2beq

Structure of a Proteolytically Resistant Core from the Severe Acute Respiratory Syndrome Coronavirus S2 Fusion Protein

Method: X-RAY DIFFRACTION D_max: 87.2 Å Quality: REASONABLE

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Spike glycoprotein

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 914–949 Chain B； UniProt 914–949 Chain C； UniProt 914–949 Chain D； UniProt 1148–1193 Chain E； UniProt 1148–1193 Chain F； UniProt 1148–1193	Fragment：RESIDUES 914-949 Non-standard monomer：Yes (specific site not provided by mmCIF) Fragment：RESIDUES 1148-1193 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；30% PEG8K, PH 7.0 100MM SODIUM CACODYLATE PH 6.5, 200MM SODIUM ACETATE	Resolution 1.60 Å R-free 0.241

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 2BEQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WNC Crystal structure of the SARS-CoV Spike protein fusion core Deposited 2004-07-29	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 900–948（49 aa） Fragment：residues 900-1184 Chain A 1144–1185（42 aa） Fragment：residues 900-1184 Chain B 900–948（49 aa） Fragment：residues 900-1184 Chain B 1144–1185（42 aa） Fragment：residues 900-1184 Chain C 900–948（49 aa） Fragment：residues 900-1184 Chain C 1144–1185（42 aa） Fragment：residues 900-1184 Chain D 900–948（49 aa） Fragment：residues 900-1184 Chain D 1144–1185（42 aa） Fragment：residues 900-1184 Chain E 900–948（49 aa） Fragment：residues 900-1184 Chain E 1144–1185（42 aa） Fragment：residues 900-1184 Chain F 900–948（49 aa） Fragment：residues 900-1184 Chain F 1144–1185（42 aa） Fragment：residues 900-1184	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 2.5；291 K；PEG4000, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.273
1WNC Crystal structure of the SARS-CoV Spike protein fusion core Deposited 2004-07-29	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 900–948（49 aa） Fragment：residues 900-1184 Chain A 1144–1185（42 aa） Fragment：residues 900-1184 Chain B 900–948（49 aa） Fragment：residues 900-1184 Chain B 1144–1185（42 aa） Fragment：residues 900-1184 Chain C 900–948（49 aa） Fragment：residues 900-1184 Chain C 1144–1185（42 aa） Fragment：residues 900-1184	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 2.5；291 K；PEG4000, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.273
1WNC Crystal structure of the SARS-CoV Spike protein fusion core Deposited 2004-07-29	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 900–948（49 aa） Fragment：residues 900-1184 Chain D 1144–1185（42 aa） Fragment：residues 900-1184 Chain E 900–948（49 aa） Fragment：residues 900-1184 Chain E 1144–1185（42 aa） Fragment：residues 900-1184 Chain F 900–948（49 aa） Fragment：residues 900-1184 Chain F 1144–1185（42 aa） Fragment：residues 900-1184	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 2.5；291 K；PEG4000, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.80 Å R-free 0.273
1WYY Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein Deposited 2005-02-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 885–981（97 aa） Fragment：residues 885-1189 Chain A 1145–1189（45 aa） Fragment：residues 885-1189	Not recorded	CL CHLORIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；PEG 8000, LiSO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.20 Å R-free 0.249
1WYY Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein Deposited 2005-02-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 885–981（97 aa） Fragment：residues 885-1189 Chain B 1145–1189（45 aa） Fragment：residues 885-1189	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；PEG 8000, LiSO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.20 Å R-free 0.249
1WYY Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein Deposited 2005-02-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 885–981（97 aa） Fragment：residues 885-1189 Chain B 1145–1189（45 aa） Fragment：residues 885-1189	Not recorded	CL CHLORIDE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；PEG 8000, LiSO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.20 Å R-free 0.249
1ZV7 A structure-based mechanism of SARS virus membrane fusion Deposited 2005-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1150–1193（44 aa） Fragment：residues 1150-1193 Chain B 1150–1193（44 aa） Fragment：residues 1150-1193	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG MME 2000, Nickel chloride, Tris-HCL, pH 8.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.70 Å R-free 0.258
1ZV8 A structure-based mechanism of SARS virus membrane fusion Deposited 2005-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 901–950（50 aa） Fragment：residues 901-950 Chain B 1150–1185（36 aa） Fragment：residues 1150-1185 Chain C 901–950（50 aa） Fragment：residues 901-950 Chain D 1150–1185（36 aa） Fragment：residues 1150-1185 Chain E 901–950（50 aa） Fragment：residues 901-950 Chain F 1150–1185（36 aa） Fragment：residues 1150-1185	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；PEG 8000, zinc acetate, sodium cacodylate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.94 Å R-free 0.274
1ZV8 A structure-based mechanism of SARS virus membrane fusion Deposited 2005-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain G 901–950（50 aa） Fragment：residues 901-950 Chain H 1150–1185（36 aa） Fragment：residues 1150-1185 Chain I 901–950（50 aa） Fragment：residues 901-950 Chain J 1150–1185（36 aa） Fragment：residues 1150-1185 Chain K 901–950（50 aa） Fragment：residues 901-950 Chain L 1150–1185（36 aa） Fragment：residues 1150-1185	Not recorded	NA SODIUM ION × 4 CAC CACODYLATE ION × 1 ZN ZINC ION × 2 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；PEG 8000, zinc acetate, sodium cacodylate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.94 Å R-free 0.274
