1c8m

REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS

Method: X-RAY DIFFRACTION D_max: 93.9 Å Quality: GOOD

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

HUMAN RHINOVIRUS 16 COAT PROTEIN

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 × 240 PDB declaration: 240-MERIC（240） Consistent with protein copy count	Chain 1； UniProt 568–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–77	Fragment：RESIDUES 569-853 Fragment：RESIDUES 79-330 Fragment：RESIDUES 331-568 Fragment：RESIDUES 2-78	ZN ZINC ION × 60 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 60	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG8000, HEPES BUFFER, SODIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.226
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain 1； UniProt 568–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–77	Fragment：RESIDUES 569-853 Fragment：RESIDUES 79-330 Fragment：RESIDUES 331-568 Fragment：RESIDUES 2-78	ZN ZINC ION × 1 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG8000, HEPES BUFFER, SODIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.226
3	Protein homooligomer Homooligomer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain 1； UniProt 568–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–77	Fragment：RESIDUES 569-853 Fragment：RESIDUES 79-330 Fragment：RESIDUES 331-568 Fragment：RESIDUES 2-78	ZN ZINC ION × 5 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 5	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG8000, HEPES BUFFER, SODIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.226
4	Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain 1； UniProt 568–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–77	Fragment：RESIDUES 569-853 Fragment：RESIDUES 79-330 Fragment：RESIDUES 331-568 Fragment：RESIDUES 2-78	ZN ZINC ION × 6 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 6	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG8000, HEPES BUFFER, SODIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.226
5	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain 1； UniProt 568–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–77	Fragment：RESIDUES 569-853 Fragment：RESIDUES 79-330 Fragment：RESIDUES 331-568 Fragment：RESIDUES 2-78	ZN ZINC ION × 1 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG8000, HEPES BUFFER, SODIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.226
6	Protein homooligomer Homooligomer Protein × 120 PDB declaration: 120-meric（120） Consistent with protein copy count	Chain 1； UniProt 568–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–77	Fragment：RESIDUES 569-853 Fragment：RESIDUES 79-330 Fragment：RESIDUES 331-568 Fragment：RESIDUES 2-78	ZN ZINC ION × 30 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 30	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG8000, HEPES BUFFER, SODIUM CHLORIDE, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.226

