8fv5

Representation of 16-mer phiPA3 PhuN Lattice, p2

Method: ELECTRON MICROSCOPY Dmax: 248.1 Å Quality: EXCELLENT

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

Maltose/maltodextrin-binding periplasmic protein, phiPA3 PhuN

Pseudomonas phage PhiPA3

UniProt F8SJT5

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain A; UniProt 1–602 Chain B; UniProt 1–602 Chain C; UniProt 1–602 Chain D; UniProt 1–602 Chain E; UniProt 1–602 Chain F; UniProt 1–602 Chain G; UniProt 1–602 Chain H; UniProt 1–602 Chain I; UniProt 1–602 Chain J; UniProt 1–602 Chain K; UniProt 1–602 Chain L; UniProt 1–602 Chain M; UniProt 1–602 Chain N; UniProt 1–602 Chain O; UniProt 1–602 Chain P; UniProt 1–602 Chain Q; UniProt 1–602 Chain R; UniProt 1–602 Chain S; UniProt 1–602 Chain T; UniProt 1–602 Chain U; UniProt 1–602 Chain V; UniProt 1–602 Chain W; UniProt 1–602 Chain X; UniProt 1–602 Chain Y; UniProt 1–602 Chain Z; UniProt 1–602 Chain a; UniProt 1–602 Chain b; UniProt 1–602 Chain c; UniProt 1–602 Chain d; UniProt 1–602 Chain e; UniProt 1–602 Chain f; UniProt 1–602 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5;0.25 cOmplete Protease Inhibitor Tablet also included cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.21 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 CHMA_BPPA3
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 395–996; UniProt 1–602 Author chain B; PDBConstruct 395–996; UniProt 1–602 Author chain C; PDBConstruct 395–996; UniProt 1–602 Author chain D; PDBConstruct 395–996; UniProt 1–602 Author chain E; PDBConstruct 395–996; UniProt 1–602 Author chain F; PDBConstruct 395–996; UniProt 1–602 Author chain G; PDBConstruct 395–996; UniProt 1–602 Author chain H; PDBConstruct 395–996; UniProt 1–602 Author chain I; PDBConstruct 395–996; UniProt 1–602 Author chain J; PDBConstruct 395–996; UniProt 1–602 Author chain K; PDBConstruct 395–996; UniProt 1–602 Author chain L; PDBConstruct 395–996; UniProt 1–602 Author chain M; PDBConstruct 395–996; UniProt 1–602 Author chain N; PDBConstruct 395–996; UniProt 1–602 Author chain O; PDBConstruct 395–996; UniProt 1–602 Author chain P; PDBConstruct 395–996; UniProt 1–602 Author chain Q; PDBConstruct 395–996; UniProt 1–602 Author chain R; PDBConstruct 395–996; UniProt 1–602 Author chain S; PDBConstruct 395–996; UniProt 1–602 Author chain T; PDBConstruct 395–996; UniProt 1–602 Author chain U; PDBConstruct 395–996; UniProt 1–602 Author chain V; PDBConstruct 395–996; UniProt 1–602 Author chain W; PDBConstruct 395–996; UniProt 1–602 Author chain X; PDBConstruct 395–996; UniProt 1–602 Author chain Y; PDBConstruct 395–996; UniProt 1–602 Author chain Z; PDBConstruct 395–996; UniProt 1–602 Author chain a; PDBConstruct 395–996; UniProt 1–602 Author chain b; PDBConstruct 395–996; UniProt 1–602 Author chain c; PDBConstruct 395–996; UniProt 1–602 Author chain d; PDBConstruct 395–996; UniProt 1–602 Author chain e; PDBConstruct 395–996; UniProt 1–602 Author chain f; PDBConstruct 395–996; UniProt 1–602

