8ubg

DpHF19 filament

Method: ELECTRON MICROSCOPY Dmax: 209.2 Å Quality: GOOD

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

DpHF19,Green fluorescent protein (Fragment)

Aequorea victoria

UniProt A0A059PIQ0

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 × 20 PDB declaration: 20-meric(20) Consistent with protein copy count Chain A; UniProt 3–238 Chain B; UniProt 3–238 Chain C; UniProt 3–238 Chain D; UniProt 3–238 Chain E; UniProt 3–238 Chain F; UniProt 3–238 Chain G; UniProt 3–238 Chain H; UniProt 3–238 Chain I; UniProt 3–238 Chain J; UniProt 3–238 Chain K; UniProt 3–238 Chain L; UniProt 3–238 Chain M; UniProt 3–238 Chain N; UniProt 3–238 Chain O; UniProt 3–238 Chain P; UniProt 3–238 Chain Q; UniProt 3–238 Chain R; UniProt 3–238 Chain S; UniProt 3–238 Chain T; UniProt 3–238 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

91 other PDB entries and 137 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 252–487; UniProt 3–238 Author chain B; PDBConstruct 252–487; UniProt 3–238 Author chain C; PDBConstruct 252–487; UniProt 3–238 Author chain D; PDBConstruct 252–487; UniProt 3–238 Author chain E; PDBConstruct 252–487; UniProt 3–238 Author chain F; PDBConstruct 252–487; UniProt 3–238 Author chain G; PDBConstruct 252–487; UniProt 3–238 Author chain H; PDBConstruct 252–487; UniProt 3–238 Author chain I; PDBConstruct 252–487; UniProt 3–238 Author chain J; PDBConstruct 252–487; UniProt 3–238 Author chain K; PDBConstruct 252–487; UniProt 3–238 Author chain L; PDBConstruct 252–487; UniProt 3–238 Author chain M; PDBConstruct 252–487; UniProt 3–238 Author chain N; PDBConstruct 252–487; UniProt 3–238 Author chain O; PDBConstruct 252–487; UniProt 3–238 Author chain P; PDBConstruct 252–487; UniProt 3–238 Author chain Q; PDBConstruct 252–487; UniProt 3–238 Author chain R; PDBConstruct 252–487; UniProt 3–238 Author chain S; PDBConstruct 252–487; UniProt 3–238 Author chain T; PDBConstruct 252–487; UniProt 3–238

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 8ubg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ubg
Deposition date deposition_date2023-09-22
Structure title titleDpHF19 filament
Keywords keywordsFilament, pH, designed, DE NOVO PROTEIN; DE NOVO PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.45
Radius of gyration Rg (electron density) rg_electron61.13
Forward intensity I(0) i03247260000.00
Molecular weight molecular_weight496880.0 kDa
Excluded volume excluded_volume632810 ų
Envelope volume envelope_volume1037200 ų
Hydration-shell volume shell_volume143230 ų
Envelope diameter envelope_diameter218.1
Shell Rg shell_rg63.44
Envelope Rg envelope_rg58.58
Shape Rg shape_rg61.14
Total Rg total_rg61.15
Total atoms total_atoms72500
Residues n_residues4520
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 dmax209.2
Rg (real space) rg_real61.44
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real3.2470e+09
I(0) uncertainty (real space) i0_real_error6.6500e+07
Rg (reciprocal space) rg_reciprocal61.44
I(0) (reciprocal space) i0_reciprocal3247000000.0000
Solution quality estimate total_estimate0.8198
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.4
Skewness Skewness skewness0.403
Kurtosis Kurtosis kurtosis-0.185
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha457100000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.698

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)