2PX6

Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	4.3	298	50mM sodium dihydrogen phosphate, 30-35% PEG 3350, 30mM dithiothreitol, pH 4.3, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
1.97	37.53

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 41.86	α = 90
b = 94.32	β = 95.82
c = 69.72	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	ADSC QUANTUM 210			M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X12C	1.0	NSLS	X12C

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	2.3	39.01	96	0.06	17	7.1	21850	21850

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)
	2.3	2.38	76.2		0.23	6.2	6.2

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	PDB ENTRY 1XKT	2.3	39.01	21850	1184	96.03	0.22753	0.225	0.27276	RANDOM	36.96

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]
		-0.01

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.008
r_dihedral_angle_4_deg	19.884
r_dihedral_angle_3_deg	17.322
r_dihedral_angle_1_deg	5.557
r_scangle_it	2.37
r_scbond_it	1.475
r_angle_refined_deg	1.273
r_mcangle_it	1.093
r_mcbond_it	0.661
r_nbtor_refined	0.303

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.008
r_dihedral_angle_4_deg	19.884
r_dihedral_angle_3_deg	17.322
r_dihedral_angle_1_deg	5.557
r_scangle_it	2.37
r_scbond_it	1.475
r_angle_refined_deg	1.273
r_mcangle_it	1.093
r_mcbond_it	0.661
r_nbtor_refined	0.303
r_nbd_refined	0.205
r_symmetry_vdw_refined	0.202
r_xyhbond_nbd_refined	0.166
r_symmetry_hbond_refined	0.12
r_chiral_restr	0.084
r_bond_refined_d	0.01
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4011
Nucleic Acid Atoms
Solvent Atoms	53
Heterogen Atoms	79

Software

Software
Software Name	Purpose
REFMAC	refinement
CBASS	data collection
d*TREK	data reduction
d*TREK	data scaling
PHASER	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.