9GBP

Human Angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor- SG3

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	6F9V

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	8.5	289.15	1 M Tris/Bicine pH 8.5 60 mM divalent cations (MgCl2 and CaCl2) 30% PEG 550MME/PEG20K

Crystal Properties
Matthews coefficient	Solvent content
2.92	57.85

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 73.088	�� = 88.265
b = 77.974	�� = 64.112
c = 83.312	�� = 74.362

Symmetry
Space Group	P 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	PIXEL	DECTRIS PILATUS 6M-F		2018-12-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	DIAMOND BEAMLINE I04	0.9795	Diamond	I04

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	Rpim I (All)	CC (Half)	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	74.704	98	0.046	0.996	10.3	3.5		105007

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2	2.03	96.8		0.297	0.781

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 (All)	R-Work	R-Free	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	FREE R-VALUE	2	74.704	104989	5130	97.959	0.185	0.183	0.2298	31.541

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]
-0.635	0.758	0.264	0.566	0.004	0.442

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	15.209
r_dihedral_angle_6_deg	14.772
r_dihedral_angle_2_deg	10.852
r_lrange_it	8.628
r_scangle_it	7.497
r_dihedral_angle_1_deg	6.967
r_scbond_it	5.549
r_mcangle_it	5.433
r_mcbond_it	4.278
r_angle_refined_deg	2.463

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	15.209
r_dihedral_angle_6_deg	14.772
r_dihedral_angle_2_deg	10.852
r_lrange_it	8.628
r_scangle_it	7.497
r_dihedral_angle_1_deg	6.967
r_scbond_it	5.549
r_mcangle_it	5.433
r_mcbond_it	4.278
r_angle_refined_deg	2.463
r_nbtor_refined	0.322
r_nbd_refined	0.228
r_symmetry_nbd_refined	0.195
r_symmetry_xyhbond_nbd_refined	0.184
r_xyhbond_nbd_refined	0.168
r_chiral_restr	0.165
r_bond_refined_d	0.015
r_gen_planes_refined	0.014

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	9902
Nucleic Acid Atoms
Solvent Atoms	864
Heterogen Atoms	294

Software

Software
Software Name	Purpose
REFMAC	refinement
DIALS	data reduction
Aimless	data scaling
PHASER	phasing

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.