2OP0

Crystal structure of plasmodium falciparum enoyl ACP reductase with triclosan reductase

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.6	298	2.35M (NH4)2SO4, 0.1M AcONa, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.36	47.99

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 132.305	α = 90
b = 132.305	β = 90
c = 82.911	γ = 90

Symmetry
Space Group	P 43 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	120	IMAGE PLATE	RIGAKU			M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU	1.54178

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	2.8	30	97.67	21.69		18748	18311	1	1

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.8	2.9	99.68

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	1NHD	2.8	93.66	18311	17379	931	97.9	0.19122	0.18689	0.27371	RANDOM	31.405

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]
0.45			0.45		-0.89

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	42.349
r_dihedral_angle_4_deg	22.631
r_dihedral_angle_3_deg	21.272
r_dihedral_angle_1_deg	8.634
r_scangle_it	6.114
r_scbond_it	4.269
r_angle_refined_deg	3.261
r_mcangle_it	2.792
r_mcbond_it	1.804
r_symmetry_hbond_refined	0.401

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	42.349
r_dihedral_angle_4_deg	22.631
r_dihedral_angle_3_deg	21.272
r_dihedral_angle_1_deg	8.634
r_scangle_it	6.114
r_scbond_it	4.269
r_angle_refined_deg	3.261
r_mcangle_it	2.792
r_mcbond_it	1.804
r_symmetry_hbond_refined	0.401
r_nbtor_refined	0.355
r_nbd_refined	0.292
r_symmetry_vdw_refined	0.253
r_xyhbond_nbd_refined	0.222
r_chiral_restr	0.211
r_bond_refined_d	0.041
r_gen_planes_refined	0.016

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4416
Nucleic Acid Atoms
Solvent Atoms	109
Heterogen Atoms	72

Software

Software
Software Name	Purpose
REFMAC	refinement
CrystalClear	data collection
HKL-2000	data reduction
HKL-2000	data scaling
XFIT	data reduction

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.