SARS-CoV-2 related structures

Structures

Our database currently contains information about 315 SARS-CoV-2 protein structures and 26 additional structures of other coronaviruses. Use the filters below to select rows with attributes of interest. Next to each filter value, the number of shown/total structures from the group is displayed. Multiple values can be selected across multiple panes. To select more than one value within a single search pane, press and hold Ctrl or Shift when selecting filters. By default, the Non-PanDDA structures filter is turned on. To show PanDDA structures, just click on the blue filter in the Presets pane to unselect it, or use the Clear All button. Text search can be performed using the search box on the left below the filters.

PDB	Resol.	Released	Title	Method	Ligand IDs	Virus	Protein	Ligand status	R-work	R-free	R-merge	Synthetics	Ligand full name	Author List	Processing Software	Completeness	I/σ	Synchrotron/Beamline	Refinement Software	Deposition Date	PubMed ID	Metals	Molstack	Re-refined PDB	Re-refined MTZ	R-free after re-refinement	Re-refinement summary	Validation summary	Polymers	P_Q1	Issues		Re-refined?	Raw data	Ref.	P_R-free	P_RSRZ	P_Geometry	RNA
1p9s	2.54 Å	2003-05-20	Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of anti-SARS Drugs	X-ray	DIO	HCoV-229E	NSP5 (Main protease)	Functional ligand	19.64%	27.89%	14.20%		1,4-DIETHYLENE DIOXIDE	Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., Hilgenfeld, R.	HKL-2000	98.22%	9.1	ELETTRA (5.2R)	REFMAC	2003-05-12	12746549	-	-	-	-	N/A	-	-	Replicase polyprotein 1ab - residue 2966-3265, 3C-like proteinase	-	-		No	-		15.7	-	9.1
1uk4	2.50 Å	2003-11-18	Crystal structure of SARS Coronavirus Main Proteinase (3CLpro) Complexed With An Inhibitor	X-ray	ATO	HCoV-229E	NSP5 (Main protease)	Functional ligand	21.30%	23.10%	N/A	5-mer peptide of inhibitor	CHLOROACETONE	Yang, H., Yang, M., Liu, Y., Bartlam, M., Ding, Y., Lou, Z., Sun, L., Zhou, Z., Ye, S., Anand, K., Pang, H., Gao, G.F., Hilgenfeld, R., Rao, Z.	HKL-2000	-	-	BSRF (3W1A)	CNS	2003-08-14	14585926	-	-	-	-	N/A	-	-	3C-like proteinase; 5-mer peptide of inhibitor	12.6	-		No	-		55.2	27.5	8.9
1xjr	2.70 Å	2005-02-01	The Structure of a Rigorously Conserved RNA Element Within the SARS Virus Genome	X-ray	-	SARS-CoV	s2m RNA	No functional ligands	23.14%	24.33%	5.60%	s2m RNA	-	Robertson, M.P., Igel, H., Baertsch, R., Haussler, D., Ares Jr., M., Scott, W.G.	MOSFLM	99.40%	31.3	SSRL (BL9-1)	REFMAC	2004-09-24	15630477	MG	-	http://covid-19.bioreproducibility.org/static/data/1xjr/1xjr-refined.pdb	http://covid-19.bioreproducibility.org/static/data/1xjr/1xjr-refined.mtz	N/A	-	-	s2m RNA	64.9	-		Yes	-		43.0	95.5	97.5	s2m RNA
1wof	2.00 Å	2005-08-30	Crystal Structure Of SARS-CoV Mpro in FL N1	X-ray	I12	SARS-CoV	NSP5 (Main protease)	Functional ligand	20.10%	23.90%	N/A	N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]-L-ALANYL-L-VALYL-N~1~-((1S)-4-ETHOXY-4-OXO-1-{[(3S)-2-OXOPYRROLIDIN-3-YL]METHYL}BUT-2-ENYL)-L-LEUCINAMIDE	N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]-L-ALANYL-L-VALYL-N~1~-((1S)-4-ETHOXY-4-OXO-1-{[(3S)-2-OXOPYRROLIDIN-3-YL]METHYL}BUT-2-ENYL)-L-LEUCINAMIDE	Yang, H., Bartlam, M., Xue, X., Yang, K., Liang, W., Rao, Z.	HKL-2000	-	-	ROTATING ANODE ()	CNS	2004-08-18	16128623	-	-	-	-	N/A	-	-	3C-like proteinase	20.3	-		No	-		46.9	42.3	21.6
2ajf	2.90 Å	2005-09-20	Structure of SARS coronavirus spike receptor-binding domain complexed with its receptor	X-ray	NAG, BMA	SARS-CoV	Spike protein	Pathogen-host interaction	21.80%	27.50%	N/A	N-ACETYL-D-GLUCOSAMINE	N-ACETYL-D-GLUCOSAMINE;BETA-D-MANNOSE	Li, F., Li, W., Farzan, M., Harrison, S.C.	HKL-2000	93.10%	20.5	ALS (8.2.1)	REFMAC	2005-08-01	16166518	ZN	-	http://covid-19.bioreproducibility.org/static/data/2ajf/2ajf_refined.pdb	http://covid-19.bioreproducibility.org/static/data/2ajf/2ajf_refined.mtz	27.60%	Placed the coordinates in a standardized location in the unit cell.	The coordinates are NOT in a standardized location in the unit cell.	Angiotensin-converting enzyme-Related Carboxypeptidase (Ace2) - residues 19-615; SARS-coronavirus spike protein - receptor-binding domain, residues 323-502	5.0	minimal	Yes	Yes	-		17.6	34.8	12.6
2d2d	2.70 Å	2005-09-20	Crystal Structure Of SARS-CoV Mpro in FL I2	X-ray	ENB	SARS-CoV	NSP5 (Main protease)	Functional ligand	20.90%	28.20%	N/A	ETHYL (2E,4S)-4-[((2R)-2-{[N-(TERT-BUTOXYCARBONYL)-L-VALYL]AMINO}-2-PHENYLETHANOYL)AMINO]-5-[(3S)-2-OXOPYRROLIDIN-3-YL]PENT-2-ENOATE	ETHYL (2E,4S)-4-[((2R)-2-{[N-(TERT-BUTOXYCARBONYL)-L-VALYL]AMINO}-2-PHENYLETHANOYL)AMINO]-5-[(3S)-2-OXOPYRROLIDIN-3-YL]PENT-2-ENOATE	Yang, H., Bartlam, M., Xue, X., Yang, K., Liang, W., Ding, Y., Rao, Z.	HKL-2000	-	-	ROTATING ANODE ()	CNS	2005-09-08	16128623	-	-	-	-	N/A	-	-	3C-like proteinase	15.6	-		No	-		14.0	80.3	5.4
2alv	1.90 Å	2006-08-08	X-ray structural analysis of SARS coronavirus 3CL proteinase in complex with designed anti-viral inhibitors	X-ray	CY6	SARS-CoV	NSP5 (Main protease)	Functional ligand	25.50%	31.50%	3.80%	N-((3S,6R)-6-((S,E)-4-ETHOXYCARBONYL-1-((S)-2-OXOPYRROLIDIN-3-YL)BUT-3-EN-2-YLCARBAMOYL)-2,9-DIMETHYL-4-OXODEC-8-EN-3-YL)-5-METHYLISOXAZOLE-3-CARBOXAMIDE	N-((3S,6R)-6-((S,E)-4-ETHOXYCARBONYL-1-((S)-2-OXOPYRROLIDIN-3-YL)BUT-3-EN-2-YLCARBAMOYL)-2,9-DIMETHYL-4-OXODEC-8-EN-3-YL)-5-METHYLISOXAZOLE-3-CARBOXAMIDE	Ghosh, A.K., Xi, K., Ratia, K., Santarsiero, B.D., Fu, W., Harcourt, B.H., Rota, P.A., Baker, S.C., Johnson, M.E., Mesecar, A.D.	DENZO; HKL-2000	98.60%	32.4	APS (14-BM-C)	CNS	2005-08-08	16250632	-	-	http://covid-19.bioreproducibility.org/static/data/2alv/2alv_refined.pdb	http://covid-19.bioreproducibility.org/static/data/2alv/2alv_refined.mtz	29.50%	Placed the coordinates in a standardized location in the unit cell. Aded link between the inhibitor and Cys145, corrected. Corrected residues Leu50, Asn51, Val125, Ile286, 301-303. C38 atom of the inhibitor, moved 5-13 oxazol moiety of the inhibitor.	Several residues and the inhibitor can be corrected. The inhibitor is not linked to the protein. The coordinates are NOT in a standardized location in the unit cell.	Replicase polyprotein 1ab - 3CL proteinase, residues 3242-3543	1.4	moderate	Yes	Yes	-		6.1	25.2	12.0
2gx4	1.93 Å	2007-05-08	Crystal structure of SARS coronavirus 3CL protease inhibitor complex	X-ray	NOL	SARS-CoV	NSP5 (Main protease)	Functional ligand	20.53%	24.88%	N/A	N-[(BENZYLOXY)CARBONYL]-O-(TERT-BUTYL)-L-THREONYL-3-CYCLOHEXYL-N-[(1S)-2-HYDROXY-1-{[(3S)-2-OXOPYRROLIDIN-3-YL]METHYL}ETHYL]-L-ALANINAMIDE	N-[(BENZYLOXY)CARBONYL]-O-(TERT-BUTYL)-L-THREONYL-3-CYCLOHEXYL-N-[(1S)-2-HYDROXY-1-{[(3S)-2-OXOPYRROLIDIN-3-YL]METHYL}ETHYL]-L-ALANINAMIDE	Hsu, M.F., Wang, A.H.-J.	HKL-2000; CrystalClear	-	-	ROTATING ANODE ()	CNS	2006-05-08	16884309	-	-	-	-	N/A	-	-	3C-like proteinase - residues 1-306	39.1	-		No	-		37.7	67.8	44.7
2qiq	1.90 Å	2008-02-12	Structure-based Design and Synthesis and Biological Evaluation of Peptidomimetic SARS-3CLpro Inhibitors	X-ray	CYV	SARS-CoV	NSP5 (Main protease)	Functional ligand	23.30%	27.50%	N/A	ETHYL (4R)-4-{[(2R,5S)-5-{[N-(TERT-BUTOXYCARBONYL)-L-SERYL]AMINO}-6-METHYL-2-(3-METHYLBUT-2-EN-1-YL)-4-OXOHEPTANOYL]AMINO}-5-[(3R)-2-OXOPYRROLIDIN-3-YL]PENTANOATE	ETHYL (4R)-4-{[(2R,5S)-5-{[N-(TERT-BUTOXYCARBONYL)-L-SERYL]AMINO}-6-METHYL-2-(3-METHYLBUT-2-EN-1-YL)-4-OXOHEPTANOYL]AMINO}-5-[(3R)-2-OXOPYRROLIDIN-3-YL]PENTANOATE	Grum-Tokars, V.	HKL-2000	91.27%	-	APS (22-BM)	REFMAC	2007-07-05	17855091	-	-	http://covid-19.bioreproducibility.org/static/data/2qiq/2qiq_refined.pdb	http://covid-19.bioreproducibility.org/static/data/2qiq/2qiq_refined.mtz	25.30%	Placed the coordinates in a standardized location in the unit cell. The inhibitor was re-refined after truncation to terminal carboxyl groups, assuming that the ester groups had been eliminated by hydrolysis before crystal formation, a supposition that is supported by the well-defined and abrupt limits of the electron density at the ends of both carboxyl groups.	While a large central part of the inhibitor is well defined in the electron density, the ethyl and t-butyl ester groups of the inhibitor molecule lack any electron density. The coordinates are NOT in a standardized location in the unit cell.	Replicase polyprotein 1ab - 3CL proteinase	5.3	significant	Yes	Yes	-		17.6	14.4	34.0
