9w22

DENV2 non-structural protein 1 (NS1) Dimer

Method: ELECTRON MICROSCOPY Dmax: 108.4 Å Quality: GOOD

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

Non-structural protein 1

dengue virus type 2

UniProt H9M645

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 776–1127 Chain a; UniProt 776–1127 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.12 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.

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

View Construct and Data Evidence
UniProt name H9M645_9FLAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–352; UniProt 776–1127 Author chain a; PDBConstruct 1–352; UniProt 776–1127

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 9w22

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w22
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9w22
Deposition date deposition_date2025-07-26
Structure title titleDENV2 non-structural protein 1 (NS1) Dimer
Keywords keywordsDengue virus; non-structural protein 1; recombinant; dimer, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.88
Radius of gyration Rg (electron density) rg_electron31.48
Forward intensity I(0) i0102013000.00
Molecular weight molecular_weight78776.0 kDa
Excluded volume excluded_volume98025 ų
Envelope volume envelope_volume132660 ų
Hydration-shell volume shell_volume36388 ų
Envelope diameter envelope_diameter112.3
Shell Rg shell_rg37.12
Envelope Rg envelope_rg31.96
Shape Rg shape_rg31.43
Total Rg total_rg32.11
Total atoms total_atoms5532
Residues n_residues692
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 dmax108.4
Rg (real space) rg_real31.95
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real1.0200e+08
I(0) uncertainty (real space) i0_real_error1.7060e+06
Rg (reciprocal space) rg_reciprocal31.92
I(0) (reciprocal space) i0_reciprocal102000000.0000
Solution quality estimate total_estimate0.8743
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.8
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.268
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25040000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.815

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)