1ZVA A structure-based mechanism of SARS virus membrane fusion Deposited 2005-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 926–962（37 aa） Fragment：residues 926-962 and residues 1150-1183 Chain A 1150–1183（34 aa） Fragment：residues 926-962 and residues 1150-1183	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；PEG 1500, sodium formate, pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.246
1ZVB A structure-based mechanism of SARS virus membrane fusion Deposited 2005-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 940–973（34 aa） Fragment：residues 940-973 Chain B 940–973（34 aa） Fragment：residues 940-973 Chain C 940–973（34 aa） Fragment：residues 940-973	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；298 K；PEG 4000, isopropanol, sodium citrate, pH 5.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.70 Å R-free 0.239
2AJF Structure of SARS coronavirus spike receptor-binding domain complexed with its receptor Deposited 2005-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 323–502（180 aa） Fragment：receptor-binding domain, residues 323-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；100 mM Tris pH 8.2, 24% PEG6000, 150 mM NaCl, 10% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, pH 7.5, pH 7.50	Resolution 2.90 Å R-free 0.275
2AJF Structure of SARS coronavirus spike receptor-binding domain complexed with its receptor Deposited 2005-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 323–502（180 aa） Fragment：receptor-binding domain, residues 323-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；100 mM Tris pH 8.2, 24% PEG6000, 150 mM NaCl, 10% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, pH 7.5, pH 7.50	Resolution 2.90 Å R-free 0.275
2BEZ Structure of a proteolitically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein Deposited 2004-12-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain C 896–972（77 aa） Fragment：RESIDUES 896-972 Chain F 1142–1183（42 aa） Fragment：RESIDUES 1142-1183	Not recorded	GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1M TRIS-HCL, PH 7.0, 1.8M AMMONIUM SULPHATE, 0.1M NACL	Resolution 1.60 Å R-free 0.244
2DD8 Crystal Structure of SARS-CoV Spike Receptor-Binding Domain Complexed with Neutralizing Antibody Deposited 2006-01-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain S 317–518（202 aa） Fragment：RECEPTOR-BINDING DOMAIN, residues 317-518	Not recorded	PO4 PHOSPHATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；15v/v% Glycerol, 20% PEG 6000, 100mM MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.30 Å R-free 0.261
2DD8 Crystal Structure of SARS-CoV Spike Receptor-Binding Domain Complexed with Neutralizing Antibody Deposited 2006-01-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain S 317–518（202 aa） Fragment：RECEPTOR-BINDING DOMAIN, residues 317-518	Not recorded	PO4 PHOSPHATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；15v/v% Glycerol, 20% PEG 6000, 100mM MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.30 Å R-free 0.261
2FXP Solution Structure of the SARS-Coronavirus HR2 Domain Deposited 2006-02-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1140–1193（54 aa） Fragment：HR2 domain, residues 1140-1193 Chain B 1140–1193（54 aa） Fragment：HR2 domain, residues 1140-1193 Chain C 1140–1193（54 aa） Fragment：HR2 domain, residues 1140-1193	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 10 mM；Pressure ambient NMR sample composition 1 mM monomer, 10 mM PO4, pH 7.0, 30% TFE	Resolution not provided
2GHV Crystal structure of SARS spike protein receptor binding domain Deposited 2006-03-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 317–512（196 aa） Fragment：RBD of spike protein S1 (318-510) Chain E 317–512（196 aa） Fragment：RBD of spike protein S1 (318-510)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；290 K；4% PEG4000, 0.1M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.20 Å R-free 0.213
2GHW Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R Deposited 2006-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 317–510（194 aa） Fragment：RBD of spike protein S1 (318-510)	Not recorded	CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；290 K；12.5% PEG4000, 0.1M sodium acetate, 0.2M ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.30 Å R-free 0.295
2GHW Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R Deposited 2006-03-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 317–510（194 aa） Fragment：RBD of spike protein S1 (318-510)	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；290 K；12.5% PEG4000, 0.1M sodium acetate, 0.2M ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.30 Å R-free 0.295
2RUM Solution structure of Fusion peptide Deposited 2014-11-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 770–788（19 aa）	Mutation：Y2W	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.7；315 K NMR sample composition 125 mM [U-99% 2H] DPC-1, 0.5 mM Fusion Peptide-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2RUN Solution Structure of Pre Transmembrane domain Deposited 2014-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1185–1202（18 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.7；315 K NMR sample composition 0.5 mM Pre transmembrane domain-1, 125 mM [U-99% 2H] DPC-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2RUO Solution Structure of Internal Fusion Peptide Deposited 2014-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 873–888（16 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.7；315 K NMR sample composition 0.5 mM Internal fusion peptide-1, 125 mM [U-99% 2H] DPC-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3BGF X-ray crystal structure of the SARS coronavirus spike receptor binding domain in complex with F26G19 Fab Deposited 2007-11-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 318–510（193 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.1 M MES, 14% PEG 20000, 10-15% glycerol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.00 Å R-free 0.286