3d0g	2.80 Å	2008-07-08	Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2	X-ray	NDG, NAG	SARS-CoV	Spike protein	Pathogen-host interaction	21.40%	27.90%	N/A		2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE;N-ACETYL-D-GLUCOSAMINE	Li, F.	DENZO	-	-	APS (19-BM)	REFMAC, CNS	2008-05-01	18448527	ZN	https://molstack.bioreproducibility.org/project/view/hnlY2nbqOGN6OoG7s3qz/	http://covid-19.bioreproducibility.org/static/data/3d0g/3d0g_refined.pdb	http://covid-19.bioreproducibility.org/static/data/3d0g/3d0g_refined.mtz	25.50%	Placed the coordinates in a standardized location in the unit cell. Corrected carbohydrate names, added several new carbohydrates. Fixed several rotamer outliers.	Not connected NAG molecules, not satisfactory Zn ion coordination. Unlikely assignment of the carbohydrate moieties bound to asparagine side chains (NDG rather than the expected NAG). Several carbohydrate moieties can be added to those already present, as well as to a few additional asparagine side chains. Coordinates are outside of the unit cell (not according to standardised placement)	Angiotensin-converting enzyme 2; Spike glycoprotein - residues 324-502	3.3	moderate	Yes	Yes	-		15.5	24.9	15.9
3d0h	3.10 Å	2008-07-08	Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2	X-ray	NDG, NAG	SARS-CoV	Spike protein	Pathogen-host interaction	22.10%	30.20%	N/A		2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE;N-ACETYL-D-GLUCOSAMINE	Li, F.		-	-	APS (19-BM)	REFMAC	2008-05-01	18448527	ZN	https://molstack.bioreproducibility.org/project/view/WrI2XslE978LiF95PQYo/	http://covid-19.bioreproducibility.org/static/data/3d0h/3d0h_refined.pdb	http://covid-19.bioreproducibility.org/static/data/3d0h/3d0h_refined.mtz	26.60%	Placed the coordinates in a standardized location in the unit cell. Corrected carbohydrate names, added several new carbohydrates. Fixed several rotamer outliers.	Not connected NAG molecules, not satisfactory Zn ion coordination. Unlikely assignment of the carbohydrate moieties bound to asparagine side chains (NDG rather than the expected NAG). Several carbohydrate moieties can be added to those already present, as well as to a few additional asparagine side chains. Coordinates are outside of the unit cell (not according to standardised placement)	Angiotensin-converting enzyme 2; Spike glycoprotein - residues 324-502	11.4	moderate	Yes	Yes	-		7.7	70.9	9.3
3d0i	2.90 Å	2008-07-08	Crystal structure of spike protein receptor-binding domain from the 2005-2006 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2	X-ray	NDG, NAG	SARS-CoV	Spike protein	Pathogen-host interaction	22.40%	27.80%	N/A		2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE;N-ACETYL-D-GLUCOSAMINE	Li, F.		-	-	APS (19-BM)	REFMAC	2008-05-01	18448527	ZN	https://molstack.bioreproducibility.org/project/view/tyBAIB4W8gsYJT2boa8Q/	http://covid-19.bioreproducibility.org/static/data/3d0i/3d0i_refined.pdb	http://covid-19.bioreproducibility.org/static/data/3d0i/3d0i_refined.mtz	26.20%	Placed the coordinates in a standardized location in the unit cell. Corrected carbohydrate names, added several new carbohydrates. Fixed several rotamer outliers.	Not connected NAG molecules, not satisfactory Zn ion coordination. Unlikely assignment of the carbohydrate moieties bound to asparagine side chains (NDG rather than the expected NAG). Several carbohydrate moieties can be added to those already present, as well as to a few additional asparagine side chains. Coordinates are outside of the unit cell (not according to standardised placement)	Angiotensin-converting enzyme 2; Spike glycoprotein - residues 324-502	4.5	moderate	Yes	Yes	-		16.0	37.2	9.7
3bgf	3.00 Å	2008-12-02	X-ray crystal structure of the SARS coronavirus spike receptor binding domain in complex with F26G19 Fab	X-ray	-	SARS-CoV	Spike protein	Pathogen-host interaction	23.40%	28.60%	13.20%		-	Pak, J.E., Sharon, C., Satkunarajah, M., Auperin, T.C., Cameron, C.M., Kelvin, D.J., Seetharaman, J., Cochrane, A., Plummer, F.A., Berry, J.D., Rini, J.M.	HKL-2000	94.40%	-	NSLS (X12C)	REFMAC	2007-11-26	19324051	-	-	-	-	N/A	-	-	Spike protein S1; F26G19 Fab	18.3	-		No	-		12.3	73.7	20.1
3aw0	2.30 Å	2011-12-14	Structure of SARS 3CL protease with peptidic aldehyde inhibitor	X-ray	-	SARS-CoV	NSP5 (Main protease)	Functional ligand	22.48%	28.64%	8.20%	peptide ACE-SER-ALA-VAL-LEU-HIS-H	-	Akaji, K., Konno, H., Mitsui, H., Teruya, K., Hattori, Y., Ozaki, T., Kusunoki, M., Sanjho, A.	HKL-2000	99.28%	21.786	Photon Factory (BL-6A)	REFMAC	2011-03-09	22014094	-	-	-	-	N/A	-	-	3C-Like Proteinase; peptide ACE-SER-ALA-VAL-LEU-HIS-H	5.8	-		No	-		12.2	38.5	17.5
3sci	2.90 Å	2012-02-08	Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus human strain complexed with human receptor ACE2	X-ray	-	SARS-CoV	Spike protein	Pathogen-host interaction	22.59%	28.26%	N/A		-	Wu, K., Peng, G., Wilken, M., Geraghty, R., Li, F.	HKL-2000	93.40%	-	APS (19-ID)	REFMAC; CNS	2011-06-07	-	ZN	-	http://covid-19.bioreproducibility.org/static/data/3sci/3sci_refined_2_tls.pdb	http://covid-19.bioreproducibility.org/static/data/3sci/3sci_refined_2.mtz	27.70%	Placed the coordinates in a standardized location in the unit cell. Added a water molecule to each Zn cation and added LINKs between Zn and each of the coordinating ligands. Removed Cl ions. Fixed someRamachandran outliers. Many more Ramachandran outliers are left; the refinement is stopped due to availability of better structures for the same proteins. Sugar moieties were not added.	Zinc cations are placed without proper coordination. There are also two Cl ions in the structure, chemically feasible, but with poor/lacking electron density. Multiple Ramachandran outliers. Some residues have electron density for the sugar moieties due to glycosylation. The coordinates are NOT in a standardized location in the unit cell.	Angiotensin-converting enzyme 2 - UNP residues 19-615; Spike glycoprotein - receptor binding domain (UNP residues 306-527)	2.4	minimal	Yes	Yes	-	-	13.9	26.8	10.7
3sck	3.00 Å	2012-02-08	Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2	X-ray	-	SARS-CoV	Spike protein	Pathogen-host interaction	23.92%	28.53%	N/A		-	Wu, K., Peng, G., Wilken, M., Geraghty, R., Li, F.	HKL-2000	91.70%	-	APS (19-ID)	REFMAC; CNS	2011-06-07	-	ZN	-	http://covid-19.bioreproducibility.org/static/data/3sck/3sck_refined_tls_2.pdb	http://covid-19.bioreproducibility.org/static/data/3sck/3sck_refined_tls_2.mtz	29.50%	Placed the coordinates in a standardized location in the unit cell. Added a water molecule to each Zn cation and added LINKs between Zn and each of the coordinating ligands. Removed Cl ions. Fixed someRamachandran outliers. Many more Ramachandran outliers are left; the refinement is stopped due to availability of better structures for the same proteins. Sugar moieties were not added.	Zinc cations are placed without proper coordination. There are also two Cl ions in the structure, chemically feasible, but with poor/lacking electron density. Multiple Ramachandran outliers. Some residues have electron density for the sugar moieties due to glycosylation. The coordinates are NOT in a standardized location in the unit cell.	Angiotensin-converting enzyme 2 chimera - SEE REMARK 999; Spike glycoprotein - receptor binding domain (UNP residues 324-502)	11.8	minimal	Yes	Yes	-	-	12.7	71.9	4.6
3scl	3.00 Å	2012-02-08	Crystal structure of spike protein receptor-binding domain from SARS coronavirus epidemic strain complexed with human-civet chimeric receptor ACE2	X-ray	-	SARS-CoV	Spike protein	Pathogen-host interaction	23.88%	29.18%	N/A		-	Wu, K., Peng, G., Wilken, M., Geraghty, R., Li, F.	HKL-2000	97.70%	-	APS (24-ID-E)	REFMAC; CNS	2011-06-07	-	ZN	-	http://covid-19.bioreproducibility.org/static/data/3scl/3scl_refined_2_tls.pdb	http://covid-19.bioreproducibility.org/static/data/3scl/3scl_refined_2_coot.mtz	29.00%	Placed the coordinates in a standardized location in the unit cell. Added a water molecule to each Zn cation and added LINKs between Zn and each of the coordinating ligands. Replaced Cl with water molecules. Fixed multiple Ramachandran outliers. Many more Ramachandran outliers are left; the refinement is stopped due to availability of better structures for the same proteins. Sugar moieties were not added.	Zinc cations are placed without proper coordination. There are also two Cl ions in the structure, chemically feasible, but with poor/lacking electron density. Multiple Ramachandran outliers. Some residues have electron density for the sugar moieties due to glycosylation. The coordinates are NOT in a standardized location in the unit cell.	Angiotensin-converting enzyme 2 chimera - SEE REMARK 999; Spike glycoprotein - receptor binding domain (UNP residues 324-502)	11.2	minimal	Yes	Yes	-	-	10.3	67.1	10.1
4rsp	1.62 Å	2015-06-17	X-ray structure of MERS-CoV nsp5 protease bound with a designed inhibitor	X-ray	-	SARS-CoV	NSP5 (Main protease)	Functional ligand	16.18%	20.27%	N/A	Peptide inhibitor	-	Tomar, S., Mesecar, A.D.	MOSFLM	95.00%	-	APS (31-ID)	PHENIX	2014-11-10	26055715	-	-	http://covid-19.bioreproducibility.org/static/data/4rsp/4rsp_refined.pdb	http://covid-19.bioreproducibility.org/static/data/4rsp/4rsp_refined.mtz	21.20%	Placed the coordinates in a standardized location in the unit cell. Reset occupancies to n/m integral values.	Many residues with unbelievable occupancies (0.74/0.26, 0.61/0.39 etc.). The coordinates are NOT in a standardized location in the unit cell.	Orf1a protein; Peptide inhibitor	81.9	minimal	Yes	Yes	-		80.8	72.8	88.8