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 1C8M	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AYM HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 240 PDB declaration: 240-MERIC	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 60 DAO LAURIC ACID × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 2.15 Å R-free 0.233
1AYM HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 1 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 2.15 Å R-free 0.233
1AYM HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 5 DAO LAURIC ACID × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 2.15 Å R-free 0.233
1AYM HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 6 DAO LAURIC ACID × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 2.15 Å R-free 0.233
1AYM HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 1 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 2.15 Å R-free 0.233
1AYM HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 120 PDB declaration: 120-meric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 30 DAO LAURIC ACID × 30 MYR MYRISTIC ACID × 30	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；pH 7.5	Resolution 2.15 Å R-free 0.233
1AYN HUMAN RHINOVIRUS 16 COAT PROTEIN Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 240 PDB declaration: 240-MERIC	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 60 DAO LAURIC ACID × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000., vapor diffusion - hanging drop	Resolution 2.90 Å R-free 0.230
1AYN HUMAN RHINOVIRUS 16 COAT PROTEIN Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 1 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000., vapor diffusion - hanging drop	Resolution 2.90 Å R-free 0.230
1AYN HUMAN RHINOVIRUS 16 COAT PROTEIN Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 5 DAO LAURIC ACID × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000., vapor diffusion - hanging drop	Resolution 2.90 Å R-free 0.230
1AYN HUMAN RHINOVIRUS 16 COAT PROTEIN Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 6 DAO LAURIC ACID × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000., vapor diffusion - hanging drop	Resolution 2.90 Å R-free 0.230
1AYN HUMAN RHINOVIRUS 16 COAT PROTEIN Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 1 DAO LAURIC ACID × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000., vapor diffusion - hanging drop	Resolution 2.90 Å R-free 0.230
1AYN HUMAN RHINOVIRUS 16 COAT PROTEIN Deposited 1997-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 120 PDB declaration: 120-meric	Chain 1 568–852（285 aa） Chain 2 69–329（261 aa） Chain 3 330–567（238 aa）	Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4 Mutation：N-TERMINAL MYRISTOYLATION ON VP4	ZN ZINC ION × 30 DAO LAURIC ACID × 30 MYR MYRISTIC ACID × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000., vapor diffusion - hanging drop	Resolution 2.90 Å R-free 0.230
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 300 PDB declaration: 300-MERIC	Chain 1 573–852（280 aa） Chain 2 78–329（252 aa） Chain 3 330–567（238 aa） Chain 4 1–68（68 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 573–852（280 aa） Chain 2 78–329（252 aa） Chain 3 330–567（238 aa） Chain 4 1–68（68 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 25 PDB declaration: 25-meric	Chain 1 573–852（280 aa） Chain 2 78–329（252 aa） Chain 3 330–567（238 aa） Chain 4 1–68（68 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 1 573–852（280 aa） Chain 2 78–329（252 aa） Chain 3 330–567（238 aa） Chain 4 1–68（68 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1D3E CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 16 (HRV16) COMPLEXED WITH A TWO-DOMAIN FRAGMENT OF ITS CELLULAR RECEPTOR, INTERCELLULAR ADHESION MOLECULE-1 (D1D2-ICAM-1). IMPLICATIONS FOR VIRUS-RECEPTOR INTERACTIONS. ALPHA CARBONS ONLY Deposited 1999-09-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain 1 573–852（280 aa） Chain 2 78–329（252 aa） Chain 3 330–567（238 aa） Chain 4 1–68（68 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions HRV16 WAS INCUBATED WITH D1D2-ICAM-1 FOR 16 HOURS AT 34 DEGREES CELSIUS (307 KELVIN) USING A SIXTEEN-FOLD EXCESS OF D1D2-ICAM-1 FOR EACH OF THE SIXTY POSSIBLE BINDING SITES PER VIRION. AFTER INCUBATION, SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626 CRYOTRANSFER HOLDER	Resolution 28.00 Å
1NCR The structure of Rhinovirus 16 when complexed with pleconaril, an antiviral compound Deposited 2002-12-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 60 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.247
1NCR The structure of Rhinovirus 16 when complexed with pleconaril, an antiviral compound Deposited 2002-12-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 1 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.247
1NCR The structure of Rhinovirus 16 when complexed with pleconaril, an antiviral compound Deposited 2002-12-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 5 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.247
1NCR The structure of Rhinovirus 16 when complexed with pleconaril, an antiviral compound Deposited 2002-12-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 6 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.247
1NCR The structure of Rhinovirus 16 when complexed with pleconaril, an antiviral compound Deposited 2002-12-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 1 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å R-free 0.247
1ND2 The structure of Rhinovirus 16 Deposited 2002-12-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 60 MYR MYRISTIC ACID × 120	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.206
1ND2 The structure of Rhinovirus 16 Deposited 2002-12-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 1 MYR MYRISTIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.206
1ND2 The structure of Rhinovirus 16 Deposited 2002-12-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 5 MYR MYRISTIC ACID × 10	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.206
1ND2 The structure of Rhinovirus 16 Deposited 2002-12-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 6 MYR MYRISTIC ACID × 12	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.206
1ND2 The structure of Rhinovirus 16 Deposited 2002-12-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 1 MYR MYRISTIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å R-free 0.206
1ND3 The structure of HRV16, when complexed with pleconaril, an antiviral compound Deposited 2002-12-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 60 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 60	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.243
1ND3 The structure of HRV16, when complexed with pleconaril, an antiviral compound Deposited 2002-12-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 1 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.243
1ND3 The structure of HRV16, when complexed with pleconaril, an antiviral compound Deposited 2002-12-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 5 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.243
1ND3 The structure of HRV16, when complexed with pleconaril, an antiviral compound Deposited 2002-12-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 6 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 6	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.243
1ND3 The structure of HRV16, when complexed with pleconaril, an antiviral compound Deposited 2002-12-06	Different construct Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 569–853（285 aa） Chain B 70–330（261 aa） Chain C 331–568（238 aa） Chain D 2–69（68 aa）	Not recorded	ZN ZINC ION × 1 W11 3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å R-free 0.243
1QJU HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209 Deposited 1999-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 60 W01 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.212
1QJU HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209 Deposited 1999-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 1 W01 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.212
1QJU HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209 Deposited 1999-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 5 W01 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.212
1QJU HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209 Deposited 1999-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 6 W01 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.212
