9vel

The composite cryo-EM structure of bacteriophage SPO1 capsid

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Gp6.1

OrganismNot specified

UniProt B6V2N7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 1320 Gp29.2 × 240 (B6V2J1) Gp2.7 × 60 (B6V2M7) Gp36.3 × 60 (B6V2H5) Consistent with protein count
2 Protein heterocomplex Heteromer Protein 22 Gp29.2 × 4 (B6V2J1) Gp2.7 × 1 (B6V2M7) Gp36.3 × 1 (B6V2H5) Consistent with protein count
3 Protein heterocomplex Heteromer Protein 110 Gp29.2 × 20 (B6V2J1) Gp2.7 × 5 (B6V2M7) Gp36.3 × 5 (B6V2H5) Consistent with protein count
4 Protein heterocomplex Heteromer Protein 132 Gp29.2 × 24 (B6V2J1) Gp2.7 × 6 (B6V2M7) Gp36.3 × 6 (B6V2H5) Consistent with protein count
5 Protein heterocomplex Heteromer Protein 22 Gp29.2 × 4 (B6V2J1) Gp2.7 × 1 (B6V2M7) Gp36.3 × 1 (B6V2H5) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name B6V2N7_BPSP1
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–468; UniProt 1–468 Author chain B; PDBConstruct 1–468; UniProt 1–468 Author chain C; PDBConstruct 1–468; UniProt 1–468 Author chain D; PDBConstruct 1–468; UniProt 1–468 Author chain E; PDBConstruct 1–468; UniProt 1–468 Author chain F; PDBConstruct 1–468; UniProt 1–468 Author chain G; PDBConstruct 1–468; UniProt 1–468 Author chain H; PDBConstruct 1–468; UniProt 1–468 Author chain I; PDBConstruct 1–468; UniProt 1–468 Author chain J; PDBConstruct 1–468; UniProt 1–468 Author chain K; PDBConstruct 1–468; UniProt 1–468 Author chain L; PDBConstruct 1–468; UniProt 1–468 Author chain M; PDBConstruct 1–468; UniProt 1–468 Author chain N; PDBConstruct 1–468; UniProt 1–468 Author chain O; PDBConstruct 1–468; UniProt 1–468 Author chain P; PDBConstruct 1–468; UniProt 1–468

Gp29.2

OrganismNot specified

UniProt B6V2J1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 1320 Gp6.1 × 960 (B6V2N7) Gp2.7 × 60 (B6V2M7) Gp36.3 × 60 (B6V2H5) Consistent with protein count
2 Protein heterocomplex Heteromer Protein 22 Gp6.1 × 16 (B6V2N7) Gp2.7 × 1 (B6V2M7) Gp36.3 × 1 (B6V2H5) Consistent with protein count
3 Protein heterocomplex Heteromer Protein 110 Gp6.1 × 80 (B6V2N7) Gp2.7 × 5 (B6V2M7) Gp36.3 × 5 (B6V2H5) Consistent with protein count
4 Protein heterocomplex Heteromer Protein 132 Gp6.1 × 96 (B6V2N7) Gp2.7 × 6 (B6V2M7) Gp36.3 × 6 (B6V2H5) Consistent with protein count
5 Protein heterocomplex Heteromer Protein 22 Gp6.1 × 16 (B6V2N7) Gp2.7 × 1 (B6V2M7) Gp36.3 × 1 (B6V2H5) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name B6V2J1_BPSP1
Isoform —
PDB entities 2
Chains and sequence ranges Author chain q; PDBConstruct 1–171; UniProt 1–171 Author chain r; PDBConstruct 1–171; UniProt 1–171 Author chain s; PDBConstruct 1–171; UniProt 1–171 Author chain v; PDBConstruct 1–171; UniProt 1–171

Gp2.7

OrganismNot specified

UniProt B6V2M7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 1320 Gp6.1 × 960 (B6V2N7) Gp29.2 × 240 (B6V2J1) Gp36.3 × 60 (B6V2H5) Consistent with protein count
2 Protein heterocomplex Heteromer Protein 22 Gp6.1 × 16 (B6V2N7) Gp29.2 × 4 (B6V2J1) Gp36.3 × 1 (B6V2H5) Consistent with protein count
3 Protein heterocomplex Heteromer Protein 110 Gp6.1 × 80 (B6V2N7) Gp29.2 × 20 (B6V2J1) Gp36.3 × 5 (B6V2H5) Consistent with protein count
4 Protein heterocomplex Heteromer Protein 132 Gp6.1 × 96 (B6V2N7) Gp29.2 × 24 (B6V2J1) Gp36.3 × 6 (B6V2H5) Consistent with protein count
5 Protein heterocomplex Heteromer Protein 22 Gp6.1 × 16 (B6V2N7) Gp29.2 × 4 (B6V2J1) Gp36.3 × 1 (B6V2H5) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name B6V2M7_BPSP1
Isoform —
PDB entities 3
Chains and sequence ranges Author chain t; PDBConstruct 1–57; UniProt 1–57

Gp36.3

OrganismNot specified

UniProt B6V2H5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 1320 Gp6.1 × 960 (B6V2N7) Gp29.2 × 240 (B6V2J1) Gp2.7 × 60 (B6V2M7) Consistent with protein count
2 Protein heterocomplex Heteromer Protein 22 Gp6.1 × 16 (B6V2N7) Gp29.2 × 4 (B6V2J1) Gp2.7 × 1 (B6V2M7) Consistent with protein count
3 Protein heterocomplex Heteromer Protein 110 Gp6.1 × 80 (B6V2N7) Gp29.2 × 20 (B6V2J1) Gp2.7 × 5 (B6V2M7) Consistent with protein count
4 Protein heterocomplex Heteromer Protein 132 Gp6.1 × 96 (B6V2N7) Gp29.2 × 24 (B6V2J1) Gp2.7 × 6 (B6V2M7) Consistent with protein count
5 Protein heterocomplex Heteromer Protein 22 Gp6.1 × 16 (B6V2N7) Gp29.2 × 4 (B6V2J1) Gp2.7 × 1 (B6V2M7) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name B6V2H5_BPSP1
Isoform —
PDB entities 4
Chains and sequence ranges Author chain w; PDBConstruct 1–96; UniProt 1–96

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_id9vel
Deposition date deposition_date2025-06-09
Structure title titleThe composite cryo-EM structure of bacteriophage SPO1 capsid
Keywords keywordsSPO1, Phage, Capsid, VIRUS; VIRUS
Experimental Method methodELECTRON 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.

9vel__assembly_1__model_1

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

Download this curve (.dat)

9vel__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 1010 1011 1012 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9vel__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)0.00 Å
Rg (electron density)449.30 Å
Total Rg449.30 Å
Atom count3689880
Residues472980
Excluded volume65745000 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9vel__assembly_1__model_1 1320-meric (1320) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 9vel__assembly_2__model_1 22-meric (22) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 9vel__assembly_3__model_1 110-meric (110) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
4 1 9vel__assembly_4__model_1 132-meric (132) Excluded — —
Exclusion reason: Auxiliary symmetry representation; not a complete or representative biological assembly.
5 1 9vel__assembly_5__model_1 22-meric (22) 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)

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7. Citations (1)