8ean

Cryo-EM structure of in-situ tailspike in bacteriophage P22

Method: ELECTRON MICROSCOPY Dmax: 163.9 Å Quality: REASONABLE

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

Tail spike protein

OrganismNot specified

UniProt P12528

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain 0; UniProt 6–667 Chain Y; UniProt 6–667 Chain Z; UniProt 6–667 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

28 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBER_BPP22
Isoform
PDB entities 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–662; UniProt 6–667 Author chain Y; PDBConstruct 1–662; UniProt 6–667 Author chain Z; PDBConstruct 1–662; UniProt 6–667

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 8ean

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ean
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ean
Deposition date deposition_date2022-08-29
Structure title titleCryo-EM structure of in-situ tailspike in bacteriophage P22
Keywords keywordsBacteriophage P22, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.64
Radius of gyration Rg (electron density) rg_electron44.44
Forward intensity I(0) i0688224000.00
Molecular weight molecular_weight213850.0 kDa
Excluded volume excluded_volume267070 ų
Envelope volume envelope_volume335060 ų
Hydration-shell volume shell_volume66953 ų
Envelope diameter envelope_diameter171.8
Shell Rg shell_rg44.81
Envelope Rg envelope_rg45.13
Shape Rg shape_rg44.43
Total Rg total_rg44.49
Total atoms total_atoms15075
Residues n_residues1986
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 dmax163.9
Rg (real space) rg_real44.18
Rg uncertainty (real space) rg_real_error1.91
I(0) (real space) i0_real6.8820e+08
I(0) uncertainty (real space) i0_real_error1.3960e+07
Rg (reciprocal space) rg_reciprocal43.64
I(0) (reciprocal space) i0_reciprocal687800000.0000
Solution quality estimate total_estimate0.5444
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.5
Skewness Skewness skewness0.789
Kurtosis Kurtosis kurtosis0.503
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha144300000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.522; Stabil: 1.000; Sysdev: 0.032; Positv: 1.000; Valcen: 0.763; Smooth: 0.647

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8eanZ01
Class class2 — Mainly Beta
Architecture architecture170 — Beta Complex
Topology topology14 — Tailspike Protein; Chain
Homologous superfamily homologous superfamily10 — Phage P22 tailspike-like, N-terminal domain

8. Citations (1)

9. Files and Curves (10)