1QJU HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209 Deposited 1999-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 1 W01 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.212
1QJU HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP61209 Deposited 1999-07-05	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 120 PDB declaration: 120-meric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 30 W01 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2N-METHYL-2H-TETRAZOL-5-YL]-PHENOL × 30 MYR MYRISTIC ACID × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.212
1QJX HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 60 W02 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.235
1QJX HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 1 W02 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.235
1QJX HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 5 W02 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.235
1QJX HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 6 W02 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.235
1QJX HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 1 W02 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.235
1QJX HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND WIN68934 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 120 PDB declaration: 120-meric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 30 W02 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[4-METHYL-2H-TETRAZOL-2-YL]-PHENOL × 30 MYR MYRISTIC ACID × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.235
1QJY HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP65099 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 60 W03 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL × 60 MYR MYRISTIC ACID × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.233
1QJY HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP65099 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 1 W03 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.233
1QJY HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP65099 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 5 W03 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL × 5 MYR MYRISTIC ACID × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.233
1QJY HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP65099 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 6 W03 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL × 6 MYR MYRISTIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.233
1QJY HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP65099 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 1 W03 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.233
1QJY HUMAN RHINOVIRUS 16 COAT PROTEIN IN COMPLEX WITH ANTIVIRAL COMPOUND VP65099 Deposited 1999-07-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 120 PDB declaration: 120-meric	Chain 1 569–853（285 aa） Fragment：RESIDUES 569-853 Chain 2 70–330（261 aa） Fragment：RESIDUES 70-330 Chain 3 331–568（238 aa） Fragment：RESIDUES 331-568 Chain 4 2–69（68 aa） Fragment：RESIDUES 2-69	Not recorded	ZN ZINC ION × 30 W03 2,6-DIMETHYL-1-(3-[3-METHYL-5-ISOXAZOLYL]-PROPANYL)-4-[2-METHYL-4-ISOXAZOLYL]-PHENOL × 30 MYR MYRISTIC ACID × 30	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；VIRUS WAS CRYSTALLISED USING THE HANGING DROP METHOD. 5 MICROLITERS OF VIRUS SOLUTION IN 0.25M HEPES BUFFER (PH 7.5), WITH 0.25M NACL WAS MIXED WITH 5 MICROLITERS OF THE RESERVOIR SOLUTION, 0.5-1.5% PEG 8000.	Resolution 2.80 Å R-free 0.233
1TP7 Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16 Deposited 2004-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1694–2153（460 aa） Fragment：RNA-directed RNA Polymerase (residues 1694-2153)	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1 DMX 3-[BENZYL(DIMETHYL)AMMONIO]PROPANE-1-SULFONATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；PEG 4000, ammonium sulfate, dimethylbenzylammonium propane sulfonate, sodium citrate, glycerol, dithiothreitol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K	Resolution 2.40 Å R-free 0.292
1TP7 Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16 Deposited 2004-06-15	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 1694–2153（460 aa） Fragment：RNA-directed RNA Polymerase (residues 1694-2153)	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；PEG 4000, ammonium sulfate, dimethylbenzylammonium propane sulfonate, sodium citrate, glycerol, dithiothreitol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K	Resolution 2.40 Å R-free 0.292
1TP7 Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16 Deposited 2004-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1694–2153（460 aa） Fragment：RNA-directed RNA Polymerase (residues 1694-2153)	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；PEG 4000, ammonium sulfate, dimethylbenzylammonium propane sulfonate, sodium citrate, glycerol, dithiothreitol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K	Resolution 2.40 Å R-free 0.292
1TP7 Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16 Deposited 2004-06-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1694–2153（460 aa） Fragment：RNA-directed RNA Polymerase (residues 1694-2153)	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；295 K；PEG 4000, ammonium sulfate, dimethylbenzylammonium propane sulfonate, sodium citrate, glycerol, dithiothreitol, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K	Resolution 2.40 Å R-free 0.292
1XR7 Crystal structure of RNA-dependent RNA Polymerase 3D from human rhinovirus serotype 16 Deposited 2004-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1694–2153（460 aa） Fragment：RNA-DIRECTED RNA POLYMERASE	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；286 K；ammonium sulfate, citrate, AMPPNP, MgCl2 or MnCl2, pH 5.60, VAPOR DIFFUSION, HANGING DROP, temperature 286K	Resolution 2.30 Å R-free 0.297
1XR7 Crystal structure of RNA-dependent RNA Polymerase 3D from human rhinovirus serotype 16 Deposited 2004-10-13	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 1694–2153（460 aa） Fragment：RNA-DIRECTED RNA POLYMERASE	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；286 K；ammonium sulfate, citrate, AMPPNP, MgCl2 or MnCl2, pH 5.60, VAPOR DIFFUSION, HANGING DROP, temperature 286K	Resolution 2.30 Å R-free 0.297
4K50 Rhinovirus 16 polymerase elongation complex (r1_form) Deposited 2013-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 1694–2153（460 aa） Fragment：unp residues 1694-2153	Not recorded	GOL GLYCEROL × 1 ACT ACETATE ION × 6 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.16 M ammonium sulfate, 0.08 M sodium acetate, pH 4.6, 20% (w/v) PEG 4000, and 20% (v/v) glycerol and directly frozen , VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 2.93 Å R-free 0.247
4K50 Rhinovirus 16 polymerase elongation complex (r1_form) Deposited 2013-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Monomer；Protein × 1 PDB declaration: trimeric	Chain E 1694–2153（460 aa） Fragment：unp residues 1694-2153	Not recorded	ACT ACETATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.16 M ammonium sulfate, 0.08 M sodium acetate, pH 4.6, 20% (w/v) PEG 4000, and 20% (v/v) glycerol and directly frozen , VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 2.93 Å R-free 0.247
4K50 Rhinovirus 16 polymerase elongation complex (r1_form) Deposited 2013-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–RNA Monomer；Protein × 1 PDB declaration: trimeric	Chain I 1694–2153（460 aa） Fragment：unp residues 1694-2153	Not recorded	GOL GLYCEROL × 2 ACT ACETATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.16 M ammonium sulfate, 0.08 M sodium acetate, pH 4.6, 20% (w/v) PEG 4000, and 20% (v/v) glycerol and directly frozen , VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 2.93 Å R-free 0.247
4K50 Rhinovirus 16 polymerase elongation complex (r1_form) Deposited 2013-04-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–RNA Monomer；Protein × 1 PDB declaration: trimeric	Chain M 1694–2153（460 aa） Fragment：unp residues 1694-2153	Not recorded	ACT ACETATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.16 M ammonium sulfate, 0.08 M sodium acetate, pH 4.6, 20% (w/v) PEG 4000, and 20% (v/v) glycerol and directly frozen , VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 2.93 Å R-free 0.247

