2RCY

Crystal structure of Plasmodium falciparum pyrroline carboxylate reductase (MAL13P1.284) with NADP bound

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291	30% PEG MME550, 50 mM MgCl2, 0.1 M Hepes pH 7.5, 5 mM NADP, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystal Properties
Matthews coefficient	Solvent content
2.52	51.12

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 160.207	α = 90
b = 113.741	β = 105.71
c = 82.651	γ = 90

Symmetry
Space Group	C 1 2 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 315		2007-06-10	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.97937	APS	19-ID

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	2.3	46.27	89.7	0.142	0.108	7.3	2.1	57815	57815

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.3	2.38	53.6		0.496	0.721	1.1	2.3	3416

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	SAD	THROUGHOUT	2.3	46.27	56209	56209	2849	88.86	0.247	0.245	0.289	RANDOM	39.213

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]
-0.02		-0.05	0.06		-0.07

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.727
r_dihedral_angle_4_deg	17.407
r_dihedral_angle_3_deg	14.542
r_dihedral_angle_1_deg	3.88
r_angle_refined_deg	0.941
r_scangle_it	0.462
r_mcangle_it	0.403
r_scbond_it	0.29
r_nbtor_refined	0.285
r_mcbond_it	0.226

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.727
r_dihedral_angle_4_deg	17.407
r_dihedral_angle_3_deg	14.542
r_dihedral_angle_1_deg	3.88
r_angle_refined_deg	0.941
r_scangle_it	0.462
r_mcangle_it	0.403
r_scbond_it	0.29
r_nbtor_refined	0.285
r_mcbond_it	0.226
r_nbd_refined	0.166
r_symmetry_vdw_refined	0.147
r_xyhbond_nbd_refined	0.09
r_symmetry_hbond_refined	0.09
r_chiral_restr	0.054
r_bond_refined_d	0.006
r_gen_planes_refined	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	9396
Nucleic Acid Atoms
Solvent Atoms	427
Heterogen Atoms	256

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
SHELX	phasing
RESOLVE	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
ADSC	data collection
SHELXD	phasing

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.