9GBR

Human Angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor- SG17

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 pH8.5 60 mM divalent cations (MgCl2 and CaCl2) 30% PEG550 MME/PEG20K

Crystal Properties
Matthews coefficient	Solvent content
2.91	57.73

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 73.053	�� = 88.38
b = 77.377	�� = 64.31
c = 82.914	�� = 74.92

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 EIGER2 XE 16M		2018-10-23	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)	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	1.9	74.365	97.8	0.054	0.997	11.3	9.5		1157631

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	1.9	1.93	96.5		1.071	0.329

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	1.9	74.365	121230	5952	97.821	0.189	0.1875	0.2253	32.98

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]
-0.147	0.882	0.253	0.393	-0.079	0.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	15.115
r_dihedral_angle_6_deg	14.751
r_dihedral_angle_2_deg	8.211
r_dihedral_angle_1_deg	6.6
r_lrange_it	5.927
r_scangle_it	4.612
r_scbond_it	3.045
r_mcangle_it	2.648
r_angle_refined_deg	2.263
r_mcbond_it	1.776

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	15.115
r_dihedral_angle_6_deg	14.751
r_dihedral_angle_2_deg	8.211
r_dihedral_angle_1_deg	6.6
r_lrange_it	5.927
r_scangle_it	4.612
r_scbond_it	3.045
r_mcangle_it	2.648
r_angle_refined_deg	2.263
r_mcbond_it	1.776
r_nbtor_refined	0.318
r_symmetry_nbd_refined	0.231
r_nbd_refined	0.222
r_symmetry_xyhbond_nbd_refined	0.167
r_xyhbond_nbd_refined	0.166
r_chiral_restr	0.149
r_bond_refined_d	0.012
r_gen_planes_refined	0.012

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	9863
Nucleic Acid Atoms
Solvent Atoms	591
Heterogen Atoms	240

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.