9sg0

CJM112 Fv in complex with human IL-17A

Method: X-RAY DIFFRACTION Dmax: 74.9 Å Quality: REASONABLE

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

Interleukin-17A

Homo sapiens

UniProt Q16552

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 24–155 Not recorded CJM112 Fv heavy-chain × 2 CJM112 Fv light-chain × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;292 K;0.1M MES pH 6.5, 0.2M ammonium sulfate, 15% PEG 5,000 MME Resolution 2.65 Å R-free 0.256

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.

43 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL17_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–138; UniProt 24–155

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 9sg0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9sg0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9sg0
Deposition date deposition_date2025-08-21
最后修订 last_revision2025-10-29
Structure title titleCJM112 Fv in complex with human IL-17A
Keywords keywordsMONOCLONAL ANTIBODY, CYTOKINE, THERAPEUTIC ANTIBODY, FV FRAGMENT; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.29
Radius of gyration Rg (electron density) rg_electron21.30
Forward intensity I(0) i023217500.00
Molecular weight molecular_weight35813.0 kDa
Excluded volume excluded_volume44418 ų
Envelope volume envelope_volume54213 ų
Hydration-shell volume shell_volume21715 ų
Envelope diameter envelope_diameter78.0
Shell Rg shell_rg27.74
Envelope Rg envelope_rg21.87
Shape Rg shape_rg21.23
Total Rg total_rg22.33
Total atoms total_atoms2520
Residues n_residues320
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 dmax74.9
Rg (real space) rg_real22.25
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.3220e+07
I(0) uncertainty (real space) i0_real_error2.9710e+05
Rg (reciprocal space) rg_reciprocal22.26
I(0) (reciprocal space) i0_reciprocal23220000.0000
Solution quality estimate total_estimate0.6251
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4858000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 0.189; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)