5zuv	2.21 Å	2019-04-10	Crystal Structure of the Human Coronavirus 229E HR1 motif in complex with pan-CoVs inhibitor EK1	X-ray	-	HCoV-229E	Spike protein	Functional ligand	20.19%	24.81%	N/A			Yan, L., Yang, B., Wilson, I.A.	HKL-3000	98.75%	18.9	SSRF (BL19U1)	REFMAC	2018-05-08	30989115	-	-	http://covid-19.bioreproducibility.org/static/data/5zuv/5zuv_refined.pdb	http://covid-19.bioreproducibility.org/static/data/5zuv/5zuv_refined.mtz	23.00%	Repositioned the coordinates with ACHESYM and improved the model by adding residue Leu8 in chain c (inhibitor peptide), correcting conformations of 13 residues (Lys23b, Gln788B/A, Glu789A, Asn790B, Gln791A/B, Leu794A, Val806C, Gln839C, Thr848B, Gln856A/B), and adding 43 water molecules.	Structure of good quality, without any additional ligands and without missing side chains. Most of the protein residues outside of the reference unit cell. The fusion molecule (HR1 motif and the peptidic inhibitor) is represented in the deposit as a single protein chain with consecutive residue numbering, not as separte chains (as in 5zvk and 5zvm).	Spike glycoprotein,Spike glycoprotein,inhibitor EK1 - UNP residues 785-873	49.3	moderate	Yes	Yes	-		38.2	43.3	88.0
5zvk	3.31 Å	2019-04-10	Crystal Structure of the Human Coronavirus MERS HR1 motif in complex with pan-CoVs inhibitor EK1	X-ray	-	MERS	Spike protein	Functional ligand	25.90%	31.36%	N/A			Yan, L., Yang, B., Wilson, I.A.	HKL-3000	99.85%	20.7	SSRF (BL19U1)	PHENIX	2018-05-11	30989115	-	-	-	-	N/A	-	Structure of good quality, without any additional ligands and with no missing side chains. Most of the protein residues outside of the reference unit cell.	Human Coronavirus MERS HR1 motif - UNP residues 984-1062; pan-CoV inhibitory peptide EK1	8.3	minimal		No	-		6.3	23.7	48.2
5zvm	3.30 Å	2019-04-10	Crystal Structure of the Human Coronavirus SARS HR1 motif in complex with pan-CoVs inhibitor EK1	X-ray	-	SARS-CoV	Spike protein	Functional ligand	24.76%	30.14%	N/A		-	Yan, L., Yang, B., Wilson, I.A.	HKL-3000	99.90%	11.9	SSRF (BL19U1)	REFMAC	2018-05-11	30989115	-	-	-	-	N/A	not done	The coordinates are NOT in a standardized location in the unit cell.	Spike glycoprotein - UNP residues 892-970; pan-CoV inhibitory peptide EK1	14.7	minimal		No	-		7.8	14.3	75.4
6u7e	3.00 Å	2019-11-13	HCoV-229E RBD Class III in complex with human APN	X-ray	NAG, BMA	HCoV-229E	Spike protein	Pathogen-host interaction	20.35%	24.39%	7.10%		N-ACETYL-D-GLUCOSAMINE;BETA-D-MANNOSE	Tomlinson, A.C.A., Li, Z., Rini, J.M.	XDS	99.78%	11.06	CLSI (08ID-1)	PHENIX	2019-09-02	31650956	ZN	-	-	-	N/A	-	-	Aminopeptidase N - ectodomain (UNP residues 66-967); Spike glycoprotein	68.2	-		No			42.5	86.1	78.3
6u7f	2.75 Å	2019-11-13	HCoV-229E RBD Class IV in complex with human APN	X-ray	NAG	HCoV-229E	Spike protein	Pathogen-host interaction	19.04%	22.51%	6.80%		N-ACETYL-D-GLUCOSAMINE	Tomlinson, A.C.A., Li, Z., Rini, J.M.	XDS	99.86%	16.24	CLSI (08ID-1)	PHENIX	2019-09-02	31650956	ZN	-	-	-	N/A	-	-	Aminopeptidase N - ectodomain (UNP residues 66-967); Spike glycoprotein	78.6	-		No			61.2	86.0	84.9
6u7g	2.35 Å	2019-11-13	HCoV-229E RBD Class V in complex with human APN	X-ray	NAG	HCoV-229E	Spike protein	Pathogen-host interaction	17.86%	21.84%	5.20%		N-ACETYL-D-GLUCOSAMINE	Tomlinson, A., Li, Z., Rini, J.M.	HKL-2000	96.03%	14.9	APS (23-ID-B)	PHENIX	2019-09-02	31650956	ZN	-	http://covid-19.bioreproducibility.org/static/data/6u7g/6u7g_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6u7g/6u7g_refined.mtz	22.40%	Fixed minor issues with geometry and solvent	-	Aminopeptidase N - ectodomain (UNP residues 66-967); Spike protein - receptor-binding domain (UNP residues 292-432)	57.4	minimal		Yes			67.7	33.4	83.9
6u7h	3.10 Å	2019-11-13	Cryo-EM structure of the HCoV-229E spike glycoprotein	Cryo-EM	NAG, BMA, MAN	HCoV-229E	Spike protein	No functional ligands	N/A	N/A	N/A		N-ACETYL-D-GLUCOSAMINE;BETA-D-MANNOSE;ALPHA-D-MANNOSE	Li, Z., Benlekbir, S., Rubinstein, J.L., Rini, J.M.		-	-	()		2019-09-02	31650956	-	-	-	-	N/A	-	-	spike glycoprotein	N/A	-		No	-		N/A	N/A	N/A
6lu7	2.16 Å	2020-02-05	The crystal structure of COVID-19 main protease in FL N3	X-ray	PRD_002214	SARS-CoV-2	NSP5 (Main protease)	Functional ligand	20.20%	23.50%	18.90%	N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-N~1~-((1R,2Z)-4-(BENZYLOXY)-4-OXO-1-{[(3R)-2-OXOPYRROLIDIN-3-YL]METHYL}BUT-2-ENYL)-L-LEUCINAMIDE		Liu, X., Zhang, B., Jin, Z., Yang, H., Rao, Z.	xia2	99.49%	6.3	SSRF (BL17U1)	PHENIX	2020-01-26	32272481	-	https://molstack.bioreproducibility.org/project/view/x9jJQnlGN25TRBSRdxJm/	http://covid-19.bioreproducibility.org/static/data/6lu7/6lu7_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6lu7/6lu7_refined.mtz	22.50%	The phenyl group was removed from the inhibitor. After re-refinement of the model negative density disappeared. A few minor model corrections.	The terminal phenyl group of the inhibitor with negative difference electron density, possible hydrolysis.	SARS-CoV-2 main protease; N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-N~1~-((1R,2Z)-4-(BENZYLOXY)-4-OXO-1-{[(3R)-2-OXOPYRROLIDIN-3-YL]METHYL}BUT-2-ENYL)-L-LEUCINAMIDE	40.8	moderate	Yes	Yes	-		51.1	33.4	68.9
6lvn	2.47 Å	2020-02-26	Structure of the 2019-nCoV HR2 Domain	X-ray	-	SARS-CoV-2	Spike protein	No functional ligands	21.48%	25.80%	13.24%			Zhu, Y., Sun, F.	XDS	99.26%	19.06	ROTATING ANODE ()	PHENIX	2020-02-04	-	-	-	-	-	27.20%	not done	Structure of good quality. No ligands bound. No Ramachandran outliers, no rotamer outliers, and no missing side chains. Four helices are not placed in the ASU as a single oligomer, but as two independent dimers	SARS-coV-2 S2 subunit - HR2 domain	52.0	minimal		No	-	-	29.3	75.4	69.9
6lxt	2.90 Å	2020-02-26	Structure of post fusion core of 2019-nCoV S2 subunit	X-ray	PG4	SARS-CoV-2	Spike protein	No functional ligands	25.93%	28.96%	16.00%		TETRAETHYLENE GLYCOL	Zhu, Y., Sun, F.	MOSFLM	94.02%	6.3	ROTATING ANODE ()	REFMAC	2020-02-11	32231345	ZN	-	-	-	N/A	not done	Structure of good quality. It has one Ramachandran outlier, probably justified. No missing side-chains. Several side-chain outliers, but most are not trivial to fix - a common problem at low resolution (% outliers is low). Most of the protein is outside of the unit cell. A metal cation (Zn2+) is missing between Asp1199 of chain B and Asp1199 of chain F. At the interface between Asp1163 and Asp1165 of chain B and a symmetry mate of Glu1188 and Asp1184 of chain A (crystallographic interface between two six-helix bundles), a molecule of PEG is modeled instead of, most probably, one or two Zn2+ ions. This PEG molecule is hilariously mismodelled: it has severe clashes with the protein residues, all contacts are polar-to-nonpolar, and it is too curled-up	SARS-CoV-2 S2 subunit, SARS-CoV-2 S2 subunit - HR1 domain,HR2 domain	11.5	moderate		No	-		10.9	48.2	29.3
6vsb	3.46 Å	2020-02-26	Prefusion 2019-nCoV spike glycoprotein with a single receptor-binding domain up	Cryo-EM	NAG	SARS-CoV-2	Spike protein	No functional ligands	N/A	N/A	N/A		N-ACETYL-D-GLUCOSAMINE	Wrapp, D., Wang, N., Corbett, K.S., Goldsmith, J.A., Hsieh, C., Abiona, O., Graham, B.S., McLellan, J.S.		-	-	()		2020-02-10	32075877	-	-	-	-	N/A	-	-	SARS-CoV-2 spike glycoprotein	N/A	-		No	-		N/A	N/A	N/A
6vw1	2.68 Å	2020-03-04	Structure of 2019-nCoV chimeric receptor-binding domain complexed with its receptor human ACE2	X-ray	NAG, BMA	SARS-CoV-2	Spike protein	Pathogen-host interaction	19.70%	22.88%	8.10%		N-ACETYL-D-GLUCOSAMINE;BETA-D-MANNOSE	Shang, J., Ye, G., Shi, K., Wan, Y.S., Aihara, H., Li, F.	HKL-2000	98.97%	12.08	APS (24-ID-E)	PHENIX, REFMAC	2020-02-18	32225175	ZN	-	http://covid-19.bioreproducibility.org/static/data/6vw1/6vw1_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6vw1/6vw1_refined.mtz	24.00%	Placed the coordinates in a standardized location in the unit cell. MC - refined the structure	Zn2+ cations have abnormally high B factors (135 and 196 Å2) and do not make any contacts with their environment that would indicate proper coordination. Otherwise the structure seems to be in good agreement with the electron density. The coordinates are NOT in a standardized location in the unit cell.	Angiotensin-converting enzyme 2; SARS-CoV-2 chimeric RBD	54.7	minimal	Yes	Yes	-		57.6	75.5	46.7
6vww	2.20 Å	2020-03-04	Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2.	X-ray	ACY	SARS-CoV-2	NSP15	No functional ligands	15.77%	17.77%	17.40%		ACETIC ACID	Kim, Y., Jedrzejczak, R., Maltseva, N., Endres, M., Godzik, A., Michalska, K., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	98.08%	10.0	APS (19-ID)	PHENIX	2020-02-20	32304108	MG	-	-	-	N/A	-	-	NSP15 endoribnuclease	87.9	-		No			93.4	95.1	83.6