12 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLG_HRV16
Isoform	—
PDB entities	1, 2, 3, 4
Chains and sequence ranges	Author chain 1； PDBConstruct 1–285； UniProt 568–852 Author chain 2； PDBConstruct 1–252； UniProt 78–329 Author chain 3； PDBConstruct 1–238； UniProt 330–567 Author chain 4； PDBConstruct 1–77； UniProt 1–77

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	1c8m
Deposition date deposition_date	2000-05-26
Structure title title	REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS
Keywords keywords	RHINOVIRUS COAT PROTEIN, HUMAN RHINOVIRUS 16, ANTIVIRAL COMPOUND, DRUG, WIN COMPOUND, Icosahedral virus, Virus; VIRUS
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	29.54 Å
Radius of gyration Rg (electron density) rg_electron	28.62 Å
Forward intensity I(0) i0	130962000.00
Molecular weight molecular_weight	90052.0 kDa
Excluded volume excluded_volume	112340 Å³
Envelope volume envelope_volume	138910 Å³
Hydration-shell volume shell_volume	39466 Å³
Envelope diameter envelope_diameter	101.0 Å
Shell Rg shell_rg	36.66 Å
Envelope Rg envelope_rg	29.25 Å
Shape Rg shape_rg	28.60 Å
Total Rg total_rg	29.42 Å
Total atoms total_atoms	6338
Residues n_residues	804
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	93.9 Å
Rg (real space) rg_real	29.47 Å
Rg uncertainty (real space) rg_real_error	0.66 Å
I(0) (real space) i0_real	1.3100e+08
I(0) uncertainty (real space) i0_real_error	1.9060e+06
Rg (reciprocal space) rg_reciprocal	29.50 Å
I(0) (reciprocal space) i0_reciprocal	131000000.0000
Solution quality estimate total_estimate	0.8953
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.8 Å
Skewness Skewness skewness	0.295
Kurtosis Kurtosis kurtosis	-0.335
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	27420000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.909

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	32501.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	6820

