9yin

Sf11 bacteriophage portal

Method: ELECTRON MICROSCOPY Dmax: 111.4 Å Quality: REASONABLE

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

Sf11 portal

Shigella phage Sf11 SMD-2017

UniProt A0A291AXK9

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–470 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–470 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 Å
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–470 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.40 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A291AXK9_9CAUD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–470; UniProt 1–470

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 9yin

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yin
Deposition date deposition_date2025-10-01
Structure title titleSf11 bacteriophage portal
Keywords keywordsSf11, bacteriophage, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.61
Radius of gyration Rg (electron density) rg_electron30.53
Forward intensity I(0) i031128200.00
Molecular weight molecular_weight42112.0 kDa
Excluded volume excluded_volume52272 ų
Envelope volume envelope_volume76959 ų
Hydration-shell volume shell_volume23592 ų
Envelope diameter envelope_diameter109.2
Shell Rg shell_rg33.00
Envelope Rg envelope_rg32.09
Shape Rg shape_rg30.49
Total Rg total_rg30.93
Total atoms total_atoms2964
Residues n_residues382
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 dmax111.4
Rg (real space) rg_real32.40
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real3.1340e+07
I(0) uncertainty (real space) i0_real_error4.4630e+05
Rg (reciprocal space) rg_reciprocal30.91
I(0) (reciprocal space) i0_reciprocal31120000.0000
Solution quality estimate total_estimate0.5889
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.668
Kurtosis Kurtosis kurtosis-0.216
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha3.1860
Highest regularization parameter α highest_alpha2959000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.629; Stabil: 0.889; Sysdev: 0.000; Positv: 1.000; Valcen: 0.436; Smooth: 0.685

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)