4FN2

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation D44G from Burkholderia pseudomallei complexed with CJ37

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	3UQB	PDB entry 3UQB

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6.5	295	Internal tracking number 233926b1. Puck VKT6-6, Morpheus well B1. 10% PEG 20,000, 20% PEG MME550, 0.03M Halides (NaF, NaBr, NaI), 0.1M MES/Imidazole pH 6.5, Direct Cryo. BupsA.00130.a.D214, 20.00 mg/ml, CJ37 (EBSI2854), vapor diffusion, sitting drop, temperature 295K

Crystal Properties
Matthews coefficient	Solvent content
1.91	35.56

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 33.63	α = 90.86
b = 35.14	β = 99.52
c = 75.64	γ = 96.24

Symmetry
Space Group	P 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	ADSC QUANTUM 315r		2012-05-26	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 5.0.1	0.9774	ALS	5.0.1

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	1.95	74.56	97.9	0.094	12.27	3.82	24732	24210		-3	25.722

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	1.95	2	97		0.505	2.7

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	PDB entry 3UQB	1.95	37.28	24732	24210	1234	97.93	0.175	0.175	0.172	0.224	RANDOM	22.48

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	0.34	0.39	0.6	0.13	-0.47

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	32.273
r_dihedral_angle_4_deg	18.951
r_dihedral_angle_3_deg	13.944
r_dihedral_angle_1_deg	6.752
r_angle_refined_deg	1.551
r_angle_other_deg	0.88
r_chiral_restr	0.083
r_bond_refined_d	0.015
r_gen_planes_refined	0.006
r_bond_other_d	0.002

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	32.273
r_dihedral_angle_4_deg	18.951
r_dihedral_angle_3_deg	13.944
r_dihedral_angle_1_deg	6.752
r_angle_refined_deg	1.551
r_angle_other_deg	0.88
r_chiral_restr	0.083
r_bond_refined_d	0.015
r_gen_planes_refined	0.006
r_bond_other_d	0.002
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2812
Nucleic Acid Atoms
Solvent Atoms	287
Heterogen Atoms	42

Software

Software
Software Name	Purpose
XSCALE	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
XDS	data reduction

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.