6vxs	2.03 Å	2020-03-04	Crystal Structure of ADP ribose phosphatase of NSP3 from SARS CoV-2	X-ray	NHE	SARS-CoV-2	NSP3: X-domain	No functional ligands	18.64%	23.35%	N/A	2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID	2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID	Kim, Y., Jedrzejczak, R., Maltseva, N., Endres, M., Mececar, A., Michalska, K., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	84.84%	8.44	APS (19-ID)	PHENIX	2020-02-24	-	-	-	-	-	N/A	-	-	ADP-ribose-1"-monophosphatase	77.0	-		No		-	52.8	89.2	85.5
6y2e	1.75 Å	2020-03-04	Crystal structure of the free enzyme of the SARS-CoV-2 (2019-nCoV) main protease	X-ray	-	SARS-CoV-2	NSP5 (Main protease)	No functional ligands	17.12%	22.24%	8.20%			Zhang, L., Sun, X., Hilgenfeld, R.	XDS	99.97%	15.0	BESSY (14.2)	REFMAC	2020-02-15	32198291	-	-	http://covid-19.bioreproducibility.org/static/data/6y2e/6y2e_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6y2e/6y2e_refined.mtz	21.90%	Fixed minor issues with side chain rotamers.	Protein chains are modeled well.	SARS-CoV-2 (2019-nCoV) main protease	65.3	minimal	Yes	Yes	-		63.9	63.2	73.6
6y2f	1.95 Å	2020-03-04	Crystal structure (monoclinic form) of the complex resulting from the reaction between SARS-CoV-2 (2019-nCoV) main protease and tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate (alpha-ketoamide 13b)	X-ray	O6K	SARS-CoV-2	NSP5 (Main protease)	Functional ligand	17.79%	21.91%	7.60%	~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate	~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate	Zhang, L., Lin, D., Sun, X., Hilgenfeld, R.	XDS	99.95%	15.5	BESSY (14.2)	REFMAC	2020-02-15	32198291	-	-	http://covid-19.bioreproducibility.org/static/data/6y2f/6y2f_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6y2f/6y2f_refined.mtz	20.60%	Re-refinement with a sodium cation modeled at the highest peak site. A few side chain rotamer corrections. Application of TLS parameters.	Structure of good quality. High positive peak coordinated by five carbonyl oxygen atoms and one water molecule; octahedral coordination.	SARS-CoV-2 (2019-nCoV) main protease	44.5	moderate	Yes	Yes	-		66.9	35.1	58.4
6y2g	2.20 Å	2020-03-04	Crystal structure (orthorhombic form) of the complex resulting from the reaction between SARS-CoV-2 (2019-nCoV) main protease and tert-butyl (1-((S)-1-(((S)-4-(benzylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-3-cyclopropyl-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate (alpha-ketoamide 13b)	X-ray	O6K	SARS-CoV-2	NSP5 (Main protease)	Functional ligand	18.62%	24.73%	17.00%	~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate	~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate	Zhang, L., Lin, D., Sun, X., Hilgenfeld, R.	XDS	99.95%	13.1	BESSY (14.2)	REFMAC	2020-02-15	32198291	-	-	http://covid-19.bioreproducibility.org/static/data/6y2g/6y2g_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6y2g/6y2g_refined.mtz	24.00%	Fixed minor issues with side chain rotamers and a couple of orphaned solvent molecules.	Protein chains are modeled well.	SARS-CoV-2 (2019-nCoV) main protease	49.7	minimal	No	Yes	-		39.0	77.7	53.6
5r7y	1.65 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z45617795	X-ray	JFM	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.94%	23.67%	11.30%	N-(2-phenylethyl)methanesulfonamide	N-(2-phenylethyl)methanesulfonamide	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	98.82%	5.8	Diamond (I04-1)	REFMAC	2020-03-03	-	-	-	-	-	24.10%	not done	Weak density for the ligand on the primary 2Fo-Fc map.	SARS-CoV-2 main protease	-	moderate		No		-	49.5	-	51.9
5r7z	1.59 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z1220452176	X-ray	HWH	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	24.47%	27.65%	9.60%	~{N}-[2-(5-fluoranyl-1~{H}-indol-3-yl)ethyl]ethanamide	~{N}-[2-(5-fluoranyl-1~{H}-indol-3-yl)ethyl]ethanamide	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	98.87%	6.2	Diamond (I04-1)	REFMAC	2020-03-03	-	-	https://molstack.bioreproducibility.org/collection/view/GqjIgzdHOk3yuQaO0ukE/	-	-	24.30%	not done	Weak density for the ligand on the primary 2Fo-Fc map.	SARS-CoV-2 main protease	43.6	moderate		No		-	53.2	46.9	58.8
5r80	1.93 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z18197050	X-ray	RZG	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	22.16%	27.57%	11.30%	methyl 4-sulfamoylbenzoate	methyl 4-sulfamoylbenzoate	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	98.85%	6.0	Diamond (I04-1)	REFMAC	2020-03-03	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	37.1	-		No		-	51.7	40.5	53.8
5r81	1.95 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z1367324110	X-ray	RZJ	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.20%	24.94%	16.20%	1-methyl-3,4-dihydro-2~{H}-quinoline-7-sulfonamide	1-methyl-3,4-dihydro-2~{H}-quinoline-7-sulfonamide	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	99.77%	4.0	Diamond (I04-1)	REFMAC	2020-03-03	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	39.6	-		No		-	36.9	63.0	51.1
5r82	1.31 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z219104216	X-ray	RZS	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.03%	21.16%	5.00%	6-(ethylamino)pyridine-3-carbonitrile	6-(ethylamino)pyridine-3-carbonitrile	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	87.51%	9.7	Diamond (I04-1)	REFMAC	2020-03-03	-	-	-	-	-	21.20%	not done	Weak density for the ligand on the primary 2Fo-Fc map.	SARS-CoV-2 main protease	-	moderate		No		-	73.8	-	50.6
5r83	1.58 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z44592329	X-ray	K0G	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	23.27%	26.52%	10.00%	N-phenyl-N'-pyridin-3-ylurea	N-phenyl-N'-pyridin-3-ylurea	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	99.39%	6.7	Diamond (I04-1)	REFMAC	2020-03-03	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	49.6	-		No		-	71.1	54.3	44.7
5r84	1.83 Å	2020-03-11	PanDDA analysis group deposition -- Crystal Structure of COVID-19 main protease in complex with Z31792168	X-ray	GWS	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	21.67%	29.26%	14.00%	2-cyclohexyl-~{N}-pyridin-3-yl-ethanamide	2-cyclohexyl-~{N}-pyridin-3-yl-ethanamide	Fearon, D., Powell, A.J., Douangamath, A., Owen, C.D., Wild, C., Krojer, T., Lukacik, P., Strain-Damerell, C.M., Walsh, M.A., von Delft, F.	XDS	99.04%	5.6	Diamond (I04-1)	REFMAC	2020-03-03	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	14.0	-		No		-	10.0	43.5	41.9
6m03	2.00 Å	2020-03-11	The crystal structure of COVID-19 main protease in apo form	X-ray	-	SARS-CoV-2	NSP5 (Main protease)	No functional ligands	19.62%	24.58%	3.90%			Zhang, B., Zhao, Y., Jin, Z., Liu, X., Yang, H., Rao, Z.	XDS	99.71%	16.29	SSRF (BL18U)	PHENIX	2020-02-19	-	-	-	http://covid-19.bioreproducibility.org/static/data/6m03/6m03_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6m03/6m03_refined.mtz	24.21%	Placed the coordinates in a standardized location in the unit cell. Added TLS (9 groups), added waters, fixed ramachandran outliers, Flipped side chains GLN 74, HIS 164, ASN 203. Changed rotamers MET 17, MET 165, ARG 298, GLN 189. Added alternative conformation for PHE 294.	Flipped sidechains, missing rotamers. The coordinates are NOT in a standardized location in the unit cell. No ligands, no metals.	SARS-CoV-2 main protease	54.4	moderate	Yes	Yes	-	-	40.7	67.8	70.9
6m17	2.90 Å	2020-03-11	The 2019-nCoV RBD/ACE2-B0AT1 complex	Cryo-EM	NAG	SARS-CoV-2	Spike protein	Pathogen-host interaction	N/A	N/A	N/A		N-ACETYL-D-GLUCOSAMINE	Yan, R.H., Zhang, Y.Y., Li, Y.N., Xia, L., Guo, Y.Y., Zhou, Q.		-	-	()		2020-02-24	32132184	ZN	-	-	-	N/A	-	Poor map	Sodium-dependent neutral amino acid transporter B(0)AT1; Angiotensin-converting enzyme 2; SARS-coV-2 Receptor Binding Domain	N/A	moderate		No	-		N/A	N/A	N/A
6vxx	2.80 Å	2020-03-11	Structure of the SARS-CoV-2 spike glycoprotein (closed state)	Cryo-EM	NAG	SARS-CoV-2	Spike protein	No functional ligands	N/A	N/A	N/A		N-ACETYL-D-GLUCOSAMINE	Walls, A.C., Park, Y.J., Tortorici, M.A., Wall, A., Seattle Structural Genomics Center for Infectious Disease (SSGCID), McGuire, A.T., Veesler, D.		-	-	()		2020-02-25	32155444	-	-	-	-	N/A	-	-	SARS-CoV-2 spike glycoprotein - ectodomain	N/A	-		No	-		N/A	N/A	N/A
6vyb	3.20 Å	2020-03-11	SARS-CoV-2 spike ectodomain structure (open state)	Cryo-EM	NAG	SARS-CoV-2	Spike protein	No functional ligands	N/A	N/A	N/A		N-ACETYL-D-GLUCOSAMINE	Walls, A.C., Park, Y.J., Tortorici, M.A., Wall, A., Seattle Structural Genomics Center for Infectious Disease (SSGCID), McGuire, A.T., Veesler, D.		-	-	()		2020-02-25	32155444	-	-	-	-	N/A	-	-	SARS-CoV-2 spike glycoprotein - ectodomain	N/A	-		No	-		N/A	N/A	N/A