Maltose/maltodextrin-binding periplasmic protein, phiPA3 PhuN

Pseudomonas phage PhiPA3

UniProt P0AEX9

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain A; UniProt 27–392 Chain B; UniProt 27–392 Chain C; UniProt 27–392 Chain D; UniProt 27–392 Chain E; UniProt 27–392 Chain F; UniProt 27–392 Chain G; UniProt 27–392 Chain H; UniProt 27–392 Chain I; UniProt 27–392 Chain J; UniProt 27–392 Chain K; UniProt 27–392 Chain L; UniProt 27–392 Chain M; UniProt 27–392 Chain N; UniProt 27–392 Chain O; UniProt 27–392 Chain P; UniProt 27–392 Chain Q; UniProt 27–392 Chain R; UniProt 27–392 Chain S; UniProt 27–392 Chain T; UniProt 27–392 Chain U; UniProt 27–392 Chain V; UniProt 27–392 Chain W; UniProt 27–392 Chain X; UniProt 27–392 Chain Y; UniProt 27–392 Chain Z; UniProt 27–392 Chain a; UniProt 27–392 Chain b; UniProt 27–392 Chain c; UniProt 27–392 Chain d; UniProt 27–392 Chain e; UniProt 27–392 Chain f; UniProt 27–392 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 6.5;0.25 cOmplete Protease Inhibitor Tablet also included cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.21 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–373; UniProt 27–392 Author chain B; PDBConstruct 8–373; UniProt 27–392 Author chain C; PDBConstruct 8–373; UniProt 27–392 Author chain D; PDBConstruct 8–373; UniProt 27–392 Author chain E; PDBConstruct 8–373; UniProt 27–392 Author chain F; PDBConstruct 8–373; UniProt 27–392 Author chain G; PDBConstruct 8–373; UniProt 27–392 Author chain H; PDBConstruct 8–373; UniProt 27–392 Author chain I; PDBConstruct 8–373; UniProt 27–392 Author chain J; PDBConstruct 8–373; UniProt 27–392 Author chain K; PDBConstruct 8–373; UniProt 27–392 Author chain L; PDBConstruct 8–373; UniProt 27–392 Author chain M; PDBConstruct 8–373; UniProt 27–392 Author chain N; PDBConstruct 8–373; UniProt 27–392 Author chain O; PDBConstruct 8–373; UniProt 27–392 Author chain P; PDBConstruct 8–373; UniProt 27–392 Author chain Q; PDBConstruct 8–373; UniProt 27–392 Author chain R; PDBConstruct 8–373; UniProt 27–392 Author chain S; PDBConstruct 8–373; UniProt 27–392 Author chain T; PDBConstruct 8–373; UniProt 27–392 Author chain U; PDBConstruct 8–373; UniProt 27–392 Author chain V; PDBConstruct 8–373; UniProt 27–392 Author chain W; PDBConstruct 8–373; UniProt 27–392 Author chain X; PDBConstruct 8–373; UniProt 27–392 Author chain Y; PDBConstruct 8–373; UniProt 27–392 Author chain Z; PDBConstruct 8–373; UniProt 27–392 Author chain a; PDBConstruct 8–373; UniProt 27–392 Author chain b; PDBConstruct 8–373; UniProt 27–392 Author chain c; PDBConstruct 8–373; UniProt 27–392 Author chain d; PDBConstruct 8–373; UniProt 27–392 Author chain e; PDBConstruct 8–373; UniProt 27–392 Author chain f; PDBConstruct 8–373; UniProt 27–392

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 8fv5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fv5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fv5
Deposition date deposition_date2023-01-18
Structure title titleRepresentation of 16-mer phiPA3 PhuN Lattice, p2
Keywords keywordsphiPA3 protein, shell protein, PhuN, phage nucleus, 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_electron100.30
Forward intensity I(0) i012868400000.00
Molecular weight molecular_weight957710.0 kDa
Excluded volume excluded_volume1194700 ų
Envelope volume envelope_volume2106300 ų
Hydration-shell volume shell_volume177470 ų
Envelope diameter envelope_diameter342.3
Shell Rg shell_rg86.11
Envelope Rg envelope_rg96.54
Shape Rg shape_rg100.30
Total Rg total_rg100.20
Total atoms total_atoms134032
Residues n_residues8592
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 dmax248.1
Rg (real space) rg_real95.69
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.2300e+10
I(0) uncertainty (real space) i0_real_error2.1240e+08
Rg (reciprocal space) rg_reciprocal98.35
I(0) (reciprocal space) i0_reciprocal12790000000.0000
Solution quality estimate total_estimate0.9102
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary132.3
Skewness Skewness skewness0.058
Kurtosis Kurtosis kurtosis-0.891
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.6867
Highest regularization parameter α highest_alpha335800000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.990; Stabil: 0.958; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; 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)