1TOU

Crystal structure of human adipocyte fatty acid binding protein in complex with a non-covalent ligand

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7	293	PEG2000, DMSO, TRIS, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.05	40

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 71.829	α = 90
b = 53.106	β = 90
c = 31.383	γ = 90

Symmetry
Space Group	P 21 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	100	IMAGE PLATE	RIGAKU RAXIS IV		2000-10-16	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU	1.5418

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	15	98.5	0.064	17.9	3.3		8483

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	2.07	93.5		0.209	4.4		792

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	FOURIER SYNTHESIS	THROUGHOUT	2	15	7997	380	98.01	0.20372	0.20032	0.27947	RANDOM	25.467

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]
-1.13			-0.46		1.59

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.262
r_dihedral_angle_4_deg	19.368
r_dihedral_angle_3_deg	13.726
r_dihedral_angle_1_deg	6.007
r_scangle_it	3.05
r_scbond_it	1.872
r_mcangle_it	1.247
r_angle_refined_deg	1.21
r_mcbond_it	0.811
r_chiral_restr	0.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.262
r_dihedral_angle_4_deg	19.368
r_dihedral_angle_3_deg	13.726
r_dihedral_angle_1_deg	6.007
r_scangle_it	3.05
r_scbond_it	1.872
r_mcangle_it	1.247
r_angle_refined_deg	1.21
r_mcbond_it	0.811
r_chiral_restr	0.31
r_nbtor_refined	0.303
r_symmetry_vdw_refined	0.239
r_nbd_refined	0.185
r_xyhbond_nbd_refined	0.152
r_symmetry_hbond_refined	0.091
r_bond_refined_d	0.011
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1021
Nucleic Acid Atoms
Solvent Atoms	134
Heterogen Atoms	21

Software

Software
Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	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.