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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

Method: ELECTRON MICROSCOPY Dmax: 124.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP1)

OrganismNot specified

UniProt P05362

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 300 PDB declaration: 300-MERIC（300） Consistent with protein copy count Chain 1； UniProt 28–212 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 60 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP2) × 60 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP3) × 60 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP4) × 60 （Q82122） 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
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain 1； UniProt 28–212 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 1 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP2) × 1 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP3) × 1 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP4) × 1 （Q82122） 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
3 Insufficient information Heteromer Protein × 25 PDB declaration: 25-meric（25） Consistent with protein copy count Chain 1； UniProt 28–212 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 5 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP2) × 5 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP3) × 5 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP4) × 5 （Q82122） 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
4 Insufficient information Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count Chain 1； UniProt 28–212 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 6 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP2) × 6 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP3) × 6 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP4) × 6 （Q82122） 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
5 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain 1； UniProt 28–212 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 1 PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP2) × 1 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP3) × 1 （Q82122） PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP4) × 1 （Q82122） 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

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 1D3E Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) 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 experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-MERIC
Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-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 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) 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 experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-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 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) 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 experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric
Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-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 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) 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 experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric
Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-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 26.00 Å
1D3I CRYO-EM STRUCTURE OF HUMAN RHINOVIRUS 14 (HRV14) 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 experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain I 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions HRV14 WAS INCUBATED WITH D1D2-ICAM-1 FOR 30 MINUTES AT 4 DEGREES CELSIUS (277 KELVIN) USING AN EIGHT-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 26.00 Å
1D3L D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES. Deposited 1999-09-29 Different construct 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 28–212（185 aa） Fragment：FIRST TWO DOMAINS, RESIDUES 1-185
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN WAS DESIALATED WITH NEURAMINIDASE (8 HR AT 37 DEGREES IN 100 MM SODIUM ACETATE, PH 6.5, 10 MG/ML PROTEIN, 0.1 ENZYME UNIT/ML), DIALYZED AGAINST 10 MM TRIS, 25 MM NACL (PH 6.0), AND PASSED THROUGH MONO-Q COLUMN. DESIALATED MATERIAL WAS CRYSTALLIZED BY HANGING DROP METHODS: 17 MG/ML PROTEIN IN BUFFER: 10 MM TRIS,25 MM NACL,1 MM MGCL2,1 MM CACL2, WAS PRECIPITATED FROM 24-27% PEG 3350 IN SAME BUFFER.
Resolution 3.25 Å
1IAM STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1 Deposited 1998-02-22 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 × 2 PDB declaration: dimeric
Chain A 28–212（185 aa） Fragment：TWO N-TERMINAL, IMMUNOGLOBULIN DOMAINS
Mutation：N103Q, N118Q, N156Q NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；PROTEIN IN 10 MM TRIS, PH 7.5, 25 MM NACL, WAS CRYSTALLIZED FROM 20% PEG 4000 IN 10 MM TRIS AS PRECIPITANT
Resolution 2.10 Å R-free 0.303
1IC1 THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1 Deposited 1998-03-09 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 28–217（190 aa） Fragment：N-TERMINAL 190 RESIDUE DOMAIN
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；17% PEG 4000, NA CACODYLATE, PH 6.5, AND 100 MM B-OCTYL-GLUCOPYRANOSIDE.
Resolution 3.00 Å R-free 0.279
1IC1 THE CRYSTAL STRUCTURE FOR THE N-TERMINAL TWO DOMAINS OF ICAM-1 Deposited 1998-03-09 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 28–217（190 aa） Fragment：N-TERMINAL 190 RESIDUE DOMAIN
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；17% PEG 4000, NA CACODYLATE, PH 6.5, AND 100 MM B-OCTYL-GLUCOPYRANOSIDE.