3BGF X-ray crystal structure of the SARS coronavirus spike receptor binding domain in complex with F26G19 Fab Deposited 2007-11-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain S 318–510（193 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；0.1 M MES, 14% PEG 20000, 10-15% glycerol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.00 Å R-free 0.286
3D0G Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 324–502（179 aa） Fragment：residues 324-502 Chain F 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 5 ZN ZINC ION × 2 CL CHLORIDE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 2.80 Å R-free 0.279
3D0H Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 324–502（179 aa） Fragment：residues 324-502 Chain F 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 5 ZN ZINC ION × 2 CL CHLORIDE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 3.10 Å R-free 0.302
3D0H Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 3.10 Å R-free 0.302
3D0H Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 4 ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 3.10 Å R-free 0.302
3D0I Crystal structure of spike protein receptor-binding domain from the 2005-2006 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain E 324–502（179 aa） Fragment：residues 324-502 Chain F 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 5 ZN ZINC ION × 2 CL CHLORIDE ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 2.90 Å R-free 0.278
3D0I Crystal structure of spike protein receptor-binding domain from the 2005-2006 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 2.90 Å R-free 0.278
3D0I Crystal structure of spike protein receptor-binding domain from the 2005-2006 SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2008-05-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 324–502（179 aa） Fragment：residues 324-502	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 4 ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；298 K；100 mM Tris, 22% PEG6000, 100 mM NaCl, pH 8.5, vapor diffusion, temperature 298K	Resolution 2.90 Å R-free 0.278
3SCI Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus human strain complexed with human receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 306–527（222 aa） Fragment：receptor binding domain (UNP residues 306-527)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 2.90 Å R-free 0.283
3SCI Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus human strain complexed with human receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 306–527（222 aa） Fragment：receptor binding domain (UNP residues 306-527)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 2.90 Å R-free 0.283
3SCJ Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 323–502（180 aa） Fragment：receptor binding domain (UNP residues 323-502)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 3.00 Å R-free 0.278
3SCJ Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 323–502（180 aa） Fragment：receptor binding domain (UNP residues 323-502)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 3.00 Å R-free 0.278
3SCK Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 324–502（179 aa） Fragment：receptor binding domain (UNP residues 324-502)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；20 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 3.00 Å R-free 0.285
3SCK Crystal structure of spike protein receptor-binding domain from a predicted SARS coronavirus civet strain complexed with human-civet chimeric receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 324–502（179 aa） Fragment：receptor binding domain (UNP residues 324-502)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；20 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 3.00 Å R-free 0.285
3SCL Crystal structure of spike protein receptor-binding domain from SARS coronavirus epidemic strain complexed with human-civet chimeric receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 324–502（179 aa） Fragment：receptor binding domain (UNP residues 324-502)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 3.00 Å R-free 0.292
3SCL Crystal structure of spike protein receptor-binding domain from SARS coronavirus epidemic strain complexed with human-civet chimeric receptor ACE2 Deposited 2011-06-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 324–502（179 aa） Fragment：receptor binding domain (UNP residues 324-502)	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.5；295 K；100 mM Tris, pH 8.5, 20% PEG6000, 100 mM sodium chloride, EVAPORATION, temperature 295K	Resolution 3.00 Å R-free 0.292
5WRG SARS-CoV spike glycoprotein Deposited 2016-12-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–1196（1196 aa） Fragment：UNP RESIDUES 1-1196 Chain B 1–1196（1196 aa） Fragment：UNP RESIDUES 1-1196 Chain C 1–1196（1196 aa） Fragment：UNP RESIDUES 1-1196	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
5X4S Structure of the N-terminal domain (NTD)of SARS-CoV spike protein Deposited 2017-02-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 14–292（279 aa） Fragment：UNP residues 14-292	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；1.3 M Na/K hydrogen phosphate	Resolution 2.20 Å R-free 0.282
