2FW3

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with antidiabetic drug ST1326

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	MICROBATCH		294	25% (v/v) PEG 1500, microbatch, temperature 294K

Crystal Properties
Matthews coefficient	Solvent content
3.48	64.7

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 85.8	α = 90
b = 96.2	β = 90
c = 124.3	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	MARRESEARCH		2005-03-05	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X10SA	1.008	SLS	X10SA

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	2.5	76.03		0.134	11.71		35312	33845

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)
	2.5	2.63	91.97		0.31	4.19

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	MOLECULAR REPLACEMENT	THROUGHOUT	2.5	15	32831	1764	95.83	0.24412	0.24124	0.29647	RANDOM	40.988

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]
6.8			-0.97		-5.83

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.791
r_dihedral_angle_4_deg	21.904
r_dihedral_angle_3_deg	18.882
r_dihedral_angle_1_deg	6.761
r_scangle_it	2.497
r_scbond_it	1.571
r_angle_refined_deg	1.502
r_mcangle_it	1.157
r_mcbond_it	0.645
r_nbtor_refined	0.309

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.791
r_dihedral_angle_4_deg	21.904
r_dihedral_angle_3_deg	18.882
r_dihedral_angle_1_deg	6.761
r_scangle_it	2.497
r_scbond_it	1.571
r_angle_refined_deg	1.502
r_mcangle_it	1.157
r_mcbond_it	0.645
r_nbtor_refined	0.309
r_nbd_refined	0.228
r_symmetry_vdw_refined	0.222
r_xyhbond_nbd_refined	0.187
r_symmetry_hbond_refined	0.126
r_chiral_restr	0.1
r_bond_refined_d	0.013
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4963
Nucleic Acid Atoms
Solvent Atoms	152
Heterogen Atoms	28

Software

Software
Software Name	Purpose
REFMAC	refinement
MAR345	data collection
XDS	data scaling
AMoRE	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.