SAXSdb — 8i1v

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

Major capsid protein

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein copy count	Chain A； UniProt 1–430 Chain B； UniProt 1–430 Chain C； UniProt 1–430 Chain D； UniProt 1–430 Chain E； UniProt 1–430 Chain F； UniProt 1–430 Chain G； UniProt 1–430	Not recorded	Scaffolding protein × 7 （P26748）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.60 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 8I1V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2M5S High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein Deposited 2013-03-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 223–345（123 aa） Fragment：;This domain has previously been called the 'extra-density domain' and 'telokin-like domain' in the literature based on cryo-EM models ;	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；310.15 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.5 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, 1% H2O/99% D2O \| 1% H2O/99% D2O	Resolution not provided
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 360 PDB declaration: 360-MERIC	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 30 PDB declaration: 30-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 36 PDB declaration: 36-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 420 PDB declaration: 420-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 42 PDB declaration: 42-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 420 PDB declaration: 420-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 42 PDB declaration: 42-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
8GN5 Designed pH-responsive P22 VLP Deposited 2022-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 4–428（425 aa） Chain B 4–428（425 aa） Chain C 4–428（425 aa） Chain D 4–428（425 aa）	Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.02 Å
8I1T The asymmetric unit of P22 empty capsid Deposited 2023-01-13	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa） Chain H 1–430（430 aa） Chain I 1–430（430 aa） Chain J 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa） Chain H 1–430（430 aa） Chain I 1–430（430 aa） Chain J 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9PGG Cryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom Deposited 2025-07-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric	Chain Aa 1–430（430 aa） Chain Ab 1–430（430 aa） Chain Ac 1–430（430 aa） Chain Ad 1–430（430 aa） Chain Ae 1–430（430 aa） Chain Af 1–430（430 aa） Chain Ag 1–430（430 aa） Chain Ah 1–430（430 aa） Chain Ai 1–430（430 aa） Chain Aj 1–430（430 aa） Chain Ak 1–430（430 aa） Chain Al 1–430（430 aa） Chain Am 1–430（430 aa） Chain An 1–430（430 aa） Chain Ao 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.76 Å

9 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CAPSD_BPP22
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–430； UniProt 1–430 Author chain B； PDBConstruct 1–430； UniProt 1–430 Author chain C； PDBConstruct 1–430； UniProt 1–430 Author chain D； PDBConstruct 1–430； UniProt 1–430 Author chain E； PDBConstruct 1–430； UniProt 1–430 Author chain F； PDBConstruct 1–430； UniProt 1–430 Author chain G； PDBConstruct 1–430； UniProt 1–430

Scaffolding protein

OrganismNot specified

UniProt P26748

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein copy count	Chain H； UniProt 1–303 Chain I； UniProt 1–303 Chain J； UniProt 1–303 Chain K； UniProt 1–303 Chain L； UniProt 1–303 Chain M； UniProt 1–303 Chain N； UniProt 1–303	Not recorded	Major capsid protein × 7 （P26747）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.60 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 8I1V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GP8 NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN Deposited 1999-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 264–303（40 aa） Fragment：C-TERMINAL FUNCTIONAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.4；293 K；Pressure 1 NMR sample composition 10% WATER/90% D2O, 99.9% D2O	Resolution not provided
2GP8 NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN Deposited 1999-05-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 264–303（40 aa） Fragment：C-TERMINAL FUNCTIONAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.4；293 K；Pressure 1 NMR sample composition 10% WATER/90% D2O, 99.9% D2O	Resolution not provided
9KYV The scaffold dimer of phage P22 Deposited 2024-12-09	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–303（303 aa） Chain B 1–303（303 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.90 Å
9KYW The scaffold C-loop of phage P22 Deposited 2024-12-09	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–303（303 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.70 Å
9KYX The scaffold tetramer of phage P22 Deposited 2024-12-09	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–303（303 aa） Chain B 1–303（303 aa） Chain C 1–303（303 aa） Chain D 1–303（303 aa） Chain E 1–303（303 aa） Chain F 1–303（303 aa） Chain G 1–303（303 aa） Chain H 1–303（303 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.90 Å