5XJK NMR Structure and Localization of a Large Fragment of the SARS-CoV Fusion Protein: Implications in Viral Cell Fusion Deposited 2017-05-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 758–821（64 aa） Fragment：UNP RESIDUES 758-821	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 0.2 M [U-13C; U-15N] Large Fragment of the SARS-CoV Fusion Protein, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
5XLR Structure of SARS-CoV spike glycoprotein Deposited 2017-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–1196（1196 aa） Chain B 1–1196（1196 aa） Chain C 1–1196（1196 aa）	Mutation：R667A Mutation：R667A Mutation：R667A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
5ZVM Crystal Structure of the Human Coronavirus SARS HR1 motif in complex with pan-CoVs inhibitor EK1 Deposited 2018-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 892–970（79 aa） Fragment：UNP residues 892-970 Chain B 892–970（79 aa） Fragment：UNP residues 892-970 Chain C 892–970（79 aa） Fragment：UNP residues 892-970	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 5.5；293 K；0.2M Li2SO4, 0.1M BIS-Tris, pH 5.5, 25% PEG3350	Resolution 3.30 Å R-free 0.301
6ACC Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with three RBD in down conformation Deposited 2018-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–1196（1196 aa） Chain B 1–1196（1196 aa） Chain C 1–1196（1196 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
6ACD Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up conformation Deposited 2018-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–1196（1196 aa） Chain B 1–1196（1196 aa） Chain C 1–1196（1196 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6ACG Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1 Deposited 2018-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1196（1196 aa） Chain B 1–1196（1196 aa） Chain C 1–1196（1196 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.40 Å
6ACJ Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 2 Deposited 2018-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1196（1196 aa） Chain B 1–1196（1196 aa） Chain C 1–1196（1196 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
6ACK Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 3 Deposited 2018-07-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1196（1196 aa） Chain B 1–1196（1196 aa） Chain C 1–1196（1196 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
6CRV SARS Spike Glycoprotein, Stabilized variant, C3 symmetry Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V969P Mutation：K968P, V969P Mutation：K968P, V969P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
6CRW SARS Spike Glycoprotein, Stabilized variant, single upwards S1 CTD conformation Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V969P Mutation：K968P, V969P Mutation：K968P, V969P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6CRX SARS Spike Glycoprotein, Stabilized variant, two S1 CTDs in the upwards conformation Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V968P Mutation：K968P, V968P Mutation：K968P, V968P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6CRZ SARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, C3 symmetry Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V968P Mutation：K968P, V968P Mutation：K968P, V968P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
6CS0 SARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, one S1 CTD in an upwards conformation Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V968P Mutation：K968P, V968P Mutation：K968P, V968P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6CS1 SARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, two S1 CTDs in an upwards conformation Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V969P Mutation：K968P, V969P Mutation：K968P, V969P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
6CS2 SARS Spike Glycoprotein - human ACE2 complex, Stabilized variant, all ACE2-bound particles Deposited 2018-03-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 14–1190（1177 aa） Chain B 14–1190（1177 aa） Chain C 14–1190（1177 aa）	Mutation：K968P, V969P Mutation：K968P, V969P Mutation：K968P, V969P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
6M3W Post-fusion structure of SARS-CoV spike glycoprotein Deposited 2020-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 688–1178（491 aa） Chain B 688–1178（491 aa） Chain C 688–1178（491 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6NB6 SARS-CoV complex with human neutralizing S230 antibody Fab fragment (state 1) Deposited 2018-12-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 14–1193（1180 aa） Chain B 14–1193（1180 aa） Chain C 14–1193（1180 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
6NB7 SARS-CoV complex with human neutralizing S230 antibody Fab fragment (state 2) Deposited 2018-12-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 14–1193（1180 aa） Chain B 14–1193（1180 aa） Chain C 14–1193（1180 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
6VW1 Structure of SARS-CoV-2 chimeric receptor-binding domain complexed with its receptor human ACE2 Deposited 2020-02-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 306–441（136 aa） Chain E 505–521（17 aa）	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Tris, PEG 6000, and 100 mM NaCl.	Resolution 2.68 Å R-free 0.229
6VW1 Structure of SARS-CoV-2 chimeric receptor-binding domain complexed with its receptor human ACE2 Deposited 2020-02-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 306–441（136 aa） Chain F 505–521（17 aa）	Not recorded	ZN ZINC ION × 1 CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Tris, PEG 6000, and 100 mM NaCl.	Resolution 2.68 Å R-free 0.229