6vyo	1.70 Å	2020-03-11	Crystal structure of RNA binding domain of nucleocapsid phosphoprotein from SARS coronavirus 2	X-ray	MES	SARS-CoV-2	Nucleocapsid	No functional ligands	15.99%	20.49%	13.10%	2-(N-MORPHOLINO)-ETHANESULFONIC ACID	2-(N-MORPHOLINO)-ETHANESULFONIC ACID	Chang, C., Michalska, K., Jedrzejczak, R., Maltseva, N., Endres, M., Godzik, A., Kim, Y., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	87.28%	6.9	APS (19-ID)	PHENIX	2020-02-27	-	ZN	-	http://covid-19.bioreproducibility.org/static/data/6vyo/6vyo_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6vyo/6vyo_refined.mtz	21.20%	-	-	RNA binding domain of nucleocapsid protein	77.9	-		Yes		-	78.8	64.4	87.0
6w01	1.90 Å	2020-03-11	The 1.9 A Crystal Structure of NSP15 Endoribonuclease from SARS CoV-2 in the Complex with a Citrate	X-ray	-	SARS-CoV-2	NSP15	No functional ligands	16.05%	18.49%	11.20%			Kim, Y., Jedrzejczak, R., Maltseva, N., Endres, M., Godzik, A., Michalska, K., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	98.70%	13.11	APS (19-ID)	PHENIX	2020-02-28	32304108	-	-	-	-	N/A	-	-	NSP15 Endoribonuclease	82.8	-		No			90.8	71.3	83.5
6w02	1.50 Å	2020-03-11	Crystal Structure of ADP ribose phosphatase of NSP3 from SARS CoV-2 in the complex with ADP ribose	X-ray	APR	SARS-CoV-2	NSP3: X-domain	Functional ligand	14.96%	17.29%	7.50%	ADENOSINE-5-DIPHOSPHORIBOSE	ADENOSINE-5-DIPHOSPHORIBOSE	Michalska, K., Kim, Y., Jedrzejczak, R., Maltseva, N., Endres, M., Mececar, A., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	79.80%	25.3	APS (19-ID)	PHENIX	2020-02-28	-	-	-	-	-	N/A	-	-	ADP ribose phosphatase	87.4	-		No		-	94.8	89.2	84.1
6y84	1.39 Å	2020-03-11	COVID-19 main protease with unliganded active site (2019-nCoV, coronavirus disease 2019, SARS-CoV-2)	X-ray	-	SARS-CoV-2	NSP5 (Main protease)	No functional ligands	17.79%	20.00%	5.90%			Owen, C.D., Lukacik, P., Strain-Damerell, C.M., Douangamath, A., Powell, A.J., Fearon, D., Brandao-Neto, J., Crawshaw, A.D., Aragao, D., Williams, M., Flaig, R., Hall, D., McAauley, K., Stuart, D.I., von Delft, F., Walsh, M.A.	DIALS; xia2	97.50%	9.7	Diamond (I04-1)	BUSTER, REFMAC	2020-03-03	-	-	-	http://covid-19.bioreproducibility.org/static/data/6y84/6y84_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6y84/6y84-sf_refined.mtz	20.20%	-	Structure of good quality.	Non-structural polyprotein 1ab	66.6	minimal		Yes	-	-	82.5	37.7	83.2
6lzg	2.50 Å	2020-03-18	Structure of novel coronavirus spike receptor-binding domain complexed with its receptor ACE2	X-ray	NAG	SARS-CoV-2	Spike protein	Pathogen-host interaction	18.46%	21.42%	12.90%		N-ACETYL-D-GLUCOSAMINE	Wang, Q.H., Song, H., Qi, J.X.	HKL-2000	99.88%	26.7	SSRF (BL17U1)	PHENIX	2020-02-19	32275855	ZN	-	-	-	N/A	-	-	Angiotensin-converting enzyme 2; SARS-CoV-2 Spike receptor-binding domain	43.0	-		No	-		70.4	31.7	55.4
6m0j	2.45 Å	2020-03-18	Crystal structure of 2019-nCoV spike receptor-binding domain bound with ACE2	X-ray	NAG	SARS-CoV-2	Spike protein	Pathogen-host interaction	19.57%	23.75%	12.00%		N-ACETYL-D-GLUCOSAMINE	Wang, X., Lan, J., Ge, J., Yu, J., Shan, S.	XDS	99.91%	24.2	SSRF (BL17U1)	PHENIX	2020-02-21	32225176	ZN	-	-	-	N/A	-	-	Angiotensin-converting enzyme 2; SARS-CoV-2 receptor-binding domain	48.9	-		No	-		59.6	58.2	50.9
6m3m	2.70 Å	2020-03-18	Crystal structure of SARS-CoV-2 nucleocapsid protein N-terminal RNA binding domain	X-ray	-	SARS-CoV-2	Nucleocapsid	No functional ligands	25.78%	29.34%	10.43%			Chen, S., Kang, S.	CrysalisPro	99.00%	14.97	ROTATING ANODE ()	PHENIX	2020-03-04	32363136	-	-	-	-	28.90%	not done	Structure of good quality. No ligands. Some ramachandran outliers at the C-terminus. Many slashed side chains due to the lack of electron density – some can be built.	SARS-CoV-2 nucleocapsid protein - N-terminal RNA binding domain	5.0	minimal		No	-		9.8	22.7	32.4
6w4b	2.95 Å	2020-03-18	The crystal structure of Nsp9 replicase protein of COVID-19	X-ray	-	SARS-CoV-2	NSP9	No functional ligands	23.98%	27.60%	19.00%			Tan, K., Kim, Y., Jedrzejczak, R., Maltseva, N., Endres, M., Michalska, K., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	97.09%	17.4	APS (19-BM)	PHENIX	2020-03-10	-	-	-	-	-	N/A	-	-	Nsp9 replicase protein	7.4	-		No		-	17.1	21.5	36.3
6w4h	1.80 Å	2020-03-18	1.80 Angstrom Resolution Crystal Structure of NSP16 - NSP10 Complex from SARS-CoV-2	X-ray	SO3, SAM, BDF	SARS-CoV-2	NSP10/NSP16	Protein-protein complex	14.90%	16.27%	6.00%	S-ADENOSYLMETHIONINE	SULFITE ION;S-ADENOSYLMETHIONINE;BETA-D-FRUCTOPYRANOSE	Minasov, G., Shuvalova, L., Rosas-Lemus, M., Kiryukhina, O., Wiersum, G., Godzik, A., Jaroszewski, L., Stogios, P.J., Skarina, T., Satchell, K.J.F., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	99.97%	29.3	APS (21-ID-F)	REFMAC	2020-03-10	-	ZN	-	-	-	N/A	-	-	SARS-CoV-2 NSP16; SARS-CoV-2 NSP10	63.8	-		No		-	96.9	13.5	87.4
6y7m	1.90 Å	2020-03-18	Crystal structure of the complex resulting from the reaction between the SARS-CoV main protease and tert-butyl (1-((S)-3-cyclohexyl-1-(((S)-4-(cyclopropylamino)-3,4-dioxo-1-((S)-2-oxopyrrolidin-3-yl)butan-2-yl)amino)-1-oxopropan-2-yl)-2-oxo-1,2-dihydropyridin-3-yl)carbamate	X-ray	OEW	SARS-CoV	NSP5 (Main protease)	Functional ligand	20.62%	25.76%	4.80%	~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclohexyl-1-[[(2~{S},3~{R})-4-(cyclopropylamino)-3-oxidanyl-4-oxidanylidene-1-[(3~{R})-2-oxidanylidene-3,4-dihydropyrrol-3-yl]butan-2-yl]amino]-1-oxidanylidene-propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate	~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclohexyl-1-[[(2~{S},3~{R})-4-(cyclopropylamino)-3-oxidanyl-4-oxidanylidene-1-[(3~{R})-2-oxidanylidene-3,4-dihydropyrrol-3-yl]butan-2-yl]amino]-1-oxidanylidene-propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate	Zhang, L., Lin, D., Hilgenfeld, R.	XDS	98.99%	12.8	PETRA III, DESY (P11)	REFMAC	2020-03-01	-	-	-	http://covid-19.bioreproducibility.org/static/data/6y7m/6y7m_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6y7m/6y7m_refined.mtz	25.60%	Added one water molecule. Some minor difficult to correction issues.	Structure of good quality.	Replicase polyprotein 1a	31.4	minimal	Yes	Yes	-	-	29.8	43.8	60.9
5re4	1.88 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1129283193	X-ray	SZY	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.91%	26.64%	22.80%	N-(4-methylpyridin-3-yl)acetamide	N-(4-methylpyridin-3-yl)acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft	XDS	99.50%	3.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	32.4	-		No		-	23.1	58.4	55.1
5re5	2.07 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z33545544	X-ray	T0J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.11%	26.49%	25.90%	N~1~-phenylpiperidine-1,4-dicarboxamide	N~1~-phenylpiperidine-1,4-dicarboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft	XDS	99.90%	4.1	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	39.0	-		No		-	24.3	72.6	52.9
5re6	1.87 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z54571979	X-ray	O0S	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.57%	25.05%	23.00%	N-{4-[(pyrimidin-2-yl)oxy]phenyl}acetamide	N-{4-[(pyrimidin-2-yl)oxy]phenyl}acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft	XDS	99.80%	4.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	48.7	-		No		-	35.9	63.0	69.4
5re7	1.79 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z30932204	X-ray	T0S	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	16.73%	22.50%	12.60%	N-[(4-sulfamoylphenyl)methyl]acetamide	N-[(4-sulfamoylphenyl)methyl]acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.40%	6.1	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	25.2	-		No		-	61.3	20.3	40.0
5re8	1.81 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2737076969	X-ray	T0V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.03%	24.83%	17.10%	1-(3-fluorophenyl)-N-[(furan-2-yl)methyl]methanamine	1-(3-fluorophenyl)-N-[(furan-2-yl)methyl]methanamine	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	36.9	-		No		-	38.0	50.5	57.1
5re9	1.72 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2856434836	X-ray	LPZ	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	16.72%	22.48%	8.20%	2-(4-methylphenoxy)-1-(4-methylpiperazin-4-ium-1-yl)ethanone	2-(4-methylphenoxy)-1-(4-methylpiperazin-4-ium-1-yl)ethanone	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.70%	8.0	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	19.2	-		No		-	61.7	10.8	35.6
5rea	1.63 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z31432226	X-ray	JGP	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.52%	22.82%	9.60%	(azepan-1-yl)(2H-1,3-benzodioxol-5-yl)methanone	(azepan-1-yl)(2H-1,3-benzodioxol-5-yl)methanone	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.50%	6.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	-	-		No		-	58.0	-	48.9
