SAXSdb — 1ik0

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

INTERLEUKIN-13

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 21–132	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6；298 K；Ionic strength (raw mmCIF value) 40 mM sodium phosphate, 2 mM NaN3, 40 mM NaCl；Pressure ambient NMR measurement conditions：pH 6；298 K；Ionic strength (raw mmCIF value) 40 mM sodium phosphate, 2 mM NaN3, 40 mM NaCl；Pressure ambient NMR measurement conditions：pH 6；298 K；Ionic strength (raw mmCIF value) 40 mM sodium phosphate, 2 mM NaN3, 40 mM NaCl；Pressure ambient NMR sample composition：1mM interleukin-13 U-15N; 40mM phosphate buffer; 2mM NaN3; 40 mM NaCl 90% H2O, 10% D2O; pH 6.0 \| 90% H2O/10% D2O NMR sample composition：1mM interleukin-13 U-15N,U-13C; 40mM phosphate buffer; 2mM NaN3; 40 mM NaCl 90% H2O, 10% D2O; pH 6.0 \| 90% H2O/10% D2O NMR sample composition：1mM interleukin-13 U-15N,U-13C; 40mM phosphate buffer; 2mM NaN3; 40 mM NaCl; 100% D2O; pH 6.0 \| 100% D2O	Resolution not provided

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.

Other PDB	Difference from Current Entry 1IK0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GA3 NMR STRUCTURE OF INTERLEUKIN-13 Deposited 2000-11-29	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 35–146（112 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.1；298 K；Ionic strength (raw mmCIF value) 50mM NaCl；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] IL-13, 25 mM phosphate buffer, 50 mM sodium chloride, 1 mM EDTA, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
1IJZ Solution Structure of Human IL-13 Deposited 2001-05-01	Parsed fields agree	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 21–132（112 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 40 mM sodium phosphate, 2 mM NaN3, 40 mM NaCl；Pressure ambient NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 40 mM sodium phosphate, 2 mM NaN3, 40 mM NaCl；Pressure ambient NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 40 mM sodium phosphate, 2 mM NaN3, 40 mM NaCl；Pressure ambient NMR sample composition 1mM interleukin-13 U-15N; 40mM phosphate buffer; 2mM NaN3; 40 mM NaCl 90% H2O, 10% D2O; pH 6.0 \| 90% H2O/10% D2O NMR sample composition 1mM interleukin-13 U-15N,U-13C; 40mM phosphate buffer; 2mM NaN3; 40 mM NaCl 90% H2O, 10% D2O; pH 6.0 \| 90% H2O/10% D2O NMR sample composition 1mM interleukin-13 U-15N,U-13C; 40mM phosphate buffer; 2mM NaN3; 40 mM NaCl; 100% D2O; pH 6.0 \| 100% D2O	Resolution not provided
3G6D Crystal structure of the complex between CNTO607 Fab and IL-13 Deposited 2009-02-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 21–132（112 aa） Fragment：UNP residues 21-132	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.5；293 K；0.1 M Sodium acetate pH 4.5, 4.9 M Sodium formate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.263
3G6D Crystal structure of the complex between CNTO607 Fab and IL-13 Deposited 2009-02-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 21–132（112 aa） Fragment：UNP residues 21-132	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.5；293 K；0.1 M Sodium acetate pH 4.5, 4.9 M Sodium formate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.20 Å R-free 0.263
3L5W Crystal structure of the complex between IL-13 and C836 FAB Deposited 2009-12-22	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 35–146（112 aa） Fragment：UNP residues 35-146	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；293 K；0.1 M HEPES PH 7.5, 20% PEG 3350, 0.2 M SODIUM TARTRATE; CRYO CONDITIONS: MOTHER LIQUOR + 18% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.00 Å R-free 0.253
3L5W Crystal structure of the complex between IL-13 and C836 FAB Deposited 2009-12-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain J 35–146（112 aa） Fragment：UNP residues 35-146	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；293 K；0.1 M HEPES PH 7.5, 20% PEG 3350, 0.2 M SODIUM TARTRATE; CRYO CONDITIONS: MOTHER LIQUOR + 18% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.00 Å R-free 0.253
3L5X Crystal structure of the complex between IL-13 and H2L6 FAB Deposited 2009-12-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 35–146（112 aa） Fragment：UNP residues 35-146	Not recorded	MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES PH 6.5, 14% PEG 3350, 0.2 M AMMONIUM TARTRATE. CRYO CONDITIONS: 0.1 M MES PH 6.5, 20% PEG 3K, 0.2 M AMM TARTRATE, 15% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.90 Å R-free 0.247
3LB6 The structure of IL-13 in complex with IL-13Ralpha2 Deposited 2010-01-07	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 15–146（132 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；100 mM MES, pH 6.0, 200 mM CaCl2, 20% PEG-6000, and 4% v/v polypropylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.05 Å R-free 0.269
3LB6 The structure of IL-13 in complex with IL-13Ralpha2 Deposited 2010-01-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 15–146（132 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；298 K；100 mM MES, pH 6.0, 200 mM CaCl2, 20% PEG-6000, and 4% v/v polypropylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.05 Å R-free 0.269
4I77 Lebrikizumab Fab bound to IL-13 Deposited 2012-11-30	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain Z 35–146（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；15% w/v PEG1000, 0.05 M sodium malonate, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K	Resolution 1.90 Å R-free 0.219
4PS4 Crystal structure of the complex between IL-13 and M1295 FAB Deposited 2014-03-06	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 35–146（112 aa） Fragment：UNP RESIDUES 35-146	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；293 K；0.1 M SODIUM ACETATE PH 4.5, 25% PEG 8K, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.80 Å R-free 0.271
5E4E Engineered Interleukin-13 bound to receptor Deposited 2015-10-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 34–146（113 aa） Fragment：UNP residues 34-146	Mutation：L10V, V18I, L39R, D87S, T88S, L101F, K104R, K105T	SO4 SULFATE ION × 7 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.2；293 K；lithium sulfate, phosphate/citrate pH 4.2, PEG 1000	Resolution 3.00 Å R-free 0.288
5L6Y il13 in complex with tralokinumab Deposited 2016-06-01	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 35–146（112 aa）	Not recorded	FMT FORMIC ACID × 15	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；sodium formate	Resolution 1.99 Å R-free 0.211