6WAQ Crystal structure of the SARS-CoV-1 RBD bound by the cross-reactive single-domain antibody SARS VHH-72 Deposited 2020-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 320–502（183 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；0.1 M Tris pH 8.5, 0.2 M LiSO4, 0.1 M LiCl, 8% PEG 8000	Resolution 2.20 Å R-free 0.236
6WAQ Crystal structure of the SARS-CoV-1 RBD bound by the cross-reactive single-domain antibody SARS VHH-72 Deposited 2020-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 320–502（183 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；293 K；0.1 M Tris pH 8.5, 0.2 M LiSO4, 0.1 M LiCl, 8% PEG 8000	Resolution 2.20 Å R-free 0.236
7FC6 Crystal structure of SARS-CoV RBD and horse ACE2 Deposited 2021-07-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain S 321–512（192 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；0.03M Citric acid/0.07M BIS-TRIS propane pH7.6, 20% w/v polyethylene glycol 3350	Resolution 2.65 Å R-free 0.235
7RKS Structure of the SARS-CoV receptor binding domain in complex with the human neutralizing antibody Fab fragment, C118 Deposited 2021-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 321–510（190 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2M sodium fluoride, 20% PEG 3,350	Resolution 2.70 Å R-free 0.247
7RKS Structure of the SARS-CoV receptor binding domain in complex with the human neutralizing antibody Fab fragment, C118 Deposited 2021-07-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain S 321–510（190 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.2M sodium fluoride, 20% PEG 3,350	Resolution 2.70 Å R-free 0.247
7SG4 Structure of SARS-CoV S protein in complex with Receptor Binding Domain antibody DH1047 Deposited 2021-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–1190（1190 aa） Chain B 1–1190（1190 aa） Chain C 1–1190（1190 aa）	Mutation：K968P, V969P Mutation：K968P, V969P Mutation：K968P, V969P	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 47	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.43 Å
7WR9 Local CryoEM structure of the SARS-CoV S2P in complex with BD55-3152 Fab Deposited 2022-01-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 323–502（180 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
7WSF Cryo-EM structure of SARS-CoV spike receptor-binding domain in complex with minke whale ACE2 Deposited 2022-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 321–502（182 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
7WSG Cryo-EM structure of SARS-CoV spike receptor-binding domain in complex with sea lion ACE2 Deposited 2022-01-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 321–502（182 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å
7X2J Crystal structure of nanobody Nb70 with SARS-CoV RBD Deposited 2022-02-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain S 306–516（211 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.4；291.15 K；0.2M Ammonium sulfate, 0.1M Bis-Tris pH 4.4, 21% w/v Polyethylene glycol 3350	Resolution 2.40 Å R-free 0.235
7X7V Cryo-EM structure of SARS-CoV spike protein in complex with three nAbs X01, X10 and X17 Deposited 2022-03-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 7 PDB declaration: heptameric	Chain E 320–508（189 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.83 Å
7Y3N Crystal structure of SARS-CoV receptor binding domain in complex with human antibody BIOLS56 Deposited 2022-06-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 306–527（222 aa） Fragment：receptor binding domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.9；291 K；20% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate pH 5.9, 20% w/v Polyethylene glycol 4000	Resolution 2.97 Å R-free 0.263
7Y3N Crystal structure of SARS-CoV receptor binding domain in complex with human antibody BIOLS56 Deposited 2022-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 306–527（222 aa） Fragment：receptor binding domain	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.9；291 K；20% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate pH 5.9, 20% w/v Polyethylene glycol 4000	Resolution 2.97 Å R-free 0.263
7Y3N Crystal structure of SARS-CoV receptor binding domain in complex with human antibody BIOLS56 Deposited 2022-06-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain E 306–527（222 aa） Fragment：receptor binding domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.9；291 K；20% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate pH 5.9, 20% w/v Polyethylene glycol 4000	Resolution 2.97 Å R-free 0.263
7ZH1 SARS CoV Spike protein, Closed C3 conformation Deposited 2022-04-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1193（1180 aa） Chain B 14–1193（1180 aa） Chain C 14–1193（1180 aa）	Not recorded	EIC LINOLEIC ACID × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.48 Å
7ZH2 SARS CoV Spike protein, Closed C1 conformation Deposited 2022-04-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1193（1180 aa） Chain B 14–1193（1180 aa） Chain C 14–1193（1180 aa）	Not recorded	EIC LINOLEIC ACID × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 27	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.71 Å
7ZH5 SARS CoV Spike protein, Open conformation Deposited 2022-04-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 14–1193（1180 aa） Chain B 14–1193（1180 aa） Chain C 14–1193（1180 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 23	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.30 Å
