9jpr

Local refinement of H11 nanotubes assembled from baculovirus capsid protein

Method: ELECTRON MICROSCOPY Dmax: 201.5 Å Quality: GOOD

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

Glutathione S-transferase class-mu 26 kDa isozyme,Viral capsid 39 protein

Helicoverpa armigera nucleopolyhedrovirus

UniProt P08515

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–218 Chain B; UniProt 1–218 Chain C; UniProt 1–218 Chain D; UniProt 1–218 Chain E; UniProt 1–218 Chain F; UniProt 1–218 Chain G; UniProt 1–218 Chain H; UniProt 1–218 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

64 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GST26_SCHJA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–218; UniProt 1–218 Author chain B; PDBConstruct 1–218; UniProt 1–218 Author chain C; PDBConstruct 1–218; UniProt 1–218 Author chain D; PDBConstruct 1–218; UniProt 1–218 Author chain E; PDBConstruct 1–218; UniProt 1–218 Author chain F; PDBConstruct 1–218; UniProt 1–218 Author chain G; PDBConstruct 1–218; UniProt 1–218 Author chain H; PDBConstruct 1–218; UniProt 1–218

Glutathione S-transferase class-mu 26 kDa isozyme,Viral capsid 39 protein

Helicoverpa armigera nucleopolyhedrovirus

UniProt Q77K63

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–293 Chain B; UniProt 1–293 Chain C; UniProt 1–293 Chain D; UniProt 1–293 Chain E; UniProt 1–293 Chain F; UniProt 1–293 Chain G; UniProt 1–293 Chain H; UniProt 1–293 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q77K63_9ABAC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 237–529; UniProt 1–293 Author chain B; PDBConstruct 237–529; UniProt 1–293 Author chain C; PDBConstruct 237–529; UniProt 1–293 Author chain D; PDBConstruct 237–529; UniProt 1–293 Author chain E; PDBConstruct 237–529; UniProt 1–293 Author chain F; PDBConstruct 237–529; UniProt 1–293 Author chain G; PDBConstruct 237–529; UniProt 1–293 Author chain H; PDBConstruct 237–529; UniProt 1–293

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9jpr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jpr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jpr
Deposition date deposition_date2024-09-26
Structure title titleLocal refinement of H11 nanotubes assembled from baculovirus capsid protein
Keywords keywordscapsid protein, self-assembly, Baculovirus, nanotube, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.95
Radius of gyration Rg (electron density) rg_electron56.15
Forward intensity I(0) i0875808000.00
Molecular weight molecular_weight247670.0 kDa
Excluded volume excluded_volume310360 ų
Envelope volume envelope_volume476330 ų
Hydration-shell volume shell_volume73730 ų
Envelope diameter envelope_diameter194.8
Shell Rg shell_rg54.29
Envelope Rg envelope_rg55.53
Shape Rg shape_rg56.14
Total Rg total_rg56.12
Total atoms total_atoms17424
Residues n_residues2160
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax201.5
Rg (real space) rg_real56.17
Rg uncertainty (real space) rg_real_error2.46
I(0) (real space) i0_real8.7580e+08
I(0) uncertainty (real space) i0_real_error1.7500e+07
Rg (reciprocal space) rg_reciprocal55.74
I(0) (reciprocal space) i0_reciprocal875200000.0000
Solution quality estimate total_estimate0.7915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.0
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46000000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.787; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)