SAXSdb — 2ers

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

Interleukin-15 receptor alpha chain

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 31–96	Fragment：sushi domain of the Interleukin-15 receptor	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 7.4；298 K；Ionic strength (raw mmCIF value) 150mM NaCl；Pressure ambient NMR sample composition：1 mM Il-15 receptor sushi domian 15N,13C; 20mM phosphate buffer; 150mM sodium chloride; 7% D2O; pH = 7.4 \| 20mM phosphate buffer; 150mM sodium chloride; 7% D2O; pH = 7.4p	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 2ERS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2Z3Q Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.85 Å R-free 0.252
2Z3Q Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.85 Å R-free 0.252
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	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 B 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain J 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain N 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
2Z3R Crystal structure of the IL-15/IL-15Ra complex Deposited 2007-06-05	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain P 31–132（102 aa） Fragment：IL-15Ra, residues in database 31-132	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å R-free 0.250
4GS7 Structure of the Interleukin-15 quaternary complex Deposited 2012-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain D 30–97（68 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 ACT ACETATE ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.75；298 K；22.5% PEG3350, 0.1M BIS-TRIS propane, 0.2M sodium acetate, pH 8.75, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.35 Å R-free 0.227

3 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	I15RA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–66； UniProt 31–96

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	2ers
Deposition date deposition_date	2005-10-25
Structure title title	Solution structure of the Interleukin-15 receptor sushi domain
Keywords keywords	sushi domain, SIGNALING PROTEIN; SIGNALING PROTEIN
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	13.70 Å
Radius of gyration Rg (electron density) rg_electron	12.88 Å
Forward intensity I(0) i0	1305410.00
Molecular weight molecular_weight	7434.0 kDa
Excluded volume excluded_volume	9275 Å³
Envelope volume envelope_volume	11259 Å³
Hydration-shell volume shell_volume	8111 Å³
Envelope diameter envelope_diameter	48.8 Å
Shell Rg shell_rg	17.37 Å
Envelope Rg envelope_rg	13.40 Å
Shape Rg shape_rg	12.85 Å
Total Rg total_rg	14.15 Å
Total atoms total_atoms	1046
Residues n_residues	66
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	50.1 Å
Rg (real space) rg_real	13.77 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	1.3050e+06
I(0) uncertainty (real space) i0_real_error	1.4500e+04
Rg (reciprocal space) rg_reciprocal	13.76 Å
I(0) (reciprocal space) i0_reciprocal	1305000.0000
Solution quality estimate total_estimate	0.8279
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	14.6 Å
Skewness Skewness skewness	0.496
Kurtosis Kurtosis kurtosis	-0.025
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	416900.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.678; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.751; Smooth: 0.975

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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	d2ersa1
Class class	g — Small proteins
Fold Fold fold	g.18 — Complement control module/SCR domain
Superfamily Superfamily superfamily	g.18.1 — Complement control module/SCR domain
Family Family family	g.18.1.1 — Complement control module/SCR domain

CATH v4.4 (1 domains)

Domain ID domain_id	2ersA01
Class class	2 — Mainly Beta
Architecture architecture	20 — Single Sheet
Topology topology	28 — Rubrerythrin, domain 2
Homologous superfamily homologous superfamily	230 —

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8. Citations (1)

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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-15 receptor alpha chain
Molecular weight formula_weight	7473.6 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	1046

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

Solution structure of the Interleukin-15 receptor sushi domain

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

Interleukin-15 receptor alpha chain

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 (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/er/2ers/2ers.fit
pddf	/app/data/pr_computation/er/2ers/2ers.pr.out
profile	/app/data/saxs_computation/er/2ers/2ers.dat