8H0X Structure of SARS-CoV-1 Spike Protein with Engineered x1 Disulfide (S370C and D967C), Locked-1 Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：S370C, D967C Mutation：S370C, D967C Mutation：S370C, D967C	EIC LINOLEIC ACID × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 42 BLA BILIVERDINE IX ALPHA × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.57 Å
8H0Y Structure of SARS-CoV-1 Spike Protein with Engineered x1 Disulfide (S370C and D967C), Locked-112 Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Not recorded	EIC LINOLEIC ACID × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 46 BLA BILIVERDINE IX ALPHA × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.85 Å
8H0Z Structure of SARS-CoV-1 Spike Protein with Engineered x1 Disulfide (S370C and D967C), Locked-122 Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：S370C, D967C Mutation：S370C, D967C Mutation：S370C, D967C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 39 BLA BILIVERDINE IX ALPHA × 3 EIC LINOLEIC ACID × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8H10 Structure of SARS-CoV-1 Spike Protein with Engineered x1 Disulfide (S370C and D967C), Locked-2 Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：S370C, D967C Mutation：S370C, D967C Mutation：S370C, D967C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 42 BLA BILIVERDINE IX ALPHA × 3 EIC LINOLEIC ACID × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å
8H11 Structure of SARS-CoV-1 Spike Protein with Engineered x1 Disulfide (S370C and D967C), Closed Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：S370C, D967C Mutation：S370C, D967C Mutation：S370C, D967C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.72 Å
8H12 Structure of SARS-CoV-1 Spike Protein with Engineered x2 Disulfide (G400C and V969C), Locked-2 Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：G400C, V969C Mutation：G400C, V969C Mutation：G400C, V969C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 39	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
8H13 Structure of SARS-CoV-1 Spike Protein with Engineered x2 Disulfide (G400C and V969C), Closed Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：G400C, V969C Mutation：G400C, V969C Mutation：G400C, V969C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.05 Å
8H14 Structure of SARS-CoV-1 Spike Protein with Engineered x3 Disulfide (D414C and V969C), Locked-1 Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Mutation：D414C and V969C Mutation：D414C and V969C Mutation：D414C and V969C	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 42 EIC LINOLEIC ACID × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.39 Å
8H15 Structure of SARS-CoV-1 Spike Protein (S/native) at pH 5.5, Closed Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18	ELECTRON MICROSCOPY cryo-EM buffer pH 5.54；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.14 Å
8H16 Structure of SARS-CoV-1 Spike Protein (S/native) at pH 5.5, Open Conformation Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 15–1193（1179 aa） Chain B 15–1193（1179 aa） Chain C 15–1193（1179 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 32	ELECTRON MICROSCOPY cryo-EM buffer pH 5.54；Gibco PBS C10010 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å
8JAG Cryo-EM structure of SARS-CoV-1 RBD in complex with W328-6H2 (local refinement) Deposited 2023-05-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–1255（1255 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.55 Å
8KDM Structure of SARS-CoV Spike protein complexed with antibody PW5-5 Deposited 2023-08-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 1–1190（1190 aa） Chain B 1–1190（1190 aa） Chain C 1–1190（1190 aa）	Mutation：S577A, K968P, V969P Mutation：S577A, K968P, V969P Mutation：S577A, K968P, V969P	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.87 Å
8KDS Trimer state of SARS-CoV Spike protein complexed with antibody PW5-535 Deposited 2023-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–1190（1190 aa） Chain B 1–1190（1190 aa） Chain C 1–1190（1190 aa）	Mutation：S577A, K968P, V969P Mutation：S577A, K968P, V969P Mutation：S577A, K968P, V969P	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.05 Å
8KDT The local refined map of SARS-CoV Spike protein complexed with antibody PW5-5 Deposited 2023-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–1190（1190 aa）	Mutation：S577A, K968P, V969P	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.04 Å
8KEK Monomer state of SARS-CoV Spike protein complexed with antibody PW5-535 Deposited 2023-08-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–1190（1190 aa）	Mutation：K968P, V969P, S577A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.54 Å
8VPF Structure of SARS-CoV spike in complex with CoV1-65 Fab (NTD-bound) Deposited 2024-01-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 1–1190（1190 aa） Chain B 1–1190（1190 aa） Chain C 1–1190（1190 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 15	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；1X TBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8WCG Crystal structure of SARS-CoV-1 RBD in complex with nanobody aSR29 and aSR347 Deposited 2023-09-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 320–516（197 aa） Chain B 320–516（197 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291.15 K；20% w/v PEG4000, 0.1 M Tris 8.0	Resolution 2.60 Å R-free 0.279
8WOZ Cryo-EM structure of SARS-CoV RBD in complex with rabbit ACE2 Deposited 2023-10-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 306–527（222 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.25 Å
8XZB The structure of fox ACE2 and SARS-CoV RBD complex Deposited 2024-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 306–527（222 aa） Fragment：RBD	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.12 Å