5reb	1.68 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2856434899	X-ray	T0Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.55%	22.37%	9.30%	1-[(thiophen-3-yl)methyl]piperidin-4-ol	1-[(thiophen-3-yl)methyl]piperidin-4-ol	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.50%	6.9	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	42.4	-		No		-	62.8	26.9	66.7
5rec	1.73 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1587220559	X-ray	T1J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.26%	23.71%	12.10%	2-{[(1H-benzimidazol-2-yl)amino]methyl}phenol	2-{[(1H-benzimidazol-2-yl)amino]methyl}phenol	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.60%	5.9	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	52.0	-		No		-	48.9	63.0	62.8
5red	1.47 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2856434865	X-ray	JJG	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.14%	21.12%	8.50%	4-[2-(phenylsulfanyl)ethyl]morpholine	4-[2-(phenylsulfanyl)ethyl]morpholine	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.40%	6.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	35.8	-		No		-	74.0	15.0	54.5
5ree	1.77 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2217052426	X-ray	T1M	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.32%	24.24%	17.00%	(2R,3R)-1-benzyl-2-methylpiperidin-3-ol	(2R,3R)-1-benzyl-2-methylpiperidin-3-ol	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	46.9	-		No		-	43.8	63.0	58.2
5ref	1.61 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z24758179	X-ray	6SU	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.81%	24.61%	12.10%	methyl 3-(methylsulfonylamino)benzoate	methyl 3-(methylsulfonylamino)benzoate	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.10%	4.7	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	41.3	-		No		-	40.1	54.3	59.9
5reg	1.67 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1545313172	X-ray	LWA	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.92%	22.72%	11.90%	(2~{S})-~{N}-(4-aminocarbonylphenyl)oxolane-2-carboxamide	(2~{S})-~{N}-(4-aminocarbonylphenyl)oxolane-2-carboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	97.20%	5.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	22.7	-		No		-	59.1	18.5	38.6
5reh	1.80 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z111507846	X-ray	AWP	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.71%	25.73%	18.00%	1-cyclohexyl-3-(2-pyridin-4-ylethyl)urea	1-cyclohexyl-3-(2-pyridin-4-ylethyl)urea	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.70%	5.4	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	28.2	-		No		-	30.0	58.4	39.6
5rei	1.82 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2856434856	X-ray	T1S	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.32%	24.01%	16.90%	4-[(3-chlorophenyl)methyl]morpholine	4-[(3-chlorophenyl)methyl]morpholine	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	5.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	55.8	-		No		-	45.9	67.6	68.5
5rej	1.72 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102241	X-ray	T1V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.00%	24.05%	18.20%	1-{4-[(thiophen-2-yl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(thiophen-2-yl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.50%	4.0	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	43.4	-		No		-	45.6	50.5	62.3
5rek	1.74 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102327	X-ray	T1Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.27%	23.04%	17.60%	1-{4-[(3-fluorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(3-fluorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	3.9	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	56.3	-		No		-	55.8	54.3	72.7
5rel	1.62 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102340	X-ray	T2G	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.21%	21.97%	10.90%	1-{4-[(3-methylphenyl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(3-methylphenyl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.70%	5.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	56.2	-		No		-	66.6	50.5	65.6
5rem	1.96 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0103016	X-ray	T2J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.50%	24.64%	16.40%	1 1-(4-(2-nitrophenyl)piperazin-1-yl)ethan-1-one	1 1-(4-(2-nitrophenyl)piperazin-1-yl)ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.7	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	41.3	-		No		-	39.9	58.4	56.0
5ren	2.15 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102425	X-ray	T2V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.38%	27.79%	27.70%	1-[(3R)-3-(1,3-benzothiazol-2-yl)piperidin-1-yl]ethan-1-one	1-[(3R)-3-(1,3-benzothiazol-2-yl)piperidin-1-yl]ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	3.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	21.2	-		No		-	16.2	46.9	49.8
5reo	1.88 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102578	X-ray	T2Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	16.76%	22.68%	21.10%	N-[(2H-1,3-benzodioxol-5-yl)methyl]acetamide	N-[(2H-1,3-benzodioxol-5-yl)methyl]acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.60%	4.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	55.8	-		No		-	59.7	67.6	54.7
5rep	1.81 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102201	X-ray	T3G	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.83%	23.11%	15.80%	1-{4-[(2,6-difluorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(2,6-difluorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.70%	5.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	66.0	-		No		-	55.1	77.7	69.5
5rer	1.88 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102615	X-ray	T3J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.72%	25.26%	21.10%	1-[(2R)-2-(4-fluorophenyl)morpholin-4-yl]ethan-1-one	1-[(2R)-2-(4-fluorophenyl)morpholin-4-yl]ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	3.8	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	50.2	-		No		-	34.1	77.7	59.5
5res	1.65 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102281	X-ray	T3V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.14%	22.63%	11.90%	1-{4-[(2-fluorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(2-fluorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.30%	6.0	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	61.2	-		No		-	60.0	63.0	69.4
5ret	1.68 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102269	X-ray	T47	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.20%	22.20%	12.50%	1-{4-[(3-chlorophenyl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(3-chlorophenyl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	5.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	46.7	-		No		-	64.2	46.9	53.6
5reu	1.69 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102395	X-ray	T4D	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.30%	23.23%	16.30%	2-[(4-acetylpiperazin-1-yl)sulfonyl]benzonitrile	2-[(4-acetylpiperazin-1-yl)sulfonyl]benzonitrile	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	55.4	-		No		-	54.0	63.0	64.3
5rev	1.60 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0103072	X-ray	T4J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.63%	22.17%	11.20%	N-[3-(thiomorpholine-4-carbonyl)phenyl]acetamide	N-[3-(thiomorpholine-4-carbonyl)phenyl]acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	97.90%	6.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	55.2	-		No		-	64.7	50.5	65.7
5rew	1.55 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102275	X-ray	T4M	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.48%	22.36%	11.60%	N-[(1R)-1-(naphthalen-1-yl)ethyl]acetamide	N-[(1R)-1-(naphthalen-1-yl)ethyl]acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.50%	5.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	53.2	-		No		-	62.8	50.5	63.6
5rex	2.07 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102287	X-ray	T4V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.49%	25.07%	13.70%	1-{4-[(naphthalen-1-yl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(naphthalen-1-yl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	5.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	42.6	-		No		-	35.8	63.0	58.0
5rey	1.96 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102911	X-ray	T4Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.58%	27.35%	20.90%	1-{4-[(2-methylphenyl)methyl]-1,4-diazepan-1-yl}ethan-1-one	1-{4-[(2-methylphenyl)methyl]-1,4-diazepan-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.60%	3.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	35.4	-		No		-	18.6	54.3	69.7
