SAXSdb — 1jli

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

INTERLEUKIN 3

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 34–144	Mutation：DEL(1-13), V14A, N18I, T25H, Q29R, L32N, F37P, G42S, Q45M, N51R, R55T, E59L, N62V, S67H, Q69E, DEL(126-133)	No other associated polymer	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	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 1JLI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 31–152（122 aa） Fragment：UNP residues 31-152	Mutation：W32Y	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 8000, 200 mM NaCI, 100 mM citrate-phosphate buffer pH 5	Resolution 2.70 Å R-free 0.286
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 31–152（122 aa） Fragment：UNP residues 31-152	Mutation：W32Y	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 8000, 200 mM NaCI, 100 mM citrate-phosphate buffer pH 5	Resolution 2.70 Å R-free 0.286
5UWC Cytokine-receptor complex Deposited 2017-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric	Chain I 31–152（122 aa） Fragment：UNP residues 31-152	Mutation：W32Y, K116W	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CIT CITRIC ACID × 2 IMD IMIDAZOLE × 1 EDT {[-(BIS-CARBOXYMETHYL-AMINO)-ETHYL]-CARBOXYMETHYL-AMINO}-ACETIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；20% PEG 8000, 200 mM NaCl and 100 mM citrate-phosphate buffer pH 4.8	Resolution 2.40 Å R-free 0.242
6NMY A Cytokine-receptor complex Deposited 2019-01-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 31–144（114 aa）	Mutation：W13Y	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；Crystals were grown in 10 mM Tris pH6.8, 8% PEG 8000, 0.15 M magnesium chloride	Resolution 3.30 Å R-free 0.278
6NMY A Cytokine-receptor complex Deposited 2019-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 31–144（114 aa）	Mutation：W13Y	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；277.15 K；Crystals were grown in 10 mM Tris pH6.8, 8% PEG 8000, 0.15 M magnesium chloride	Resolution 3.30 Å R-free 0.278

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IL3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–112； UniProt 34–144

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	1jli
Deposition date deposition_date	1995-12-14
Structure title title	HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C-TERMINI AND 14 RESIDUE CHANGES, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords	HEMATOPOIETIC GROWTH FACTOR, COLONY-STIMULATING FACTOR, 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	15.19 Å
Radius of gyration Rg (electron density) rg_electron	13.55 Å
Forward intensity I(0) i0	3405500.00
Molecular weight molecular_weight	12827.0 kDa
Excluded volume excluded_volume	16098 Å³
Envelope volume envelope_volume	18480 Å³
Hydration-shell volume shell_volume	11555 Å³
Envelope diameter envelope_diameter	50.6 Å
Shell Rg shell_rg	19.35 Å
Envelope Rg envelope_rg	14.20 Å
Shape Rg shape_rg	13.53 Å
Total Rg total_rg	14.92 Å
Total atoms total_atoms	1819
Residues n_residues	112
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	49.7 Å
Rg (real space) rg_real	15.10 Å
Rg uncertainty (real space) rg_real_error	0.24 Å
I(0) (real space) i0_real	3.4060e+06
I(0) uncertainty (real space) i0_real_error	3.4420e+04
Rg (reciprocal space) rg_reciprocal	15.10 Å
I(0) (reciprocal space) i0_reciprocal	3406000.0000
Solution quality estimate total_estimate	0.8804
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.5 Å
Skewness Skewness skewness	0.182
Kurtosis Kurtosis kurtosis	-0.290
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	707200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.984

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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1jlia_
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

CATH v4.4 (1 domains)

Domain ID domain_id	1jliA00
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 (2)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	INTERLEUKIN 3
Molecular weight formula_weight	12844.9 kDa
Mutation mutation	DEL(1-13), V14A, N18I, T25H, Q29R, L32N, F37P, G42S, Q45M, N51R, R55T, E59L, N62V, S67H, Q69E, DEL(126-133)
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1819

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

HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C-TERMINI AND 14 RESIDUE CHANGES, NMR, MINIMIZED AVERAGE STRUCTURE

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

INTERLEUKIN 3

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

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/jl/1jli/1jli.fit
pddf	/app/data/pr_computation/jl/1jli/1jli.pr.out
profile	/app/data/saxs_computation/jl/1jli/1jli.dat