SAXSdb — 1rue

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

RHINOVIRUS 14

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	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE × 60	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE × 1	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 20	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE × 5	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 24	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE × 6	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 4	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE × 1	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 80	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE × 20	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	1rue
Deposition date deposition_date	1995-06-09
Structure title title	RHINOVIRUS 14 SITE DIRECTED MUTANT N1219A COMPLEXED WITH ANTIVIRAL COMPOUND WIN 52035
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.

1rue__assembly_1__model_1

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

Download this curve (.dat)

1rue__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1rue__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	377280
Residues	48240
Excluded volume	6713800 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1rue__assembly_1__model_1`	240-MERIC （240）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1rue__assembly_2__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`1rue__assembly_3__model_1`	eicosameric （20）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`1rue__assembly_4__model_1`	24-meric （24）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`1rue__assembly_5__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
6	1	`1rue__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	RHINOVIRUS 14
Molecular weight formula_weight	32517.5 kDa
Mutation mutation	N(1)219A
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	6288

GLGDELEEVIVEKTKQTVASISSGPKHTQKVPILTANETGATMPVLPSDSIETRTTYMHFNGSETDVECFLGRAACVHVTEIQNKDATGIDNHREAKLFNDWKINLSSLVQLRKKLELFTYVRFDSEYTILATASQPDSANYSSNLVVQAMYVPPGAPNPKEWDDYTWQSASNPSVFFKVGDTSRFSVPYVGLASAYNCFYDGYSHDDAETQYGITVLAHMGSMAFRIVNEHDEHKTLVKIRVYHRAKHVEAWIPRAPRALPYTSIGRTNYPKNTEPVIKKRKGDIKSY

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	RHINOVIRUS 14
Molecular weight formula_weight	28501.4 kDa
Mutation mutation	N(1)219A
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	RHINOVIRUS 14
Molecular weight formula_weight	26236.8 kDa
Mutation mutation	N(1)219A
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	RHINOVIRUS 14
Molecular weight formula_weight	7183.9 kDa
Mutation mutation	N(1)219A
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 non-polymer

Description description	5-(5-(4-(4,5-DIHYDRO-2-OXAZOLY)PHENOXY)PENTYL)-3-METHYL ISOXAZOLE
Molecular weight formula_weight	314.4 kDa
Source method src_method	syn
Copy count entity_count	1

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1rue.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	d1rue1_
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	d1rue3_
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	1rue100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1rue200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1rue300
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1rue400
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 (12)

Structural studies on human rhinovirus 14 drug-resistant compensation mutants.

J.Mol.Biol. (1995)

PMID: 7473717 · DOI: 10.1006/jmbi.1995.0536 PRIMARY

Win 52035-2 Inhibits Both Attachment and Eclipse of Human Rhinovirus 14

J.Virol. (1993)

Analysis of the Structure of a Common Cold Virus, Human Rhinovirus 14, Refined at a Resolution of 3.0 Angstroms

J.Mol.Biol. (1990)

Three Dimensional Structures of Drug-Resistant Mutants of Human Rhinovirus 14

J.Mol.Biol. (1989)

Structural Analysis of Antiviral Agents that Interact with the Capsid of Human Rhinoviruses

Proteins (1989)

Genetics and Molecular Basis for Resistance of Human Rhinovirus 14 to an Antiviral Drug

J.Virol. (1989)

The Use of Molecular Replacement Phases for the Refinement of the Human Rhinovirus 14 Structure

Acta Crystallogr.,Sect.A (1988)

Structural Analysis of a Series of Antiviral Agents Complexed with Human Rhinovirus 14

Proc.Natl.Acad.Sci.USA (1988)

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

Acta Crystallogr.,Sect.A (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)

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	2.900 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

RHINOVIRUS 14 SITE DIRECTED MUTANT N1219A COMPLEXED WITH ANTIVIRAL COMPOUND WIN 52035

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

RHINOVIRUS 14

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

1rue__assembly_1__model_1

1rue__assembly_1__model_1 | I(q)

1rue__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 non-polymer

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (12)

RHINOVIRUS 14 SITE DIRECTED MUTANT N1219A COMPLEXED WITH ANTIVIRAL COMPOUND WIN 52035

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

RHINOVIRUS 14

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

1rue__assembly_1__model_1

1rue__assembly_1__model_1 | I(q)

1rue__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 non-polymer

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (12)