3G5V

Antibodies Specifically Targeting a Locally Misfolded Region of Tumor Associated EGFR

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	EVAPORATION		293	0.2M ammonium acetate, 16-18% PEG5000 monomethylether, EVAPORATION, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.25	45.32

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 35.925	α = 90
b = 83.161	β = 92.43
c = 72.214	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 315r			M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X29A	1.1	NSLS	X29A

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	50	96.6	0.066				27692	1	1

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)
1	2	2.07	79.2		0.282

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Cut-off Sigma (F)	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	2.001	41.581	1.36	26284	1389	96.61	0.229	0.226	0.279	RANDOM	33.822

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]
2.42		0.56	-0.26		-2.11

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.239
r_dihedral_angle_3_deg	15.147
r_dihedral_angle_4_deg	13.802
r_dihedral_angle_1_deg	6.433
r_scangle_it	1.2
r_angle_refined_deg	1.115
r_scbond_it	0.796
r_mcangle_it	0.519
r_mcbond_it	0.311
r_nbtor_refined	0.298

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.239
r_dihedral_angle_3_deg	15.147
r_dihedral_angle_4_deg	13.802
r_dihedral_angle_1_deg	6.433
r_scangle_it	1.2
r_angle_refined_deg	1.115
r_scbond_it	0.796
r_mcangle_it	0.519
r_mcbond_it	0.311
r_nbtor_refined	0.298
r_nbd_refined	0.197
r_symmetry_hbond_refined	0.167
r_symmetry_vdw_refined	0.155
r_xyhbond_nbd_refined	0.117
r_chiral_restr	0.075
r_bond_refined_d	0.007
r_gen_planes_refined	0.003

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3285
Nucleic Acid Atoms
Solvent Atoms	199
Heterogen Atoms	23

Software

Software
Software Name	Purpose
HKL-2000	data collection
MOLREP	phasing
PHENIX	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
REFMAC	refinement

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.