3G5Z

Antibodies Specifically Targeting a Locally Misfolded Region of Tumor Associated EGFR

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	EVAPORATION	9	293	0.2M NH4 acetate, 24% PEG6K, 0.1M Bis-tris propane, pH9.0, EVAPORATION, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.02	38.97

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 36.37	α = 90
b = 94.8	β = 90
c = 108.9	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	RIGAKU RAXIS IV++			M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU MICROMAX-007

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	2.8	50	98.4	0.14				9171	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	2.8	2.87	90.5		0.332

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	MOLECULAR REPLACEMENT	THROUGHOUT	2.6	35.75	9171	534	92.01	0.2179	0.2138	0.30121	RANDOM	33.986

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]
0.08			-1		0.92

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.564
r_dihedral_angle_3_deg	19.104
r_dihedral_angle_4_deg	9.689
r_dihedral_angle_1_deg	6.586
r_scangle_it	5.306
r_scbond_it	3.677
r_mcangle_it	2.597
r_mcbond_it	1.427
r_angle_refined_deg	1.409
r_nbtor_refined	0.314

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.564
r_dihedral_angle_3_deg	19.104
r_dihedral_angle_4_deg	9.689
r_dihedral_angle_1_deg	6.586
r_scangle_it	5.306
r_scbond_it	3.677
r_mcangle_it	2.597
r_mcbond_it	1.427
r_angle_refined_deg	1.409
r_nbtor_refined	0.314
r_nbd_refined	0.246
r_symmetry_vdw_refined	0.236
r_xyhbond_nbd_refined	0.187
r_symmetry_hbond_refined	0.095
r_chiral_restr	0.083
r_bond_refined_d	0.011
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3276
Nucleic Acid Atoms
Solvent Atoms	39
Heterogen Atoms

Software

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

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.