2H79

Crystal Structure of human TR alpha bound T3 in orthorhombic space group

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.2	298	1.0 M sodium cacodylate and 0.1M sodium acetate threehydrate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
4.01	69.34

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 59.981	α = 90
b = 80.795	β = 90
c = 102.211	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	IMAGE PLATE	MAR scanner 345 mm plate	Mirrors	2004-01-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU	1.54

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	1.87	63.25	98.18			39069	39069	2	2

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	1.87	1.917	7.11

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	1.87	63.25	41150	39069	2081	98.18	0.15	0.15	0.149	0.187	RANDOM	29.302

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]
0.03			-0.19		0.16

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	6.924
r_dihedral_angle_1_deg	6.397
r_scbond_it	4.809
r_angle_refined_deg	3.846
r_mcangle_it	2.887
r_mcbond_it	1.73
r_symmetry_vdw_refined	0.327
r_chiral_restr	0.292
r_xyhbond_nbd_refined	0.286
r_nbd_refined	0.267

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	6.924
r_dihedral_angle_1_deg	6.397
r_scbond_it	4.809
r_angle_refined_deg	3.846
r_mcangle_it	2.887
r_mcbond_it	1.73
r_symmetry_vdw_refined	0.327
r_chiral_restr	0.292
r_xyhbond_nbd_refined	0.286
r_nbd_refined	0.267
r_symmetry_hbond_refined	0.247
r_bond_refined_d	0.041
r_gen_planes_refined	0.014

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2237
Nucleic Acid Atoms
Solvent Atoms	427
Heterogen Atoms	23

Software

Software
Software Name	Purpose
REFMAC	refinement
PDB_EXTRACT	data extraction

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 R01GM157729.