5gai

Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins

Method: ELECTRON MICROSCOPY Dmax: 278.3 Å Quality: GOOD

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

Portal protein

Enterobacteria phage P22

UniProt P26744

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain A; UniProt 5–725 Chain B; UniProt 5–725 Chain C; UniProt 5–725 Chain D; UniProt 5–725 Chain E; UniProt 5–725 Chain F; UniProt 5–725 Chain G; UniProt 5–725 Chain H; UniProt 5–725 Chain I; UniProt 5–725 Chain J; UniProt 5–725 Chain W; UniProt 5–725 Chain X; UniProt 5–725 Not recorded Peptidoglycan hydrolase gp4 × 12 (P26746) Tail fiber protein × 3 (P12528) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 2 seconds before plunging. Resolution 10.50 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.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PORTL_BPP22
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–717; UniProt 5–725 Author chain B; PDBConstruct 1–717; UniProt 5–725 Author chain C; PDBConstruct 1–717; UniProt 5–725 Author chain D; PDBConstruct 1–717; UniProt 5–725 Author chain E; PDBConstruct 1–717; UniProt 5–725 Author chain F; PDBConstruct 1–717; UniProt 5–725 Author chain G; PDBConstruct 1–717; UniProt 5–725 Author chain H; PDBConstruct 1–717; UniProt 5–725 Author chain I; PDBConstruct 1–717; UniProt 5–725 Author chain J; PDBConstruct 1–717; UniProt 5–725 Author chain W; PDBConstruct 1–717; UniProt 5–725 Author chain X; PDBConstruct 1–717; UniProt 5–725

Peptidoglycan hydrolase gp4

Enterobacteria phage P22

UniProt P26746

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain K; UniProt 5–150 Chain L; UniProt 5–150 Chain M; UniProt 5–150 Chain N; UniProt 5–150 Chain O; UniProt 5–150 Chain P; UniProt 5–150 Chain Q; UniProt 5–150 Chain R; UniProt 5–150 Chain S; UniProt 5–150 Chain T; UniProt 5–150 Chain U; UniProt 5–150 Chain V; UniProt 5–150 Mutation:P150A Portal protein × 12 (P26744) Tail fiber protein × 3 (P12528) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 2 seconds before plunging. Resolution 10.50 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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXLYS_BPP22
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–146; UniProt 5–150 Author chain L; PDBConstruct 1–146; UniProt 5–150 Author chain M; PDBConstruct 1–146; UniProt 5–150 Author chain N; PDBConstruct 1–146; UniProt 5–150 Author chain O; PDBConstruct 1–146; UniProt 5–150 Author chain P; PDBConstruct 1–146; UniProt 5–150 Author chain Q; PDBConstruct 1–146; UniProt 5–150 Author chain R; PDBConstruct 1–146; UniProt 5–150 Author chain S; PDBConstruct 1–146; UniProt 5–150 Author chain T; PDBConstruct 1–146; UniProt 5–150 Author chain U; PDBConstruct 1–146; UniProt 5–150 Author chain V; PDBConstruct 1–146; UniProt 5–150

Tail fiber protein

Enterobacteria phage P22

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 heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain 0; UniProt 6–667 Chain Y; UniProt 6–667 Chain Z; UniProt 6–667 Not recorded Portal protein × 12 (P26744) Peptidoglycan hydrolase gp4 × 12 (P26746) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Blot for 2 seconds before plunging. Resolution 10.50 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 3
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 5gai

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5gai
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5gai
Deposition date deposition_date2015-12-01
Structure title titleProbabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins
Keywords keywordsvirion, portal, tailspike, adhesin, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron103.20
Forward intensity I(0) i027937100000.00
Molecular weight molecular_weight1392400.0 kDa
Excluded volume excluded_volume1728200 ų
Envelope volume envelope_volume2604400 ų
Hydration-shell volume shell_volume245940 ų
Envelope diameter envelope_diameter477.2
Shell Rg shell_rg82.32
Envelope Rg envelope_rg103.90
Shape Rg shape_rg103.10
Total Rg total_rg103.20
Total atoms total_atoms98043
Residues n_residues12390
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 dmax278.3
Rg (real space) rg_real93.01
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real2.6650e+10
I(0) uncertainty (real space) i0_real_error5.3560e+08
Rg (reciprocal space) rg_reciprocal91.04
I(0) (reciprocal space) i0_reciprocal27120000000.0000
Solution quality estimate total_estimate0.8848
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.8
Skewness Skewness skewness0.532
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.6142
Highest regularization parameter α highest_alpha739500000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.018; Oscil: 0.860; Stabil: 0.971; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.042

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)