3jbf

Complex of poliovirus with VHH PVSP19B

Method: ELECTRON MICROSCOPY Dmax: 103.0 Å Quality: EXCELLENT

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

Capsid protein VP1

OrganismNot specified

UniProt P03300

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 × 300 PDB declaration: 300-meric(300) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–578 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-578 Fragment:UNP residues 2-69 Non-standard monomer:Yes (specific site not provided by mmCIF) nanobody VHH PVSP19B × 60 PLM PALMITIC ACID × 60 ELECTRON MICROSCOPY cryo-EM buffer:145 mM NaCl, 50 mM Na2HPO4.12H2O;pH 7.4;145 mM NaCl, 50 mM Na2HPO4.12H2O cryo-EM vitrification conditions:4 second blot;154 K;Cryogen ETHANE;Blotted for 4 seconds before plunging into liquid ethane (homemade plunger). Resolution 4.60 Å
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–578 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-578 Fragment:UNP residues 2-69 Non-standard monomer:Yes (specific site not provided by mmCIF) nanobody VHH PVSP19B × 1 PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:145 mM NaCl, 50 mM Na2HPO4.12H2O;pH 7.4;145 mM NaCl, 50 mM Na2HPO4.12H2O cryo-EM vitrification conditions:4 second blot;154 K;Cryogen ETHANE;Blotted for 4 seconds before plunging into liquid ethane (homemade plunger). Resolution 4.60 Å
3 Protein heterocomplex Heteromer Protein × 25 PDB declaration: 25-meric(25) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–578 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-578 Fragment:UNP residues 2-69 Non-standard monomer:Yes (specific site not provided by mmCIF) nanobody VHH PVSP19B × 5 PLM PALMITIC ACID × 5 ELECTRON MICROSCOPY cryo-EM buffer:145 mM NaCl, 50 mM Na2HPO4.12H2O;pH 7.4;145 mM NaCl, 50 mM Na2HPO4.12H2O cryo-EM vitrification conditions:4 second blot;154 K;Cryogen ETHANE;Blotted for 4 seconds before plunging into liquid ethane (homemade plunger). Resolution 4.60 Å
4 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–578 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-578 Fragment:UNP residues 2-69 Non-standard monomer:Yes (specific site not provided by mmCIF) nanobody VHH PVSP19B × 6 PLM PALMITIC ACID × 6 ELECTRON MICROSCOPY cryo-EM buffer:145 mM NaCl, 50 mM Na2HPO4.12H2O;pH 7.4;145 mM NaCl, 50 mM Na2HPO4.12H2O cryo-EM vitrification conditions:4 second blot;154 K;Cryogen ETHANE;Blotted for 4 seconds before plunging into liquid ethane (homemade plunger). Resolution 4.60 Å
5 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain 1; UniProt 580–881 Chain 2; UniProt 70–341 Chain 3; UniProt 342–578 Chain 4; UniProt 2–69 Fragment:UNP residues 580-881 Fragment:UNP residues 70-341 Fragment:UNP residues 342-578 Fragment:UNP residues 2-69 Non-standard monomer:Yes (specific site not provided by mmCIF) nanobody VHH PVSP19B × 1 PLM PALMITIC ACID × 1 ELECTRON MICROSCOPY cryo-EM buffer:145 mM NaCl, 50 mM Na2HPO4.12H2O;pH 7.4;145 mM NaCl, 50 mM Na2HPO4.12H2O cryo-EM vitrification conditions:4 second blot;154 K;Cryogen ETHANE;Blotted for 4 seconds before plunging into liquid ethane (homemade plunger). Resolution 4.60 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.

80 other PDB entries and 246 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POLG_POL1M
Isoform
PDB entities 1, 2, 3, 4
Chains and sequence ranges Author chain 1; PDBConstruct 1–302; UniProt 580–881 Author chain 2; PDBConstruct 1–272; UniProt 70–341 Author chain 3; PDBConstruct 1–237; UniProt 342–578 Author chain 4; PDBConstruct 2–69; UniProt 2–69

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 3jbf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jbf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3jbf
Deposition date deposition_date2015-08-26
Structure title titleComplex of poliovirus with VHH PVSP19B
Keywords keywordspoliovirus, nanobodies, VHH, neutralizing antibodies, VIRUS-IMMUNE SYSTEM complex; VIRUS/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.22
Radius of gyration Rg (electron density) rg_electron31.11
Forward intensity I(0) i0187154000.00
Molecular weight molecular_weight108400.0 kDa
Excluded volume excluded_volume135290 ų
Envelope volume envelope_volume173370 ų
Hydration-shell volume shell_volume45425 ų
Envelope diameter envelope_diameter108.8
Shell Rg shell_rg38.98
Envelope Rg envelope_rg31.50
Shape Rg shape_rg31.10
Total Rg total_rg31.82
Total atoms total_atoms7630
Residues n_residues976
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 dmax103.0
Rg (real space) rg_real32.07
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.8720e+08
I(0) uncertainty (real space) i0_real_error2.7890e+06
Rg (reciprocal space) rg_reciprocal32.14
I(0) (reciprocal space) i0_reciprocal187200000.0000
Solution quality estimate total_estimate0.9006
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.9
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29260000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)