SAXSdb — 4rhv

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

HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1)

Human rhinovirus 14

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 240	water × 240	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 20	water × 20	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 24	water × 24	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 80	water × 80	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	POLG_HRV14
Isoform	—
PDB entities	1, 2, 3, 4
Chains and sequence ranges	Author chain 1； PDBConstruct 1–289； UniProt 567–855 Author chain 2； PDBConstruct 1–262； UniProt 69–330 Author chain 3； PDBConstruct 1–236； UniProt 331–566 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4rhv
Deposition date deposition_date	1988-01-25
Structure title title	THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT OF THE HUMAN RHINOVIRUS 14 STRUCTURE
Keywords keywords	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.

4rhv__assembly_1__model_1

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

Download this curve (.dat)

4rhv__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4rhv__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)	133.40 Å
Total Rg	133.40 Å
Atom count	376080
Residues	48240
Excluded volume	6689300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4rhv__assembly_1__model_1`	240-MERIC （240）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4rhv__assembly_2__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`4rhv__assembly_3__model_1`	eicosameric （20）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`4rhv__assembly_4__model_1`	24-meric （24）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`4rhv__assembly_5__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
6	1	`4rhv__assembly_6__model_1`	80-meric （80）	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 (5)

Entity 1 Entity 1 polymer

Description description	HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1)
Molecular weight formula_weight	32560.5 kDa
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	6542

GLGDELEEVIVEKTKQTVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHFNGSETDVECFLGRAACVHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFTYVRFDSEYTILATASQPDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFSVPYVGLASAYNCFYDGYSHDDAETQYGITVLNHMGSMAFRIVNEHDEHKTLVKIRVYHRAKHVEAWIPRAPRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY

Source Source

Source organism organism	Human rhinovirus 14
NCBI taxonomy ID ncbi_taxonomy_id	12131
Host organism host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2)
Molecular weight formula_weight	28501.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

SPNVEACGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSVCRFYTLDSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSGCLLVVVIPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVLYNMNGTLLGNLLIFPHQFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPITVTIAPMCTEFSGIRSKSIVPQ

Source Source

Source organism organism	Human rhinovirus 14
NCBI taxonomy ID ncbi_taxonomy_id	12131
Host organism host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3)
Molecular weight formula_weight	26236.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

GLPTTTLPGSGQFLTTDDRQSPSALPNYEPTPRIHIPGKVHNLLEIIQVDTLIPMNNTHTKDEVNSYLIPLNANRQNEQVFGTNLFIGDGVFKTTLLGEIVQYYTHWSGSLRFSLMYTGPALSSAKLILAYTPPGARGPQDRREAMLGTHVVWDIGLQSTIVMTIPWTSGVQFRYTDPDTYTSAGFLSCWYQTSLILPPETTGQVYLLSFISACPDFKLRLMKDTQTISQTVALTE

Source Source

Source organism organism	Human rhinovirus 14
NCBI taxonomy ID ncbi_taxonomy_id	12131
Host organism host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP4)
Molecular weight formula_weight	7183.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GAQVSTQKSGSHENQNILTNGSNQTFTVINYYKDAASTSSAGQSLSMDPSKFTEPVKDLMLKGAPALN

Source Source

Source organism organism	Human rhinovirus 14
NCBI taxonomy ID ncbi_taxonomy_id	12131
Host organism host_organism	Homo sapiens

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	274

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d4rhv.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	d4rhv1_
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	d4rhv3_
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 (4 domains)

Domain ID domain_id	4rhv100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4rhv200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4rhv300
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	4rhv400
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	80 — Rhinovirus 14, subunit 4
Homologous superfamily homologous superfamily	10 — Picornavirus coat protein VP4

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7. Citations (10)

The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure.

Acta Crystallogr.,Sect.A (1988)

PMID: 2856083 · DOI: 10.1107/S0108767387011875 PRIMARY

The Structure Determination of a Common Cold Virus, Human Rhinovirus 14

Acta Crystallogr.,Sect.A (1987)

Implications of the Picornavirus Capsid Structure for Polyprotein Structure

Proc.Natl.Acad.Sci.USA (1987)

The Structure of a Human Common Cold Virus (Rhinovirus 14) and its Evolutionary Relations to Other Viruses

Chem.Scr. (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)

Virion Orientation in Cubic Crystals of the Human Common Cold Virus Hrv14

J.Mol.Biol. (1984)

Picornaviruses of Two Different Genera Have Similar Structures

J.Mol.Biol. (1984)

Crystallization of a Common Cold Virus, Human Rhinovirus 14. (Quote)Isomorphism(Quote) with Poliovirus Crystals

Proc.Natl.Acad.Sci.USA (1983)

Analysis of the Structure of Human Rhinovirus 14 Refined at a Resolution of 3.0 Angstroms

To be Published

Unit-cell length a length_a	445.100 Å
Unit-cell length b length_b	445.100 Å
Unit-cell length c length_c	445.100 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	240

Space group space_group	P 21 3
Space-group number int_tables_number	198
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	—
R_work r_work	0.1600
R_free r_free	—

THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT OF THE HUMAN RHINOVIRUS 14 STRUCTURE

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

HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1)

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

4rhv__assembly_1__model_1

4rhv__assembly_1__model_1 | I(q)

4rhv__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (5)

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 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (10)

THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT OF THE HUMAN RHINOVIRUS 14 STRUCTURE

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

HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1)

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

4rhv__assembly_1__model_1

4rhv__assembly_1__model_1 | I(q)

4rhv__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (5)

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 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (10)