76 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SPIKE_CVHSA
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 2–37； UniProt 914–949 Author chain B； PDBConstruct 2–37； UniProt 914–949 Author chain C； PDBConstruct 2–37； UniProt 914–949 Author chain D； PDBConstruct 2–47； UniProt 1148–1193 Author chain E； PDBConstruct 2–47； UniProt 1148–1193 Author chain F； PDBConstruct 2–47； UniProt 1148–1193

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2beq
Deposition date deposition_date	2004-11-29
Structure title title	Structure of a Proteolytically Resistant Core from the Severe Acute Respiratory Syndrome Coronavirus S2 Fusion Protein
Keywords keywords	VIRAL PROTEIN, COILED COIL, MEMBRANE FUSION, SARS, VIRAL ENTRY, ENVELOPE PROTEIN, GLYCOPROTEIN, TRANSMEMBRANE, VIRULENCE; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	23.58 Å
Radius of gyration Rg (electron density) rg_electron	23.56 Å
Forward intensity I(0) i0	13504800.00
Molecular weight molecular_weight	27108.0 kDa
Excluded volume excluded_volume	33915 Å³
Envelope volume envelope_volume	42037 Å³
Hydration-shell volume shell_volume	17030 Å³
Envelope diameter envelope_diameter	89.3 Å
Shell Rg shell_rg	27.90 Å
Envelope Rg envelope_rg	24.38 Å
Shape Rg shape_rg	23.58 Å
Total Rg total_rg	24.11 Å
Total atoms total_atoms	1904
Residues n_residues	246
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	87.2 Å
Rg (real space) rg_real	23.97 Å
Rg uncertainty (real space) rg_real_error	0.93 Å
I(0) (real space) i0_real	1.3500e+07
I(0) uncertainty (real space) i0_real_error	2.1120e+05
Rg (reciprocal space) rg_reciprocal	23.88 Å
I(0) (reciprocal space) i0_reciprocal	13500000.0000
Solution quality estimate total_estimate	0.7377
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.8 Å
Skewness Skewness skewness	0.732
Kurtosis Kurtosis kurtosis	0.090
Angular range angular_range	— – 0.3350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3899000.0000
Real-space data points n_real_points	65
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.416; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.384; Smooth: 0.955

