3R9F

Crystal structure of Microcin C7 self immunity acetyltransferase MccE in complex with Coenzyme A and Glutamyl sulfamoyl adenosine (ESA)

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	48.14

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 78.979	�� = 90
b = 94.804	�� = 90
c = 53.339	�� = 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	1.2	50	99.3	0.065	12.2	8.6		124743

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	1.2	1.24	96		0.447		6.9	11911

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	1.2	25	124642	6263	99.3	0.1853	0.1845	0.1995	RANDOM	16.0726

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]
0.18			-0.22		0.05

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.896
r_dihedral_angle_4_deg	21.069
r_dihedral_angle_3_deg	10.007
r_dihedral_angle_1_deg	6.01
r_scangle_it	2.606
r_sphericity_bonded	1.919
r_scbond_it	1.701
r_angle_refined_deg	1.521
r_mcangle_it	1.214
r_rigid_bond_restr	0.886

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.896
r_dihedral_angle_4_deg	21.069
r_dihedral_angle_3_deg	10.007
r_dihedral_angle_1_deg	6.01
r_scangle_it	2.606
r_sphericity_bonded	1.919
r_scbond_it	1.701
r_angle_refined_deg	1.521
r_mcangle_it	1.214
r_rigid_bond_restr	0.886
r_mcbond_it	0.674
r_chiral_restr	0.1
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	665
Heterogen Atoms	160

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.