5rez	1.79 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with POB0129	X-ray	T54	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	20.15%	27.21%	15.00%	(1R,2S)-2-(thiophen-3-yl)cyclopentane-1-carboxamide	(1R,2S)-2-(thiophen-3-yl)cyclopentane-1-carboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.30%	4.9	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	27.4	-		No		-	19.3	58.4	48.4
5rf0	1.65 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with POB0073	X-ray	T5D	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.11%	22.64%	13.10%	[1-(pyridin-2-yl)cyclopentyl]methanol	[1-(pyridin-2-yl)cyclopentyl]methanol	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	5.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	60.1	-		No		-	60.0	54.3	76.1
5rf1	1.73 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with NCL-00023830	X-ray	T5G	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.62%	23.61%	13.00%	4-bromobenzene-1-sulfonamide	4-bromobenzene-1-sulfonamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.50%	5.7	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	52.8	-		No		-	49.9	63.0	63.2
5rf2	1.53 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1741969146	X-ray	HVB	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.17%	22.16%	9.40%	1-azanylpropylideneazanium	1-azanylpropylideneazanium	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.00%	6.1	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	64.8	-		No		-	64.8	58.4	76.5
5rf3	1.50 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1741970824	X-ray	T5V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.53%	22.10%	9.80%	pyrimidin-5-amine	pyrimidin-5-amine	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.60%	6.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	59.2	-		No		-	65.2	46.9	76.4
5rf4	1.61 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1741982125	X-ray	T5Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.00%	22.49%	10.70%	pyridin-2-ol	pyridin-2-ol	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	5.9	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	57.6	-		No		-	61.7	50.5	73.3
5rf5	1.74 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z3241250482	X-ray	HV2	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.76%	23.06%	14.60%	1,1-bis(oxidanylidene)thietan-3-ol	1,1-bis(oxidanylidene)thietan-3-ol	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	5.4	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	50.7	-		No		-	55.7	54.3	62.2
5rf6	1.45 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1348371854	X-ray	NTG	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.06%	21.74%	9.30%	5-(1,4-oxazepan-4-yl)pyridine-2-carbonitrile	5-(1,4-oxazepan-4-yl)pyridine-2-carbonitrile	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.10%	5.4	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	53.1	-		No		-	68.7	46.9	61.2
5rf7	1.54 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z316425948_minor	X-ray	T67	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.04%	21.69%	8.80%	1-(4-methylpiperazin-1-yl)-2-(1H-pyrrolo[2,3-b]pyridin-3-yl)ethan-1-one	1-(4-methylpiperazin-1-yl)-2-(1H-pyrrolo[2,3-b]pyridin-3-yl)ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.30%	6.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	61.9	-		No		-	69.3	54.3	70.3
5rf8	1.44 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z271004858	X-ray	SFY	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.73%	21.32%	7.80%	4-amino-N-(pyridin-2-yl)benzenesulfonamide	4-amino-N-(pyridin-2-yl)benzenesulfonamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.00%	6.7	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	67.3	-		No		-	72.3	54.3	78.4
5rf9	1.43 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z217038356	X-ray	S7D	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.20%	21.54%	7.70%	1-[(2~{S})-2-methylmorpholin-4-yl]-2-pyrazol-1-yl-ethanone	1-[(2~{S})-2-methylmorpholin-4-yl]-2-pyrazol-1-yl-ethanone	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	95.40%	7.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	53.7	-		No		-	70.5	37.7	69.6
5rfa	1.52 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z2643472210	X-ray	JGY	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.67%	21.51%	7.80%	1-methyl-N-{[(2S)-oxolan-2-yl]methyl}-1H-pyrazole-3-carboxamide	1-methyl-N-{[(2S)-oxolan-2-yl]methyl}-1H-pyrazole-3-carboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.80%	7.1	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	61.4	-		No		-	70.7	50.1	72.0
5rfb	1.48 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z1271660837	X-ray	K3S	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.33%	22.35%	7.70%	N-[(1-methyl-1H-1,2,3-triazol-4-yl)methyl]ethanamine	N-[(1-methyl-1H-1,2,3-triazol-4-yl)methyl]ethanamine	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	97.90%	6.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	58.5	-		No		-	62.9	63.0	61.2
5rfc	1.40 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z979145504	X-ray	K1Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.95%	21.28%	6.90%	methyl (2-methyl-4-phenyl-1,3-thiazol-5-yl)carbamate	methyl (2-methyl-4-phenyl-1,3-thiazol-5-yl)carbamate	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	92.70%	7.7	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	59.4	-		No		-	72.8	46.9	69.1
5rfd	1.41 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z126932614	X-ray	T6J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.76%	21.10%	7.90%	2-[(methylsulfonyl)methyl]-1H-benzimidazole	2-[(methylsulfonyl)methyl]-1H-benzimidazole	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	94.20%	6.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	71.9	-		No		-	74.2	63.0	77.9
5rfe	1.46 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with Z509756472	X-ray	JGG	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.69%	21.36%	6.00%	N-[(4-cyanophenyl)methyl]morpholine-4-carboxamide	N-[(4-cyanophenyl)methyl]morpholine-4-carboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	94.40%	9.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	59.5	-		No		-	72.1	40.5	76.5
5rff	1.78 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102704	X-ray	T6M	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.20%	24.74%	18.50%	1-{4-[(4-chlorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(4-chlorophenyl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	27.9	-		No		-	38.9	24.0	64.3
5rfg	2.32 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102372	X-ray	T6V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	21.21%	30.65%	36.10%	N-[(3S)-1,1-dioxo-2,3-dihydro-1H-1lambda~6~-thiophen-3-yl]-N-phenylacetamide	N-[(3S)-1,1-dioxo-2,3-dihydro-1H-1lambda~6~-thiophen-3-yl]-N-phenylacetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	2.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	24.3	-		No		-	7.1	40.5	72.0
5rfh	1.58 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102277	X-ray	T6Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.86%	23.68%	10.60%	1-{4-[(5-chlorothiophen-2-yl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(5-chlorothiophen-2-yl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.40%	5.1	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	27.5	-		No		-	49.5	20.3	56.6
5rfi	1.69 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102353	X-ray	T71	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.33%	24.23%	11.60%	1-{4-[(2,5-dimethylphenyl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(2,5-dimethylphenyl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.50%	5.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	40.1	-		No		-	43.9	43.5	64.6
5rfj	1.80 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0103067	X-ray	T7A	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.64%	24.14%	19.40%	N-(4-methoxy-1,3-benzothiazol-2-yl)acetamide	N-(4-methoxy-1,3-benzothiazol-2-yl)acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.0	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	51.2	-		No		-	44.7	72.6	55.8
5rfk	1.75 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102575	X-ray	T7D	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.75%	23.48%	18.10%	N-(1-acetylpiperidin-4-yl)benzamide	N-(1-acetylpiperidin-4-yl)benzamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.50%	4.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	50.2	-		No		-	51.6	58.4	61.3
5rfl	1.64 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102389	X-ray	T7G	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.43%	22.47%	13.40%	1-acetyl-N-(2-hydroxyphenyl)piperidine-4-carboxamide	1-acetyl-N-(2-hydroxyphenyl)piperidine-4-carboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.40%	4.8	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	51.4	-		No		-	61.8	43.5	68.1