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Spike glycoprotein
Molecular weight formula_weight	3869.3 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	2110

XSQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSX

Entity 2 Entity 2 polymer

Description description	Spike glycoprotein
Molecular weight formula_weight	5217.9 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

XLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKX

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	202

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2beq.1
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.3 — Coronavirus S2 glycoprotein
Family Family family	h.3.3.1 — Coronavirus spike glycoprotein S2 fragments

Domain ID domain_id	d2beq.2
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.3 — Coronavirus S2 glycoprotein
Family Family family	h.3.3.1 — Coronavirus spike glycoprotein S2 fragments

Domain ID domain_id	d2beq.3
Class class	h — Coiled coil proteins
Fold Fold fold	h.3 — Stalk segment of viral fusion proteins
Superfamily Superfamily superfamily	h.3.3 — Coronavirus S2 glycoprotein
Family Family family	h.3.3.1 — Coronavirus spike glycoprotein S2 fragments

CATH v4.4 (3 domains)

Domain ID domain_id	2beqD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	790 — Single helix bin

Domain ID domain_id	2beqE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	790 — Single helix bin

Domain ID domain_id	2beqF00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	790 — Single helix bin

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8. Citations (1)

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Unit-cell length a length_a	99.907 Å
Unit-cell length b length_b	42.903 Å
Unit-cell length c length_c	59.826 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	116.69 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2010
R_work r_work	0.1990
R_free r_free	0.2410

fit	/app/data/saxs_computation/be/2beq/2beq.fit
pddf	/app/data/pr_computation/be/2beq/2beq.pr.out
profile	/app/data/saxs_computation/be/2beq/2beq.dat

Structure of a Proteolytically Resistant Core from the Severe Acute Respiratory Syndrome Coronavirus S2 Fusion Protein

1. Protein Identity and Related Structures Protein Identity & Related Structures

Spike glycoprotein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)