1aym

HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION

Method: X-RAY DIFFRACTION

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

HUMAN RHINOVIRUS 16 COAT PROTEIN

Human rhinovirus sp.

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 240	HUMAN RHINOVIRUS 16 COAT PROTEIN × 60 （P23008） ZINC ION × 60 LAURIC ACID × 60 MYRISTIC ACID × 60 water × 240	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （P23008） ZINC ION × 1 LAURIC ACID × 1 MYRISTIC ACID × 1 water × 4	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 20	HUMAN RHINOVIRUS 16 COAT PROTEIN × 5 （P23008） ZINC ION × 5 LAURIC ACID × 5 MYRISTIC ACID × 5 water × 20	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 24	HUMAN RHINOVIRUS 16 COAT PROTEIN × 6 （P23008） ZINC ION × 6 LAURIC ACID × 6 MYRISTIC ACID × 6 water × 24	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 4	HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （P23008） ZINC ION × 1 LAURIC ACID × 1 MYRISTIC ACID × 1 water × 4	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 120	HUMAN RHINOVIRUS 16 COAT PROTEIN × 30 （P23008） ZINC ION × 30 LAURIC ACID × 30 MYRISTIC ACID × 30 water × 120	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	POLG_HRV16
Isoform	—
PDB entities	1, 2, 3
Chains and sequence ranges	Author chain 1； PDBConstruct 1–285； UniProt 568–852 Author chain 2； PDBConstruct 1–261； UniProt 69–329 Author chain 3； PDBConstruct 1–238； UniProt 330–567

HUMAN RHINOVIRUS 16 COAT PROTEIN

Human rhinovirus sp.

UniProt P23008

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 240	HUMAN RHINOVIRUS 16 COAT PROTEIN × 60 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 60 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 60 （Q82122） ZINC ION × 60 LAURIC ACID × 60 MYRISTIC ACID × 60 water × 240	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （Q82122） ZINC ION × 1 LAURIC ACID × 1 MYRISTIC ACID × 1 water × 4	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 20	HUMAN RHINOVIRUS 16 COAT PROTEIN × 5 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 5 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 5 （Q82122） ZINC ION × 5 LAURIC ACID × 5 MYRISTIC ACID × 5 water × 20	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 24	HUMAN RHINOVIRUS 16 COAT PROTEIN × 6 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 6 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 6 （Q82122） ZINC ION × 6 LAURIC ACID × 6 MYRISTIC ACID × 6 water × 24	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 4	HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 1 （Q82122） ZINC ION × 1 LAURIC ACID × 1 MYRISTIC ACID × 1 water × 4	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 120	HUMAN RHINOVIRUS 16 COAT PROTEIN × 30 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 30 （Q82122） HUMAN RHINOVIRUS 16 COAT PROTEIN × 30 （Q82122） ZINC ION × 30 LAURIC ACID × 30 MYRISTIC ACID × 30 water × 120	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	POLG_HRV1A
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain 4； PDBConstruct 1–68； UniProt 1–44

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1aym
Deposition date deposition_date	1997-11-06
Structure title title	HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION
Keywords keywords	HUMAN RHINOVIRUS 16, RNA, SITE-DIRECTED MUTAGENESIS, RHINOVIRUS COAT PROTEIN, Icosahedral virus, Virus; VIRUS
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1aym__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1aym__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1aym__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	0.00 Å
Rg (electron density)	132.20 Å
Total Rg	132.20 Å
Atom count	381732
Residues	48240
Excluded volume	6776900 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1aym__assembly_1__model_1`	240-MERIC （240）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1aym__assembly_2__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`1aym__assembly_3__model_1`	eicosameric （20）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`1aym__assembly_4__model_1`	24-meric （24）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`1aym__assembly_5__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
6	1	`1aym__assembly_6__model_1`	120-meric （120）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	32501.4 kDa
Mutation mutation	N-TERMINAL MYRISTOYLATION ON VP4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	6975

NPVERYVDEVLNEVLVVPNINQSHPTTSNAAPVLDAAETGHTNKIQPEDTIETRYVQSSQTLDEMSVESFLGRSGCIHESVLDIVDNYNDQSFTKWNINLQEMAQIRRKFEMFTYARFDSEITMVPSVAAKDGHIGHIVMQYMYVPPGAPIPTTRDDYAWQSGTNASVFWQHGQPFPRFSLPFLSIASAYYMFYDGYDGDTYKSRYGTVVTNDMGTLCSRIVTSEQLHKVKVVTRIYHKAKHTKAWCPRPPRAVQYSHTHTTNYKLSSEVHNDVAIRPRTNLTTV

