5n7w

Computationally designed functional antibody

Method: X-RAY DIFFRACTION Dmax: 166.4 Å Quality: GOOD

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 X; UniProt 1–155 Chain Y; UniProt 1–155 Not recorded Antibody Fragment Heavy Chain × 2 Antibody Fragment Light Chain × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;18% (w/v) PEG-MME 2000, 100mM PCTP pH4.5 Resolution 1.96 Å R-free 0.250

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 3
Chains and sequence ranges Author chain X; PDBConstruct 1–155; UniProt 1–155 Author chain Y; PDBConstruct 1–155; UniProt 1–155

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 5n7w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n7w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5n7w
Deposition date deposition_date2017-02-21
Structure title titleComputationally designed functional antibody
Keywords keywordsComputationally designed antibody IL17, immune system; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier47.14
Radius of gyration Rg (electron density) rg_electron48.24
Forward intensity I(0) i0208963000.00
Molecular weight molecular_weight117030.0 kDa
Excluded volume excluded_volume145940 ų
Envelope volume envelope_volume214620 ų
Hydration-shell volume shell_volume41945 ų
Envelope diameter envelope_diameter175.4
Shell Rg shell_rg43.50
Envelope Rg envelope_rg48.84
Shape Rg shape_rg48.16
Total Rg total_rg48.27
Total atoms total_atoms8244
Residues n_residues1070
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 dmax166.4
Rg (real space) rg_real48.04
Rg uncertainty (real space) rg_real_error2.05
I(0) (real space) i0_real2.0900e+08
I(0) uncertainty (real space) i0_real_error3.8560e+06
Rg (reciprocal space) rg_reciprocal47.14
I(0) (reciprocal space) i0_reciprocal208700000.0000
Solution quality estimate total_estimate0.7512
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.4
Skewness Skewness skewness0.650
Kurtosis Kurtosis kurtosis-0.070
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7745000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.678; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.635; Smooth: 0.094

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id5n7wA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5n7wB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5n7wB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5n7wH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5n7wL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5n7wL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5n7wX01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5n7wY01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)