5rfm	2.06 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102539	X-ray	T7J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.79%	25.72%	21.60%	N-[(3R)-1,1-dioxo-2,3-dihydro-1H-1lambda~6~-thiophen-3-yl]-N-(4-methylphenyl)acetamide	N-[(3R)-1,1-dioxo-2,3-dihydro-1H-1lambda~6~-thiophen-3-yl]-N-(4-methylphenyl)acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	4.5	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	40.4	-		No		-	30.0	67.6	55.0
5rfn	1.80 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102868	X-ray	T7P	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.61%	23.90%	17.20%	N-[(3R)-1,1-dioxo-2,3-dihydro-1H-1lambda~6~-thiophen-3-yl]-N-(4-fluorophenyl)acetamide	N-[(3R)-1,1-dioxo-2,3-dihydro-1H-1lambda~6~-thiophen-3-yl]-N-(4-fluorophenyl)acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.90%	4.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	50.9	-		No		-	46.9	63.0	62.7
5rfo	1.83 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102972	X-ray	T7S	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	20.49%	27.75%	23.50%	1-[4-(piperidine-1-carbonyl)piperidin-1-yl]ethan-1-one	1-[4-(piperidine-1-carbonyl)piperidin-1-yl]ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.90%	3.4	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	12.6	-		No		-	16.4	35.2	40.1
5rfp	2.03 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102190	X-ray	T7V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	20.67%	29.68%	29.70%	N-[(1S)-1-(3-chlorophenyl)ethyl]acetamide	N-[(1S)-1-(3-chlorophenyl)ethyl]acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.80%	2.8	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	19.7	-		No		-	8.9	54.3	46.2
5rfq	1.76 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102179	X-ray	T7Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.00%	22.70%	19.40%	N-[3-(2-oxopyrrolidin-1-yl)phenyl]acetamide	N-[3-(2-oxopyrrolidin-1-yl)phenyl]acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.60%	4.7	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	61.8	-		No		-	59.2	63.0	71.5
5rfr	1.71 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102169	X-ray	T81	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.53%	23.77%	13.10%	1-{4-[(5-bromothiophen-2-yl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(5-bromothiophen-2-yl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	5.4	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	38.7	-		No		-	48.5	46.9	53.9
5rfs	1.70 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102739	X-ray	T84	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.69%	23.27%	14.20%	1-{4-[(thiophen-3-yl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(thiophen-3-yl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	5.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	44.2	-		No		-	53.7	40.5	65.7
5rft	1.58 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102432	X-ray	T8A	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	19.53%	23.68%	12.10%	1-[(4S)-4-phenyl-3,4-dihydroisoquinolin-2(1H)-yl]ethan-1-one	1-[(4S)-4-phenyl-3,4-dihydroisoquinolin-2(1H)-yl]ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	98.70%	4.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	44.9	-		No		-	49.5	43.5	68.3
5rfu	1.53 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102121	X-ray	T8D	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	17.53%	20.98%	9.40%	1-{4-[(5-chlorothiophen-2-yl)sulfonyl]piperazin-1-yl}ethan-1-one	1-{4-[(5-chlorothiophen-2-yl)sulfonyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	6.8	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	60.3	-		No		-	75.4	50.5	64.8
5rfv	1.48 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102306	X-ray	T8J	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.73%	22.36%	8.70%	1-[4-(thiophene-2-carbonyl)piperazin-1-yl]ethan-1-one	1-[4-(thiophene-2-carbonyl)piperazin-1-yl]ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	97.90%	6.2	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	60.1	-		No		-	62.8	54.3	73.2
5rfw	1.43 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102243	X-ray	T8M	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.95%	22.32%	5.80%	1-{4-[(thiophen-2-yl)methyl]piperazin-1-yl}ethan-1-one	1-{4-[(thiophen-2-yl)methyl]piperazin-1-yl}ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	97.90%	9.0	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	33.5	-		No		-	63.1	14.0	61.8
5rfx	1.55 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102254	X-ray	T8P	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.44%	21.63%	10.40%	1-[4-(4-methoxyphenyl)piperazin-1-yl]ethan-1-one	1-[4-(4-methoxyphenyl)piperazin-1-yl]ethan-1-one	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.20%	5.8	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	56.0	-		No		-	69.7	43.5	69.1
5rfy	1.90 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102974	X-ray	T8S	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	20.98%	27.67%	24.00%	1-acetyl-N-methyl-N-(propan-2-yl)piperidine-4-carboxamide	1-acetyl-N-methyl-N-(propan-2-yl)piperidine-4-carboxamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.30%	3.6	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	36.7	-		No		-	16.8	67.6	60.6
5rfz	1.68 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102274	X-ray	T8V	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.08%	22.65%	14.60%	N-(2-chloropyridin-3-yl)acetamide	N-(2-chloropyridin-3-yl)acetamide	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.70%	4.9	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	51.1	-		No		-	59.9	46.9	66.3
5rg0	1.72 Å	2020-03-25	PanDDA analysis group deposition -- Crystal Structure of SARS-CoV-2 main protease in complex with PCM-0102535	X-ray	T8Y	SARS-CoV-2	NSP5 (Main protease)	PanDDA fragment screening	18.81%	23.59%	12.80%	1,1'-(piperazine-1,4-diyl)di(ethan-1-one)	1,1'-(piperazine-1,4-diyl)di(ethan-1-one)	Fearon, D., Owen, C.D., Douangamath, A., Lukacik, P., Powell, A.J., Strain-Damerell, C.M., Resnick, E., Krojer, T., Gehrtz, P., Wild, C., Aimon, A., Brandao-Neto, J., Carbery, A., Dunnett, L., Skyner, R., Snee, M., London, N., Walsh, M.A., von Delft, F.	XDS	99.10%	5.3	Diamond (I04-1)	REFMAC	2020-03-15	-	-	-	-	-	N/A	-	-	SARS-CoV-2 main protease	50.4	-		No		-	50.4	63.0	58.1
6w41	3.08 Å	2020-03-25	Crystal structure of SARS-CoV-2 receptor binding domain in complex with human antibody CR3022	X-ray	NAG	SARS-CoV-2	Spike protein	Functional ligand	22.26%	24.33%	13.60%		N-ACETYL-D-GLUCOSAMINE	Yuan, M., Wu, N.C., Zhu, X.Y., Wilson, I.A.	HKL-2000	100.00%	5.0	APS (23-ID-D)	PHENIX	2020-03-09	32245784	-	-	http://covid-19.bioreproducibility.org/static/data/6w41/6w41_refined.pdb	http://covid-19.bioreproducibility.org/static/data/6w41/6w41_refined.mtz	24.70%	Shifted the coordinates into the reference unit cell with ACHESYM. Flipped two peptide bonds (Tyr380 of the spike fragment and Ile98 of the antibody heavy chain). There is some evidence of the presence of another NAG group bound to Asn343 of the spike protein, but we did not attempt to model it.	The coordinates are NOT in a standardized location in the unit cell. Comparatively low-resolution structure that is highly idealized.	CR3022 Fab heavy chain; CR3022 Fab light chain; Spike glycoprotein receptor binding domain	65.9	minimal	Yes	Yes	-		42.9	95.0	64.1
6w61	2.00 Å	2020-03-25	Crystal Structure of the methyltransferase-stimulatory factor complex of NSP16 and NSP10 from SARS CoV-2.	X-ray	SAM	SARS-CoV-2	NSP10/NSP16	Protein-protein complex	17.06%	19.30%	13.90%	S-ADENOSYLMETHIONINE	S-ADENOSYLMETHIONINE	Kim, Y., Jedrzejczak, R., Maltseva, N., Endres, M., Godzik, A., Joachimiak, A., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-3000	100.00%	37.1	APS (19-ID)	PHENIX	2020-03-15	-	ZN	-	-	-	N/A	-	-	2'-O-methyltransferase NSP16; Stimulatory factor NSP10	61.8	-		No		-	86.8	37.8	69.0
6w63	2.10 Å	2020-03-25	Structure of COVID-19 main protease bound to potent broad-spectrum non-covalent inhibitor X77	X-ray	X77	SARS-CoV-2	NSP5 (Main protease)	Functional ligand	14.99%	22.14%	N/A	N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-1H-imidazole-4-carboxamide	N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-1H-imidazole-4-carboxamide	Mesecar, A.D., Center for Structural Genomics of Infectious Diseases (CSGID)	HKL-2000	99.30%	17.2	APS (21-ID-G)	PHENIX	2020-03-16	-	-	-	-	-	N/A	-	-	Main protease	70.3	-		No	-	-	64.9	93.0	53.6
6w6y	1.45 Å	2020-03-25	Crystal Structure of ADP ribose phosphatase of NSP3 from SARS CoV-2 in complex with AMP	X-ray	AMP, MES	SARS-CoV-2	NSP3: X-domain	Functional ligand	14.21%	18.91%	10.90%	2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ADENOSINE MONOPHOSPHATE	ADENOSINE MONOPHOSPHATE;2-(N-MORPHOLINO)-ETHANESULFONIC ACID	Michalska, K., Kim, Y., Jedrzejczak, R., Maltseva, N.

Validated SARS-CoV-2 related structural models of potential drug targets

Structures