9bgm

Pseudomonas phage DEV neck and tail (portal, head-to-tail and tail tube proteins)

Method: ELECTRON MICROSCOPY Dmax: 263.4 Å Quality: EXCELLENT

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

gp75 tail tube

OrganismNot specified

UniProt A0A2K8I3N9

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain A; UniProt 1–321 Chain D; UniProt 1–321 Chain G; UniProt 1–321 Chain J; UniProt 1–321 Chain M; UniProt 1–321 Chain P; UniProt 1–321 Chain S; UniProt 1–321 Chain W; UniProt 1–321 Chain Z; UniProt 1–321 Chain a; UniProt 1–321 Chain f; UniProt 1–321 Chain i; UniProt 1–321 Not recorded gp83 head-to-tail × 12 (A0A2K8I0C0) gp80 portal protein × 12 (A0A2K8IC08) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 A0A2K8I3N9_9CAUD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–321; UniProt 1–321 Author chain D; PDBConstruct 1–321; UniProt 1–321 Author chain G; PDBConstruct 1–321; UniProt 1–321 Author chain J; PDBConstruct 1–321; UniProt 1–321 Author chain M; PDBConstruct 1–321; UniProt 1–321 Author chain P; PDBConstruct 1–321; UniProt 1–321 Author chain S; PDBConstruct 1–321; UniProt 1–321 Author chain W; PDBConstruct 1–321; UniProt 1–321 Author chain Z; PDBConstruct 1–321; UniProt 1–321 Author chain a; PDBConstruct 1–321; UniProt 1–321 Author chain f; PDBConstruct 1–321; UniProt 1–321 Author chain i; PDBConstruct 1–321; UniProt 1–321

gp83 head-to-tail

OrganismNot specified

UniProt A0A2K8I0C0

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain B; UniProt 1–244 Chain E; UniProt 1–244 Chain H; UniProt 1–244 Chain K; UniProt 1–244 Chain N; UniProt 1–244 Chain Q; UniProt 1–244 Chain T; UniProt 1–244 Chain X; UniProt 1–244 Chain b; UniProt 1–244 Chain d; UniProt 1–244 Chain g; UniProt 1–244 Chain j; UniProt 1–244 Not recorded gp75 tail tube × 12 (A0A2K8I3N9) gp80 portal protein × 12 (A0A2K8IC08) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2K8I0C0_9CAUD
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–244; UniProt 1–244 Author chain E; PDBConstruct 1–244; UniProt 1–244 Author chain H; PDBConstruct 1–244; UniProt 1–244 Author chain K; PDBConstruct 1–244; UniProt 1–244 Author chain N; PDBConstruct 1–244; UniProt 1–244 Author chain Q; PDBConstruct 1–244; UniProt 1–244 Author chain T; PDBConstruct 1–244; UniProt 1–244 Author chain X; PDBConstruct 1–244; UniProt 1–244 Author chain b; PDBConstruct 1–244; UniProt 1–244 Author chain d; PDBConstruct 1–244; UniProt 1–244 Author chain g; PDBConstruct 1–244; UniProt 1–244 Author chain j; PDBConstruct 1–244; UniProt 1–244

gp80 portal protein

OrganismNot specified

UniProt A0A2K8IC08

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain C; UniProt 1–726 Chain F; UniProt 1–726 Chain I; UniProt 1–726 Chain L; UniProt 1–726 Chain O; UniProt 1–726 Chain R; UniProt 1–726 Chain V; UniProt 1–726 Chain Y; UniProt 1–726 Chain c; UniProt 1–726 Chain e; UniProt 1–726 Chain h; UniProt 1–726 Chain k; UniProt 1–726 Not recorded gp75 tail tube × 12 (A0A2K8I3N9) gp83 head-to-tail × 12 (A0A2K8I0C0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2K8IC08_9CAUD
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–726; UniProt 1–726 Author chain F; PDBConstruct 1–726; UniProt 1–726 Author chain I; PDBConstruct 1–726; UniProt 1–726 Author chain L; PDBConstruct 1–726; UniProt 1–726 Author chain O; PDBConstruct 1–726; UniProt 1–726 Author chain R; PDBConstruct 1–726; UniProt 1–726 Author chain V; PDBConstruct 1–726; UniProt 1–726 Author chain Y; PDBConstruct 1–726; UniProt 1–726 Author chain c; PDBConstruct 1–726; UniProt 1–726 Author chain e; PDBConstruct 1–726; UniProt 1–726 Author chain h; PDBConstruct 1–726; UniProt 1–726 Author chain k; PDBConstruct 1–726; UniProt 1–726

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 9bgm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bgm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9bgm
Deposition date deposition_date2024-04-19
Structure title titlePseudomonas phage DEV neck and tail (portal, head-to-tail and tail tube proteins)
Keywords keywordsportal, tail hub, tail tube, complex, STRUCTURAL PROTEIN, gp75, gp83, gp80, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier91.60
Radius of gyration Rg (electron density) rg_electron92.21
Forward intensity I(0) i030283800000.00
Molecular weight molecular_weight1457100.0 kDa
Excluded volume excluded_volume1813500 ų
Envelope volume envelope_volume2989300 ų
Hydration-shell volume shell_volume285720 ų
Envelope diameter envelope_diameter442.8
Shell Rg shell_rg88.19
Envelope Rg envelope_rg91.67
Shape Rg shape_rg92.25
Total Rg total_rg92.07
Total atoms total_atoms102504
Residues n_residues13212
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 dmax263.4
Rg (real space) rg_real85.41
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.8890e+10
I(0) uncertainty (real space) i0_real_error5.6330e+08
Rg (reciprocal space) rg_reciprocal87.56
I(0) (reciprocal space) i0_reciprocal29920000000.0000
Solution quality estimate total_estimate0.9077
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary108.4
Skewness Skewness skewness0.502
Kurtosis Kurtosis kurtosis0.031
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha0.6235
Highest regularization parameter α highest_alpha2048000000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.020; Oscil: 0.886; Stabil: 0.986; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.248

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)