9tnz

SP100 CARD filament

Method: ELECTRON MICROSCOPY Dmax: 226.7 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Nuclear autoantigen Sp-100

Homo sapiens

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 × 26 PDB declaration: 26-meric(26) Consistent with protein copy count Chain A; UniProt 27–361 Chain AA; UniProt 27–361 Chain B; UniProt 27–361 Chain C; UniProt 27–361 Chain D; UniProt 27–361 Chain E; UniProt 27–361 Chain F; UniProt 27–361 Chain G; UniProt 27–361 Chain H; UniProt 27–361 Chain I; UniProt 27–361 Chain J; UniProt 27–361 Chain K; UniProt 27–361 Chain L; UniProt 27–361 Chain M; UniProt 27–361 Chain N; UniProt 27–361 Chain O; UniProt 27–361 Chain P; UniProt 27–361 Chain Q; UniProt 27–361 Chain R; UniProt 27–361 Chain S; UniProt 27–361 Chain T; UniProt 27–361 Chain V; UniProt 27–361 Chain W; UniProt 27–361 Chain X; UniProt 27–361 Chain Y; UniProt 27–361 Chain Z; UniProt 27–361 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.52 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 15–349; UniProt 27–361 Author chain AA; PDBConstruct 15–349; UniProt 27–361 Author chain B; PDBConstruct 15–349; UniProt 27–361 Author chain C; PDBConstruct 15–349; UniProt 27–361 Author chain D; PDBConstruct 15–349; UniProt 27–361 Author chain E; PDBConstruct 15–349; UniProt 27–361 Author chain F; PDBConstruct 15–349; UniProt 27–361 Author chain G; PDBConstruct 15–349; UniProt 27–361 Author chain H; PDBConstruct 15–349; UniProt 27–361 Author chain I; PDBConstruct 15–349; UniProt 27–361 Author chain J; PDBConstruct 15–349; UniProt 27–361 Author chain K; PDBConstruct 15–349; UniProt 27–361 Author chain L; PDBConstruct 15–349; UniProt 27–361 Author chain M; PDBConstruct 15–349; UniProt 27–361 Author chain N; PDBConstruct 15–349; UniProt 27–361 Author chain O; PDBConstruct 15–349; UniProt 27–361 Author chain P; PDBConstruct 15–349; UniProt 27–361 Author chain Q; PDBConstruct 15–349; UniProt 27–361 Author chain R; PDBConstruct 15–349; UniProt 27–361 Author chain S; PDBConstruct 15–349; UniProt 27–361 Author chain T; PDBConstruct 15–349; UniProt 27–361 Author chain V; PDBConstruct 15–349; UniProt 27–361 Author chain W; PDBConstruct 15–349; UniProt 27–361 Author chain X; PDBConstruct 15–349; UniProt 27–361 Author chain Y; PDBConstruct 15–349; UniProt 27–361 Author chain Z; PDBConstruct 15–349; UniProt 27–361

Maltose/maltodextrin-binding periplasmic protein,Nuclear autoantigen Sp-100

Homo sapiens

UniProt P23497

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 × 26 PDB declaration: 26-meric(26) Consistent with protein copy count Chain A; UniProt 33–149 Chain AA; UniProt 33–149 Chain B; UniProt 33–149 Chain C; UniProt 33–149 Chain D; UniProt 33–149 Chain E; UniProt 33–149 Chain F; UniProt 33–149 Chain G; UniProt 33–149 Chain H; UniProt 33–149 Chain I; UniProt 33–149 Chain J; UniProt 33–149 Chain K; UniProt 33–149 Chain L; UniProt 33–149 Chain M; UniProt 33–149 Chain N; UniProt 33–149 Chain O; UniProt 33–149 Chain P; UniProt 33–149 Chain Q; UniProt 33–149 Chain R; UniProt 33–149 Chain S; UniProt 33–149 Chain T; UniProt 33–149 Chain V; UniProt 33–149 Chain W; UniProt 33–149 Chain X; UniProt 33–149 Chain Y; UniProt 33–149 Chain Z; UniProt 33–149 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.52 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.

122 other PDB entries and 242 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SP100_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 409–525; UniProt 33–149 Author chain AA; PDBConstruct 409–525; UniProt 33–149 Author chain B; PDBConstruct 409–525; UniProt 33–149 Author chain C; PDBConstruct 409–525; UniProt 33–149 Author chain D; PDBConstruct 409–525; UniProt 33–149 Author chain E; PDBConstruct 409–525; UniProt 33–149 Author chain F; PDBConstruct 409–525; UniProt 33–149 Author chain G; PDBConstruct 409–525; UniProt 33–149 Author chain H; PDBConstruct 409–525; UniProt 33–149 Author chain I; PDBConstruct 409–525; UniProt 33–149 Author chain J; PDBConstruct 409–525; UniProt 33–149 Author chain K; PDBConstruct 409–525; UniProt 33–149 Author chain L; PDBConstruct 409–525; UniProt 33–149 Author chain M; PDBConstruct 409–525; UniProt 33–149 Author chain N; PDBConstruct 409–525; UniProt 33–149 Author chain O; PDBConstruct 409–525; UniProt 33–149 Author chain P; PDBConstruct 409–525; UniProt 33–149 Author chain Q; PDBConstruct 409–525; UniProt 33–149 Author chain R; PDBConstruct 409–525; UniProt 33–149 Author chain S; PDBConstruct 409–525; UniProt 33–149 Author chain T; PDBConstruct 409–525; UniProt 33–149 Author chain V; PDBConstruct 409–525; UniProt 33–149 Author chain W; PDBConstruct 409–525; UniProt 33–149 Author chain X; PDBConstruct 409–525; UniProt 33–149 Author chain Y; PDBConstruct 409–525; UniProt 33–149 Author chain Z; PDBConstruct 409–525; UniProt 33–149

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 9tnz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9tnz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9tnz
Deposition date deposition_date2025-12-16
Structure title titleSP100 CARD filament
Keywords keywordsInnate immunity, interferon, DNA damage, cryo-EM, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier76.33
Radius of gyration Rg (electron density) rg_electron78.23
Forward intensity I(0) i01200440000.00
Molecular weight molecular_weight304450.0 kDa
Excluded volume excluded_volume386620 ų
Envelope volume envelope_volume672060 ų
Hydration-shell volume shell_volume83401 ų
Envelope diameter envelope_diameter279.1
Shell Rg shell_rg57.09
Envelope Rg envelope_rg77.56
Shape Rg shape_rg78.24
Total Rg total_rg77.70
Total atoms total_atoms21502
Residues n_residues2574
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 dmax226.7
Rg (real space) rg_real73.79
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real1.1780e+09
I(0) uncertainty (real space) i0_real_error2.2120e+07
Rg (reciprocal space) rg_reciprocal71.85
I(0) (reciprocal space) i0_reciprocal1187000000.0000
Solution quality estimate total_estimate0.7778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.4
Skewness Skewness skewness0.549
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.1630
Highest regularization parameter α highest_alpha54580000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 0.986; Sysdev: 1.000; Positv: 1.000; Valcen: 0.763; Smooth: 0.105

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (2)

9. Files and Curves (10)