5JBT

Mesotrypsin in complex with cleaved amyloid precursor like protein 2 inhibitor (APLP2)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	0.2 M Ammonium Sulfate 0.1 M Sodium Cacodylate Trihydrate 30% PEG 8000

Crystal Properties
Matthews coefficient	Solvent content
2.52	51.2

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 98.956	α = 90
b = 54.539	β = 90
c = 56.632	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		2013-11-10	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X25	1.1	NSLS	X25

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	1.398	50	99.8	0.064	27.2	12.8		57667			16.1

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	1.398	1.42	99.8		0.231	6.76	7.3

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	3L33	1.4	36.51	57667	3082	98.9	0.1647	0.1629	0.1985	RANDOM	19.638

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]
-0.04			0.01		0.03

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.389
r_sphericity_free	31.238
r_dihedral_angle_4_deg	20.342
r_sphericity_bonded	12.908
r_dihedral_angle_3_deg	11.453
r_rigid_bond_restr	7.104
r_dihedral_angle_1_deg	6.463
r_angle_other_deg	2.303
r_angle_refined_deg	2.156
r_chiral_restr	0.147

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.389
r_sphericity_free	31.238
r_dihedral_angle_4_deg	20.342
r_sphericity_bonded	12.908
r_dihedral_angle_3_deg	11.453
r_rigid_bond_restr	7.104
r_dihedral_angle_1_deg	6.463
r_angle_other_deg	2.303
r_angle_refined_deg	2.156
r_chiral_restr	0.147
r_bond_refined_d	0.024
r_gen_planes_other	0.016
r_gen_planes_refined	0.012
r_bond_other_d	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2096
Nucleic Acid Atoms
Solvent Atoms	261
Heterogen Atoms	6

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-2000	data scaling
PDB_EXTRACT	data extraction
HKL-2000	data reduction

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.