3OMT

Putative antitoxin component, CHU_2935 protein, from Xre family from Prevotella buccae.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	4.2	277	2 M ammonium sulfate, 0.1 M phosphate citrate-buffer, pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.31	46.74

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 39.855	α = 90
b = 44.882	β = 90
c = 86.408	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	CCD	ADSC QUANTUM 315		2007-12-02	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.9792	APS	19-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	1.65	39.8	100	0.098	7.1	11.5	19302	19302			24.7

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)
	1.65	1.68	100		0.895	2.74	10.2	952

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	3BS3	1.65	39.8	19239	19239	986	99.79	0.1384	0.1384	0.1356	0.1919	RANDOM	16.7633

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]
0.01			0.36		-0.38

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.128
r_dihedral_angle_3_deg	11.8
r_dihedral_angle_4_deg	10.318
r_scangle_it	5.935
r_dihedral_angle_1_deg	4.647
r_scbond_it	3.996
r_mcangle_it	2.507
r_mcbond_it	1.601
r_rigid_bond_restr	1.593
r_angle_refined_deg	1.432

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.128
r_dihedral_angle_3_deg	11.8
r_dihedral_angle_4_deg	10.318
r_scangle_it	5.935
r_dihedral_angle_1_deg	4.647
r_scbond_it	3.996
r_mcangle_it	2.507
r_mcbond_it	1.601
r_rigid_bond_restr	1.593
r_angle_refined_deg	1.432
r_angle_other_deg	0.968
r_mcbond_other	0.524
r_chiral_restr	0.097
r_bond_refined_d	0.017
r_gen_planes_refined	0.006
r_bond_other_d	0.003
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1087
Nucleic Acid Atoms
Solvent Atoms	230
Heterogen Atoms	5

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
SBC-Collect	data collection
HKL-2000	data reduction
HKL-2000	data scaling
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 R01GM133198.