SAXSdb — 1m0f

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

Capsid Protein F

Enterobacteria phage alpha3

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 420	Scaffolding protein D × 240 Major Spike Protein G × 60 （P31281） Scaffolding Protein B × 60	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 7	Scaffolding protein D × 4 Major Spike Protein G × 1 （P31281） Scaffolding Protein B × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 35	Scaffolding protein D × 20 Major Spike Protein G × 5 （P31281） Scaffolding Protein B × 5	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 42	Scaffolding protein D × 24 Major Spike Protein G × 6 （P31281） Scaffolding Protein B × 6	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 7	Scaffolding protein D × 4 Major Spike Protein G × 1 （P31281） Scaffolding Protein B × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VGF_BPAL3
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain F； PDBConstruct 1–431； UniProt 1–431

Major Spike Protein G

Enterobacteria phage alpha3

UniProt P31281

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 420	Scaffolding protein D × 240 Capsid Protein F × 60 （P08767） Scaffolding Protein B × 60	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 7	Scaffolding protein D × 4 Capsid Protein F × 1 （P08767） Scaffolding Protein B × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 35	Scaffolding protein D × 20 Capsid Protein F × 5 （P08767） Scaffolding Protein B × 5	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 42	Scaffolding protein D × 24 Capsid Protein F × 6 （P08767） Scaffolding Protein B × 6	Consistent with protein count
5	Protein heterocomplex	Heteromer	Protein 7	Scaffolding protein D × 4 Capsid Protein F × 1 （P08767） Scaffolding Protein B × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VGG_BPAL3
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 1–187； UniProt 1–187

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	1m0f
Deposition date deposition_date	2002-06-12
Structure title title	Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy
Keywords keywords	Bacteriophage, Cryo Electron Microscopy, Procapsid, morphogenesis, microviridae, assembly, Icosahedral virus, Virus; VIRUS
Experimental Method method	ELECTRON MICROSCOPY

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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.

1m0f__assembly_1__model_1

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

Download this curve (.dat)

1m0f__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1m0f__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)	142.20 Å
Total Rg	142.20 Å
Atom count	0
Residues	0
Excluded volume	9682300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1m0f__assembly_1__model_1`	420-MERIC （420）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1m0f__assembly_2__model_1`	heptameric （7）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`1m0f__assembly_3__model_1`	35-meric （35）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`1m0f__assembly_4__model_1`	42-meric （42）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`1m0f__assembly_5__model_1`	heptameric （7）	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 (4)

Entity 1 Entity 1 polymer

Description description	Scaffolding protein D
Molecular weight formula_weight	16953.3 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1,2,3,4
Atom count atom_count	1179

MSQVTEQSVRFQTALASIKLIQASAVLDLTEDDFDFLTSNKVWIATDRSRARRCVEACVYGTLDFVGYPRFPAPVEFIAAVIAYYVHPVNIQTACLIMEGAEFTENIINGVERPVKAAELFAFTLRVRAGNTDVLTDAEENVRQKLRAEGVM

Source Source

Source organism organism	Enterobacteria phage alpha3
NCBI taxonomy ID ncbi_taxonomy_id	10849
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Capsid Protein F
Molecular weight formula_weight	49294.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

MSNVQTSAEREIVDLSHLAFDCGMLGRLKTVSWTPVIAGDSFELDAVGALRLSPLRRGLAIDSKVDFFTFYIPHRHVYGDQWIQFMRDGVNAQPLPSVTCNRYPDHAGYVGTIVPANNRIPKFLHQSYLNIYNNYFRAPWMPERTEANPSNLNEDDARYGFRCCHLKNIWSAPLPPETKLAEEMGIESNSIDIMGLQAAYAQLHTEQERTYFMQRYRDVISSFGGSTSYDADNRPLLVMHTDFWASGYDVDGTDQSSLGQFSGRVQQTFKHSVPRFFVPEHGVMMTLALIRFPPISPLEHHYLAGKSQLTYTDLAGDPALIGNLPPREISYRDLFRDGRSGIKIKVAESIWYRTHPDYVNFKYHDLHGFPFLDDAPGTSTGDNLQEAILVRHQDYDACFQSQQLLQWNKQARYNVSVYRHMPTVRDSIMTS

Source Source

Source organism organism	Enterobacteria phage alpha3
NCBI taxonomy ID ncbi_taxonomy_id	10849
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Major Spike Protein G
Molecular weight formula_weight	19599.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

MYQNFVTKHDTAIQTSRFSVTGNVIPAAPTGNIPVINGGSITAERAVVNLYANMNVSTSSDGSFIVAMKVDTSPTDPNCVISAGVNLSFAGTSYPIVGIVRFESASEQPTSIAGSEVEHYPIEMSVGSGGVCSARDCATVDIHPRTSGNNVFVGVICSSAKWTSGRVIGTIATTQVIHEYQVLQPLK

Source Source

Source organism organism	Enterobacteria phage alpha3
NCBI taxonomy ID ncbi_taxonomy_id	10849
Host organism host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Scaffolding Protein B
Molecular weight formula_weight	8150.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MEQLTKNQRKKRDEIEAGKSYCSRRFGGATCDDKSAQIYARFDKNDWRIQPAEFYRFHDAEVNTFGYF

Source Source

Source organism organism	Enterobacteria phage alpha3
NCBI taxonomy ID ncbi_taxonomy_id	10849
Host organism host_organism	Escherichia coli

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6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

Domain ID domain_id	d1m0f1_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1m0f2_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1m0f3_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1m0f4_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1m0fb_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1m0ff_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1m0fg_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	16.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	16.00 Å
Resolution测定Method resolution_method	Model based polar fourier transform (Projection matching).
颗粒数 num_particles	2378

Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy

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

Capsid Protein F

State in the Current Structure

Other States of the Same Protein in the Database

Major Spike Protein G

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

1m0f__assembly_1__model_1

1m0f__assembly_1__model_1 | I(q)

1m0f__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

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

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

7. Citations (1)

Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy

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

Capsid Protein F

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Major Spike Protein G

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

1m0f__assembly_1__model_1

1m0f__assembly_1__model_1 | I(q)

1m0f__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

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

6. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

7. Citations (1)