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VG08_BPP22
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain H； PDBConstruct 1–303； UniProt 1–303 Author chain I； PDBConstruct 1–303； UniProt 1–303 Author chain J； PDBConstruct 1–303； UniProt 1–303 Author chain K； PDBConstruct 1–303； UniProt 1–303 Author chain L； PDBConstruct 1–303； UniProt 1–303 Author chain M； PDBConstruct 1–303； UniProt 1–303 Author chain N； PDBConstruct 1–303； UniProt 1–303

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	8i1v
Deposition date deposition_date	2023-01-13
Structure title title	The asymmetric unit of P22 procapsid
Keywords keywords	Complex, VIRUS, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	52.46 Å
Radius of gyration Rg (electron density) rg_electron	52.06 Å
Forward intensity I(0) i0	1679850000.00
Molecular weight molecular_weight	339610.0 kDa
Excluded volume excluded_volume	424170 Å³
Envelope volume envelope_volume	618480 Å³
Hydration-shell volume shell_volume	96449 Å³
Envelope diameter envelope_diameter	175.9 Å
Shell Rg shell_rg	58.02 Å
Envelope Rg envelope_rg	50.71 Å
Shape Rg shape_rg	52.05 Å
Total Rg total_rg	52.27 Å
Total atoms total_atoms	23870
Residues n_residues	3127
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	175.8 Å
Rg (real space) rg_real	52.35 Å
Rg uncertainty (real space) rg_real_error	1.42 Å
I(0) (real space) i0_real	1.6800e+09
I(0) uncertainty (real space) i0_real_error	3.2090e+07
Rg (reciprocal space) rg_reciprocal	52.54 Å
I(0) (reciprocal space) i0_reciprocal	1680000000.0000
Solution quality estimate total_estimate	0.8900
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	64.5 Å
Skewness Skewness skewness	0.186
Kurtosis Kurtosis kurtosis	-0.566
Angular range angular_range	— – 0.1500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	241900000.0000
Real-space data points n_real_points	31
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.913

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Major capsid protein
Molecular weight formula_weight	46795.6 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,A,B,F,C,D,E
Atom count atom_count	23870

MALNEGQIVTLAVDEIIETISAITPMAQKAKKYTPPAASMQRSSNTIWMPVEQESPTQEGWDLTDKATGLLELNVAVNMGEPDNDFFQLRADDLRDETAYRRRIQSAARKLANNVELKVANMAAEMGSLVITSPDAIGTNTADAWNFVADAEEIMFSRELNRDMGTSYFFNPQDYKKAGYDLTKRDIFGRIPEEAYRDGTIQRQVAGFDDVLRSPKLPVLTKSTATGITVSGAQSFKPVAWQLDNDGNKVNVDNRFATVTLSATTGMKRGDKISFAGVKFLGQMAKNVLAQDATFSVVRVVDGTHVEITPKPVALDDVSLSPEQRAYANVNTSLADAMAVNILNVKDARTNVFWADDAIRIVSQPIPANHELFAGMKTTSFSIPDVGLNGIFATQGDISTLSGLCRIALWYGVNATRPEAIGVGLPGQTA

Entity 2 Entity 2 polymer

Description description	Scaffolding protein
Molecular weight formula_weight	33609.5 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I,J,K,L,M,N

MEPTTEIQATEDLTLSGDHAAASADSLVVDNANDNAGQEEGFEIVLKDDETAPKQDPAKNAEFARRRIERKRQRELEQQMEAVKRGELPESLRVNPDLPPQPDINAYLSEEGLAKYDYDNSRALAAFNAANTEWLMKAQDARSNAVAEQGRKTQEFTQQSAQYVEAARKHYDAAEKLNIPDYQEKEDAFMQLVPPAVGADIMRLFPEKSAALMYHLGANPEKARQLLAMDGQSALIELTRLSERLTLKPRGKQISSAPPADQPITGDVSAANKDAIRKQMDAAASKGDVETYRKLKAKLKGIR

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7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	8i1vB01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	240 —

Domain ID domain_id	8i1vC01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	240 —

Domain ID domain_id	8i1vD01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	240 —

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8. Citations (1)

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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	—

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

Resolution resolution	2.60 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	1329660

fit	/app/data/saxs_computation/i1/8i1v/8i1v.fit
pddf	/app/data/pr_computation/i1/8i1v/8i1v.pr.out
profile	/app/data/saxs_computation/i1/8i1v/8i1v.dat

The asymmetric unit of P22 procapsid

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

Major capsid protein

State in the Current Structure

Other States of the Same Protein in the Database

Scaffolding protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)