenzyme A and aspartyl sulfamoyl adenosine (DSA)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	hanging drop	7	282	PEG550MME, MgCl2, pH 7.0, hanging drop, temperature 282K

Crystal Properties
Matthews coefficient	Solvent content
2.37	48.04

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 78.986	�� = 90
b = 94.763	�� = 90
c = 53.252	�� = 90

Symmetry
Space Group	P 21 21 2

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray						M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-D		APS	21-ID-D

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	1.25	50	99.5	0.063	11.8	9.1		110989

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	1.25	1.29	96.6		0.427		5.4	10665

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	1.25	25	110916	5557	99.47	0.1831	0.1821	0.2016	RANDOM	15.3032

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]
0.29			-0.21		-0.07

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.771
r_dihedral_angle_4_deg	20.428
r_dihedral_angle_3_deg	10.061
r_dihedral_angle_1_deg	5.898
r_scangle_it	2.713
r_sphericity_bonded	1.958
r_scbond_it	1.784
r_angle_refined_deg	1.432
r_mcangle_it	1.236
r_rigid_bond_restr	0.931

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.771
r_dihedral_angle_4_deg	20.428
r_dihedral_angle_3_deg	10.061
r_dihedral_angle_1_deg	5.898
r_scangle_it	2.713
r_sphericity_bonded	1.958
r_scbond_it	1.784
r_angle_refined_deg	1.432
r_mcangle_it	1.236
r_rigid_bond_restr	0.931
r_mcbond_it	0.7
r_chiral_restr	0.104
r_bond_refined_d	0.007
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2836
Nucleic Acid Atoms
Solvent Atoms	610
Heterogen Atoms	158

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction

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.