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IL13_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–113； UniProt 21–132

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1ik0
Deposition date deposition_date	2001-05-01
Structure title title	Solution Structure of Human IL-13
Keywords keywords	left-handed four-helix bundle, CYTOKINE; CYTOKINE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	14.47 Å
Radius of gyration Rg (electron density) rg_electron	14.06 Å
Forward intensity I(0) i0	1881060000.00
Molecular weight molecular_weight	373880.0 kDa
Excluded volume excluded_volume	470730 Å³
Envelope volume envelope_volume	34315 Å³
Hydration-shell volume shell_volume	17192 Å³
Envelope diameter envelope_diameter	58.4 Å
Shell Rg shell_rg	23.05 Å
Envelope Rg envelope_rg	16.91 Å
Shape Rg shape_rg	14.03 Å
Total Rg total_rg	14.30 Å
Total atoms total_atoms	52950
Residues n_residues	3390
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	50.3 Å
Rg (real space) rg_real	14.38 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	1.8810e+09
I(0) uncertainty (real space) i0_real_error	2.0940e+07
Rg (reciprocal space) rg_reciprocal	14.39 Å
I(0) (reciprocal space) i0_reciprocal	1881000000.0000
Solution quality estimate total_estimate	0.8439
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	17.8 Å
Skewness Skewness skewness	0.126
Kurtosis Kurtosis kurtosis	-0.225
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	293700.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.669; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.962

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1ik0a1
Class class	a — All alpha proteins
Fold Fold fold	a.26 — 4-helical cytokines
Superfamily Superfamily superfamily	a.26.1 — 4-helical cytokines
Family Family family	a.26.1.2 — Short-chain cytokines

Domain ID domain_id	d1ik0a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	1ik0A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily	10 —

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8. Citations (1)

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Description description	INTERLEUKIN-13
Molecular weight formula_weight	12490.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	52950

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

fit	/app/data/saxs_computation/ik/1ik0/1ik0.fit
pddf	/app/data/pr_computation/ik/1ik0/1ik0.pr.out
profile	/app/data/saxs_computation/ik/1ik0/1ik0.dat

Solution Structure of Human IL-13

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

INTERLEUKIN-13

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)