5kp9

Structure of Nanoparticle Released from Enveloped Protein Nanoparticle

Method: ELECTRON MICROSCOPY Dmax: 52.2 Å Quality: GOOD

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

EPN-01*

Human immunodeficiency virus type 1 group M subtype B (isolate BH10)

UniProt P03347

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 × 60 PDB declaration: 60-meric(60) Consistent with protein copy count Chain B; UniProt 461–512 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 461–512 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
3 Insufficient information Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 461–512 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
4 Insufficient information Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 461–512 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
5 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 461–512 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 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 GAG_HV1B1
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 231–282; UniProt 461–512

EPN-01*

Human immunodeficiency virus type 1 group M subtype B (isolate BH10)

UniProt Q9WXS1

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 × 60 PDB declaration: 60-meric(60) Consistent with protein copy count Chain B; UniProt 2–205 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–205 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
3 Insufficient information Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 2–205 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
4 Insufficient information Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 2–205 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 Å
5 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–205 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Phosphate-buffered saline cryo-EM vitrification conditions:Cryogen ETHANE;11 second blot, 0 mm offset Resolution 5.70 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.

16 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9WXS1_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 19–222; UniProt 2–205

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 5kp9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5kp9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5kp9
Deposition date deposition_date2016-07-02
Structure title titleStructure of Nanoparticle Released from Enveloped Protein Nanoparticle
Keywords keywords;protein design, icosahedral assemblies, cell transduction, enveloped viruses, virus assembly, enveloped protein, nanoparticle, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier17.26
Radius of gyration Rg (electron density) rg_electron16.07
Forward intensity I(0) i07540430.00
Molecular weight molecular_weight21598.0 kDa
Excluded volume excluded_volume27705 ų
Envelope volume envelope_volume30708 ų
Hydration-shell volume shell_volume15893 ų
Envelope diameter envelope_diameter51.7
Shell Rg shell_rg22.21
Envelope Rg envelope_rg16.30
Shape Rg shape_rg16.03
Total Rg total_rg17.28
Total atoms total_atoms1518
Residues n_residues202
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 dmax52.2
Rg (real space) rg_real17.14
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real7.5400e+06
I(0) uncertainty (real space) i0_real_error7.3800e+04
Rg (reciprocal space) rg_reciprocal17.15
I(0) (reciprocal space) i0_reciprocal7540000.0000
Solution quality estimate total_estimate0.8986
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2407000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)