3O4L

Genetic and structural basis for selection of a ubiquitous T cell receptor deployed in Epstein-Barr virus

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6	291	0.16 M Ca Acetate, 0.08 M Na Cacodylate, 12.5% PEG 8000, 20% Glycerol, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K

Crystal Properties
Matthews coefficient	Solvent content
2.52	51.23

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 94.08	α = 90
b = 122.5	β = 90
c = 82.37	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	CCD	ADSC QUANTUM 315		2009-11-27	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	DIAMOND BEAMLINE I03	0.976	Diamond	I03

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	2.54	61.25	99.1	0.163	12.2	7.9	31817	31817

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	2.54	2.61	95.1		0.832	0.832	0.9	7.9	2222

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	2P5E	2.54	61.25	31773	1603	100	0.2245	0.2207	0.2962	RANDOM	27.6561

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]
-0.27			-0.98		1.26

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	22.954
r_dihedral_angle_3_deg	12.696
r_dihedral_angle_4_deg	11.216
r_scangle_it	4.74
r_scbond_it	3.098
r_dihedral_angle_1_deg	2.716
r_mcangle_it	2.441
r_rigid_bond_restr	1.569
r_mcbond_other	1.478
r_mcbond_it	1.395

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	22.954
r_dihedral_angle_3_deg	12.696
r_dihedral_angle_4_deg	11.216
r_scangle_it	4.74
r_scbond_it	3.098
r_dihedral_angle_1_deg	2.716
r_mcangle_it	2.441
r_rigid_bond_restr	1.569
r_mcbond_other	1.478
r_mcbond_it	1.395
r_angle_refined_deg	1.233
r_angle_other_deg	0.756
r_chiral_restr	0.112
r_bond_refined_d	0.017
r_gen_planes_refined	0.009
r_bond_other_d	0.002
r_gen_planes_other	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	6618
Nucleic Acid Atoms
Solvent Atoms	334
Heterogen Atoms	113

Software

Software
Software Name	Purpose
SCALA	data scaling
AMoRE	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
GDA	data collection
xia2	data reduction

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.