Resolution 3.00 Å R-free 0.279
1MQ8 Crystal structure of alphaL I domain in complex with ICAM-1 Deposited 2002-09-15 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 28–318（291 aa） Fragment：domains 1 and 2
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25% PEG 4000, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP at 298K
Resolution 3.30 Å R-free 0.313
1MQ8 Crystal structure of alphaL I domain in complex with ICAM-1 Deposited 2002-09-15 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 28–318（291 aa） Fragment：domains 1 and 2
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25% PEG 4000, 0.1 M sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP at 298K
Resolution 3.30 Å R-free 0.313
1P53 The Crystal Structure of ICAM-1 D3-D5 fragment Deposited 2003-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 212–477（266 aa） Fragment：ICAM-1 extracellular Domain 3-5, ecto-fragment
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；15mg/ml protein, NH4H2PO4, 0.1 M Na-citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.06 Å R-free 0.252
1P53 The Crystal Structure of ICAM-1 D3-D5 fragment Deposited 2003-04-24 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 212–477（266 aa） Fragment：ICAM-1 extracellular Domain 3-5, ecto-fragment
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；15mg/ml protein, NH4H2PO4, 0.1 M Na-citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.06 Å R-free 0.252
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-MERIC
Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5
Mutation：K29M NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 480 ELECTRON MICROSCOPY
cryo-EM buffer TRIS；pH 7.2；TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE
Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5
Mutation：K29M NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer TRIS；pH 7.2；TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE
Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric
Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5
Mutation：K29M NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 40 ELECTRON MICROSCOPY
cryo-EM buffer TRIS；pH 7.2；TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE
Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric
Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5
Mutation：K29M NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 48 ELECTRON MICROSCOPY
cryo-EM buffer TRIS；pH 7.2；TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE
Resolution 8.00 Å
1Z7Z Cryo-em structure of human coxsackievirus A21 complexed with five domain icam-1kilifi Deposited 2005-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain I 28–477（450 aa） Fragment：ICAM-1 EXTRACELLULAR DOMAIN 1-5
Mutation：K29M NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer TRIS；pH 7.2；TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE AT LIQUID NITROGEN TEMPERATURE
Resolution 8.00 Å
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 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 A 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 10 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain S 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 11 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain U 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 12 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain W 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 13 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Y 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 14 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain a 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain M 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain O 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
3TCX Structure of Engineered Single Domain ICAM-1 D1 with High-Affinity aL Integrin I Domain of Native C-Terminal Helix Conformation Deposited 2011-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 29–112（84 aa） Fragment：DOMAIN 1, unp residues 29-112
Mutation：T2V, I10T, T23A, P38V, P63V, S67A, T78A MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6；277 K；pH 6.0, EVAPORATION, temperature 277K
Resolution 3.60 Å R-free 0.234
5MZA The DBLb domain of PF11_0521 PfEMP1 bound to human ICAM-1 Deposited 2017-01-31 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 28–212（185 aa）
Not recorded 3PO TRIPHOSPHATE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；10% (w/v) PEG 20000, 20% (v/v) PEG 500 and 0.1M Tris-BICINE (pH 8.5)
Resolution 2.78 Å R-free 0.236
6EIT Coxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1 Deposited 2017-09-19 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 240 PDB declaration: 240-meric
Chain 4 28–112（85 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；TBS buffer (Coxsackievirus A24v) Phosphate buffer (ICAM-1 D1-D2)
cryo-EM vitrification conditions Cryogen ETHANE；On-grid binding of the receptor was performed by applying 3 microliters of ICAM-1 (9.85 mg/ml) to the pre-blotted, virus-containing grid, and leaving for 30 seconds before blotting and freezing
Resolution 3.90 Å
6S8U Structure of the PfEMP1 IT4var13 DBLbeta domain bound to ICAM-1 Deposited 2019-07-10 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 28–212（185 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1M Tris pH 8, 25% PEG 350 MME
Resolution 3.67 Å R-free 0.286
7BG7 HRV14 in complex with its receptor ICAM-1 Deposited 2021-01-06 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: 300-meric
Chain B 28–480（453 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.40 Å