NPVERYVDEVLNEVLVVPNINQSHPTTSNAAPVLDAAETGHTNKIQPEDTIETRYVQSSQTLDEMSVESFLGRSGCIHESVLDIVDNYNDQSFTKWNINLQEMAQIRRKFEMFTYARFDSEITMVPSVAAKDGHIGHIVMQYMYVPPGAPIPTTRDDYAWQSGTNASVFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDTYKSRYGTVVTNDMGTLCSRIVTSEQLHKVKVVTRIYHKAKHTKAWCPRPPRAVQYSHTHTTNYKLSSEVHNDVAIRPRTNLTTV

Entity 2 Entity 2 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	28096.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

SDRIIQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLDSKMWNSTSKGWWWKLPDALKDMGIFGENMFYHFLGRSGYTVHVQCNASKFHQGTLLVVMIPEHQLATVNKGNVNAGYKYTHPGEAGREVGTQVENEKQPSDDNWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMVRHNNWSLVIIPVCQLQSNNISNIVPITVSISPMCAEFSGARAKTVVQ

Entity 3 Entity 3 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	26314.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

GLPVYVTPGSGQFMTTDDMQSPCALPWYHPTKEIFIPGEVKNLIEMCQVDTLIPINSTQSNIGNVSMYTVTLSPQTKLAEEIFAIKVDIASHPLATTLIGEIASYFTHWTGSLRFSFMFCGTANTTLKVLLAYTPPGIGKPRSRKEAMLGTHVVWDVGLQSTVSLVVPWISASQYRFTTPDTYSSAGYITCWYQTNFVVPPNTPNTAEMLCFVSGCKDFCLRMARDTDLHKQTGPITQ

Entity 4 Entity 4 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	8268.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GAQVSRQNVGTHSTQNMVSNGSSINYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPSVEACGY

Entity 5 Entity 5 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	3-{3,5-DIMETHYL-4-[3-(3-METHYL-ISOXAZOL-5-YL)-PROPOXY]-PHENYL}-5-TRIFLUOROMETHYL-[1,2,4]OXADIAZOLE
Molecular weight formula_weight	381.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	482

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1c8m.1
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

Domain ID domain_id	d1c8m1_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

Domain ID domain_id	d1c8m3_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

CATH v4.4 (3 domains)

Domain ID domain_id	1c8m100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c8m200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1c8m300
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

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8. Citations (9)

THE REFINED STRUCTURE OF A PICORNAVIRUS INHIBITOR CURRENTLY IN CLINICAL TRIALS, WHEN COMPLEXED WITH HUMAN RHINOVIRUS 16

to be published

PRIMARY

ANALYSIS OF THREE STRUCTURALLY RELATED ANTIVIRAL COMPOUNDS IN COMPLEX WITH HUMAN RHINOVIRUS 16

Proc.Natl.Acad.Sci.USA (1999)

DOI: 10.1073/pnas.96.26.14730

The Refined Structure of Human Rhinovirus 16 at 2.15 A Resolution: Implications for the Viral Life Cycle

Structure (1997)

DOI: 10.1016/S0969-2126(97)00199-8

The Structure of Human Rhinovirus 16

Structure (1993)

Structure of a Human Rhinovirus Complexed with its Receptor Molecule

Proc.Natl.Acad.Sci.USA (1993)

A Comparison of the Anti-Rhinoviral Drug Binding Pocket in HRV14 and HRV1A

J.Mol.Biol. (1993)

DOI: 10.1006/jmbi.1993.1137

Crystal Structure of Human Rhinovirus Serotype 1A (HRV1A)

J.Mol.Biol. (1989)

The Site of Attachment in Human Rhinovirus 14 for Antiviral Agents that Inhibit Uncoating

Science (1986)

Structure of a Human Common Cold Virus and Functional Relationship to Other Picornaviruses

Nature (1985)

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Unit-cell length a length_a	360.300 Å
Unit-cell length b length_b	343.330 Å
Unit-cell length c length_c	332.630 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	120

Space group space_group	P 2 21 21
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2430
R_work r_work	0.2190
R_free r_free	0.2260

fit	/app/data/saxs_computation/c8/1c8m/1c8m.fit
pddf	/app/data/pr_computation/c8/1c8m/1c8m.pr.out
profile	/app/data/saxs_computation/c8/1c8m/1c8m.dat

REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS

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

HUMAN RHINOVIRUS 16 COAT PROTEIN

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

6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

8. Citations (9)

9. Files and Curves (10)

Files (7)

Curves (3)