Source Source

Source organism organism	Human rhinovirus sp.
NCBI taxonomy ID ncbi_taxonomy_id	169066
Host organism host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	28990.6 kDa
Mutation mutation	N-TERMINAL MYRISTOYLATION ON VP4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

SPSVEACGYSDRIIQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLDSKMWNSTSKGWWWKLPDALKDMGIFGENMFYHFLGRSGYTVHVQCNASKFHQGTLLVVMIPEHQLATVNKGNVNAGYKYTHPGEAGREVGTQVENEKQPSDDNWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMVRHNNWSLVIIPVCQLQSNNISNIVPITVSISPMCAEFSGARAKTVVQ

Source Source

Source organism organism	Human rhinovirus sp.
NCBI taxonomy ID ncbi_taxonomy_id	169066
Host organism host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	26314.2 kDa
Mutation mutation	N-TERMINAL MYRISTOYLATION ON VP4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

GLPVYVTPGSGQFMTTDDMQSPCALPWYHPTKEIFIPGEVKNLIEMCQVDTLIPINSTQSNIGNVSMYTVTLSPQTKLAEEIFAIKVDIASHPLATTLIGEIASYFTHWTGSLRFSFMFCGTANTTLKVLLAYTPPGIGKPRSRKEAMLGTHVVWDVGLQSTVSLVVPWISASQYRFTTPDTYSSAGYITCWYQTNFVVPPNTPNTAEMLCFVSGCKDFCLRMARDTDLHKQTGPITQ

Source Source

Source organism organism	Human rhinovirus sp.
NCBI taxonomy ID ncbi_taxonomy_id	169066
Host organism host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	HUMAN RHINOVIRUS 16 COAT PROTEIN
Molecular weight formula_weight	7374.0 kDa
Mutation mutation	N-TERMINAL MYRISTOYLATION ON VP4
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GAQVSRQNVGTHSTQNMVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQ

Source Source

Source organism organism	Human rhinovirus sp.
NCBI taxonomy ID ncbi_taxonomy_id	169066
Host organism host_organism	Homo sapiens

Entity 5 Entity 5 non-polymer

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

Entity 6 Entity 6 non-polymer

Description description	LAURIC ACID
Molecular weight formula_weight	200.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	MYRISTIC ACID
Molecular weight formula_weight	228.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 8 Entity 8 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	533

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1aym.1
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

Domain ID domain_id	d1aym1_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

Domain ID domain_id	d1aym3_
Class class	b — All beta proteins
Fold Fold fold	b.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamily	b.121.4 — Positive stranded ssRNA viruses
Family Family family	b.121.4.1 — Picornaviridae-like VP (VP1, VP2, VP3 and VP4)

CATH v4.4 (3 domains)

Domain ID domain_id	1aym100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1aym200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1aym300
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

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7. Citations (8)

The refined structure of human rhinovirus 16 at 2.15 A resolution: implications for the viral life cycle.

Structure (1997)

PMID: 9083115 · DOI: 10.1016/S0969-2126(97)00199-8 PRIMARY

The Structure of Human Rhinovirus 16

Structure (1993)

A Comparison of the Anti-Rhinoviral Drug Binding Pocket in Hrv14 and Hrv1A

J.Mol.Biol. (1993)

Structure of a Human Rhinovirus Complexed with its Receptor Molecule

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

Crystal Structure of Human Rhinovirus Serotype 1A (Hrv1A)

J.Mol.Biol. (1989)

Common Cold Viruses

Trends Biochem.Sci. (1987)

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

Science (1986)

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

Nature (1985)

Unit-cell length a length_a	362.600 Å
Unit-cell length b length_b	347.100 Å
Unit-cell length c length_c	334.900 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	120

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

Resolution resolution	2.150 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.2300
R_work r_work	0.2300
R_free r_free	0.2330

HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION

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

HUMAN RHINOVIRUS 16 COAT PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

HUMAN RHINOVIRUS 16 COAT PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1aym__assembly_1__model_1

1aym__assembly_1__model_1 | I(q)

1aym__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (8)

HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION

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

HUMAN RHINOVIRUS 16 COAT PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

HUMAN RHINOVIRUS 16 COAT PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1aym__assembly_1__model_1

1aym__assembly_1__model_1 | I(q)

1aym__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (8)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 polymer

Polymer Polymer

Source Source

Entity 4 Entity 4 polymer

Polymer Polymer

Source Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

CATH v4.4 (3 domains)

7. Citations (8)