12 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ICAM1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain 1； PDBConstruct 1–185； UniProt 28–212

PROTEIN (RHINOVIRUS 16 COAT PROTEIN VP1)

OrganismNot specified

UniProt Q82122

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 300 PDB declaration: 300-MERIC（300） Consistent with protein copy count Chain 1； UniProt 573–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–68 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 60 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
2 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain 1； UniProt 573–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–68 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 1 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
3 Insufficient information Heteromer Protein × 25 PDB declaration: 25-meric（25） Consistent with protein copy count Chain 1； UniProt 573–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–68 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 5 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
4 Insufficient information Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count Chain 1； UniProt 573–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–68 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 6 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
5 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain 1； UniProt 573–852 Chain 2； UniProt 78–329 Chain 3； UniProt 330–567 Chain 4； UniProt 1–68 Not recorded PROTEIN (INTERCELLULAR ADHESION MOLECULE-1) × 1 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

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 1D3E 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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
1C8M REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS Deposited 2000-05-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-MERIC
Chain 1 568–852（285 aa） Fragment：RESIDUES 569-853
Chain 2 78–329（252 aa） Fragment：RESIDUES 79-330
Chain 3 330–567（238 aa） Fragment：RESIDUES 331-568
Chain 4 1–77（77 aa） Fragment：RESIDUES 2-78
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
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
1C8M REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS Deposited 2000-05-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain 1 568–852（285 aa） Fragment：RESIDUES 569-853
Chain 2 78–329（252 aa） Fragment：RESIDUES 79-330
Chain 3 330–567（238 aa） Fragment：RESIDUES 331-568
Chain 4 1–77（77 aa） Fragment：RESIDUES 2-78
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
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
1C8M REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS Deposited 2000-05-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 20 PDB declaration: eicosameric
Chain 1 568–852（285 aa） Fragment：RESIDUES 569-853
Chain 2 78–329（252 aa） Fragment：RESIDUES 79-330
Chain 3 330–567（238 aa） Fragment：RESIDUES 331-568
Chain 4 1–77（77 aa） Fragment：RESIDUES 2-78
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
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
1C8M REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS Deposited 2000-05-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 568–852（285 aa） Fragment：RESIDUES 569-853
Chain 2 78–329（252 aa） Fragment：RESIDUES 79-330
Chain 3 330–567（238 aa） Fragment：RESIDUES 331-568
Chain 4 1–77（77 aa） Fragment：RESIDUES 2-78
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
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
1C8M REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS Deposited 2000-05-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain 1 568–852（285 aa） Fragment：RESIDUES 569-853
Chain 2 78–329（252 aa） Fragment：RESIDUES 79-330
Chain 3 330–567（238 aa） Fragment：RESIDUES 331-568
Chain 4 1–77（77 aa） Fragment：RESIDUES 2-78
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
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
1C8M REFINED CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS 16 COMPLEXED WITH VP63843 (PLECONARIL), AN ANTI-PICORNAVIRAL DRUG CURRENTLY IN CLINICAL TRIALS Deposited 2000-05-26 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 120 PDB declaration: 120-meric
Chain 1 568–852（285 aa） Fragment：RESIDUES 569-853
Chain 2 78–329（252 aa） Fragment：RESIDUES 79-330
Chain 3 330–567（238 aa） Fragment：RESIDUES 331-568
Chain 4 1–77（77 aa） Fragment：RESIDUES 2-78
Not recorded 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
1NCR The structure of Rhinovirus 16 when complexed with pleconaril, an antiviral compound Deposited 2002-12-05 Different construct Different oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 oligomeric state Different ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 experimental method 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 experimental method 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 method 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 method 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 method 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 method 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 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_HRV16
Isoform —
PDB entities 2, 3, 4, 5
Chains and sequence ranges Author chain 1； PDBConstruct 1–285； UniProt 573–852 Author chain 2； PDBConstruct 1–252； UniProt 78–329 Author chain 3； PDBConstruct 1–238； UniProt 330–567 Author chain 4； PDBConstruct 1–68； UniProt 1–68

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

SAXS profile for 1d3e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d3e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d3e
Deposition date deposition_date1999-09-29
Structure title titleCRYO-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
Keywords keywords;HUMAN RHINOVIRUS, HRV16, ICAM-1, FITTING OF X-RAY STRUCTURES INTO CRYO-EM RECONSTRUCTIONS, COMMON COLD, VIRUS UNCOATING, VIRUS/ VIRAL PROTEIN, RHINOVIRUS-RECEPTOR COMPLEX, Icosahedral virus, Virus-Receptor COMPLEX ;; Virus/Receptor
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.25 Å
Radius of gyration Rg (electron density) rg_electron34.15 Å
Forward intensity I(0) i0186859000.00
Molecular weight molecular_weight110050.0 kDa
Excluded volume excluded_volume134200 ų
Envelope volume envelope_volume119030 ų
Hydration-shell volume shell_volume33073 ų
Envelope diameter envelope_diameter131.1 Å
Shell Rg shell_rg35.95 Å
Envelope Rg envelope_rg32.74 Å
Shape Rg shape_rg34.14 Å
Total Rg total_rg34.26 Å
Total atoms total_atoms—
Residues n_residues—
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax124.7 Å
Rg (real space) rg_real34.37 Å
Rg uncertainty (real space) rg_real_error1.17 Å
I(0) (real space) i0_real1.8690e+08
I(0) uncertainty (real space) i0_real_error3.4140e+06
Rg (reciprocal space) rg_reciprocal34.30 Å
I(0) (reciprocal space) i0_reciprocal186800000.0000
Solution quality estimate total_estimate0.8473
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.9 Å
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.068
Angular range angular_range— – 0.2300 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22190000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.952
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd1d3e1_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1d3e2_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1d3e3_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1d3e4_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1d3ei_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
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8. Citations (5)

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9. Files and Curves (10)