SAXSdb — 1mec

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

MENGO VIRUS COAT PROTEIN (SUBUNIT VP1)

Mengo virus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 240	PHOSPHATE ION × 120 water × 240	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	PHOSPHATE ION × 2 water × 4	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 20	PHOSPHATE ION × 10 water × 20	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 24	PHOSPHATE ION × 12 water × 24	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 4	PHOSPHATE ION × 2 water × 4	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 240	PHOSPHATE ION × 120 water × 240	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	POLG_ENMGO
Isoform	—
PDB entities	1, 2, 3, 4
Chains and sequence ranges	Author chain 1； PDBConstruct 1–274； UniProt 558–831 Author chain 2； PDBConstruct 1–256； UniProt 71–326 Author chain 3； PDBConstruct 1–231； UniProt 327–557 Author chain 4； PDBConstruct 1–70； UniProt 1–70

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	1mec
Deposition date deposition_date	1992-01-17
Structure title title	CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY
Keywords keywords	CARDIO PICORNAVIRUS 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.

1mec__assembly_1__model_1

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

Download this curve (.dat)

1mec__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1mec__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)	133.80 Å
Total Rg	133.80 Å
Atom count	384840
Residues	49380
Excluded volume	6820200 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1mec__assembly_1__model_1`	240-MERIC （240）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1mec__assembly_2__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`1mec__assembly_3__model_1`	eicosameric （20）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`1mec__assembly_4__model_1`	24-meric （24）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`1mec__assembly_5__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
6	1	`1mec__assembly_6__model_1`	240-meric （240）	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 (6)

Entity 1 Entity 1 polymer

Description description	MENGO VIRUS COAT PROTEIN (SUBUNIT VP1)
Molecular weight formula_weight	30274.0 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	6710

GVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGRFAVKSGSLESGFAPFSNKACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGAHGLLVRWCPTGTPTKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGDLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVL

Source Source

Source organism organism	Mengo virus
NCBI taxonomy ID ncbi_taxonomy_id	12107

Entity 2 Entity 2 polymer

Description description	MENGO VIRUS COAT PROTEIN (SUBUNIT VP2)
Molecular weight formula_weight	28791.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

DQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQ

Source Source

Source organism organism	Mengo virus
NCBI taxonomy ID ncbi_taxonomy_id	12107

Entity 3 Entity 3 polymer

Description description	MENGO VIRUS COAT PROTEIN (SUBUNIT VP1)
Molecular weight formula_weight	25186.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

SPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKMPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDQANITNVDGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQ

Source Source

Source organism organism	Mengo virus
NCBI taxonomy ID ncbi_taxonomy_id	12107

Entity 4 Entity 4 polymer

Description description	MENGO VIRUS COAT PROTEIN (SUBUNIT VP1)
Molecular weight formula_weight	7336.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLA

Source Source

Source organism organism	Mengo virus
NCBI taxonomy ID ncbi_taxonomy_id	12107

Entity 5 Entity 5 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	296

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1mec.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	d1mec1_
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	d1mec3_
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	1mec100
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1mec200
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1mec300
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1mec400
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	90 — Foot-And-Mouth Disease Virus, subunit 4
Homologous superfamily homologous superfamily	10 — Capsid protein VP4 superfamily, Picornavirus

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7. Citations (8)

;Conformational variability of a picornavirus capsid: pH-dependent structural changes of Mengo virus related to its host receptor attachment site and disassembly. ;

Virology (1990)

PMID: 2155508 · DOI: 10.1016/0042-6822(90)90198-Z PRIMARY

Structural Refinement and Analysis of Mengo Virus

J.Mol.Biol. (1990)

Structure Determination of Mengo Virus

Acta Crystallogr.,Sect.B (1989)

The Atomic Structure of Mengo Virus at 3.0 Angstroms Resolution

Science (1987)

Implications of the Picornavirus Capsid Structure for Polyprotein Processing

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. (1986)

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

Nature (1985)

Picornaviruses of Two Different Genera Have Similar Structures

J.Mol.Biol. (1984)

Unit-cell length a length_a	439.800 Å
Unit-cell length b length_b	426.900 Å
Unit-cell length c length_c	421.200 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 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.200 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY

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

MENGO VIRUS 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

1mec__assembly_1__model_1

1mec__assembly_1__model_1 | I(q)

1mec__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 (6)

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 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (8)

CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY

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

MENGO VIRUS 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

1mec__assembly_1__model_1

1mec__assembly_1__model_1 | I(q)

1mec__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 (6)

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 water

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

7. Citations (8)