3URZ

Crystal structure of a putative protein binding protein (BACOVA_03105) from Bacteroides ovatus ATCC 8483 at 2.19 A resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.93	277	0.20 M zinc acetate, 16.40 % polyethylene glycol 8000, 0.1M MES pH 5.93, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
3.08	60.12

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 30.703	α = 90
b = 41.597	β = 92.52
c = 236.878	γ = 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 325 mm CCD	Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (ho rizontal focusing)	2010-11-22	M	MAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRL BEAMLINE BL11-1	0.91837,0.98021,0.97963	SSRL	BL11-1

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	2.19	29.581	93.3	0.035	10.96			29857		-3	56.56

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	2.21	2.29	94.2		0.451	2.1

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	MAD	THROUGHOUT	2.19	29.581	29857	1508	95.57	0.2184	0.2173	0.2397	RANDOM	101.8585

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]
-0.07		1.32	-1.12		1.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	23.789
r_dihedral_angle_4_deg	11.443
r_torsion_it	9.769
r_dihedral_angle_3_deg	9.205
r_angle_it	5.851
r_bond_it	4.144
r_angle_others	3.749
r_dihedral_angle_1_deg	2.514
r_angle_refined_deg	1.415
r_angle_other_deg	1.197

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	23.789
r_dihedral_angle_4_deg	11.443
r_torsion_it	9.769
r_dihedral_angle_3_deg	9.205
r_angle_it	5.851
r_bond_it	4.144
r_angle_others	3.749
r_dihedral_angle_1_deg	2.514
r_angle_refined_deg	1.415
r_angle_other_deg	1.197
r_bond_other	0.963
r_chiral_restr	0.09
r_bond_refined_d	0.011
r_gen_planes_refined	0.004
r_bond_other_d	0.002
r_gen_planes_other	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3278
Nucleic Acid Atoms
Solvent Atoms	55
Heterogen Atoms	18

Software

Software
Software Name	Purpose
MolProbity	model building
PDB_EXTRACT	data extraction
SHELX	phasing
SHARP	phasing
XSCALE	data scaling
REFMAC	refinement
XDS	data reduction
SHELXD	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.