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6nmy

A Cytokine-receptor complex

Method: X-RAY DIFFRACTION Dmax: 197.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Interleukin-3 receptor subunit alpha

Homo sapiens

UniProt P26951

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain F； UniProt 20–307 Mutation：N194Q Cytokine receptor common subunit beta × 1 （P32927） Interleukin-3 × 1 （P08700） Cytokine receptor common subunit beta × 1 （P32927） ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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
2 Other combination Heteromer Protein × 4 其他Polymer 3 PDB declaration: tetrameric（4） Consistent with protein copy count Chain M； UniProt 20–307 Mutation：N194Q Cytokine receptor common subunit beta × 1 （P32927） Interleukin-3 × 1 （P08700） Cytokine receptor common subunit beta × 1 （P32927） beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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 6NMY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4JZJ Crystal Structure of Receptor-Fab Complex Deposited 2013-04-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 20–307（288 aa） Fragment：DOMAIN 2, DOMAIN 3, UNP residues 20-307
Chain D 20–307（288 aa） Fragment：DOMAIN 2, DOMAIN 3, UNP residues 20-307
Mutation：Deletion R145, A298V Mutation：Deletion R145, A298V NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；293 K；22% PEG 3350, 200mM Sodium Malonate, 100mM Citrate Buffer, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.244
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 20–307（288 aa） Fragment：UNP residues 20-307
Mutation：N212Q, A298V 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 conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 20–307（288 aa） Fragment：UNP residues 20-307
Mutation：N212Q, A298V 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 conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 20–307（288 aa） Fragment：UNP residues 20-307
Mutation：N212Q, A298V 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

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL3RA_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain F； PDBConstruct 1–288； UniProt 20–307 Author chain M； PDBConstruct 1–288； UniProt 20–307

Cytokine receptor common subunit beta

Homo sapiens

UniProt P32927

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 25–240 Chain B； UniProt 241–438 Mutation：N346Q Interleukin-3 receptor subunit alpha × 1 （P26951） Interleukin-3 × 1 （P08700） ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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
2 Other combination Heteromer Protein × 4 其他Polymer 3 PDB declaration: tetrameric（4） Consistent with protein copy count Chain C； UniProt 25–240 Chain D； UniProt 241–438 Mutation：N346Q Interleukin-3 receptor subunit alpha × 1 （P26951） Interleukin-3 × 1 （P08700） beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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 6NMY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C8P NMR STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE COMMON BETA-CHAIN IN THE GM-CSF, IL-3 AND IL-5 RECEPTORS Deposited 1999-10-05 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 338–438（101 aa） Fragment：DOMAIN 4
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.1；293 K；Ionic strength (raw mmCIF value) 0.06M；Pressure AMBIENT
NMR sample composition 0.4MM D4BC U-15N; 10MM PHOSPHATE BUFFER;90% H2O, 10% D2O
NMR sample composition 0.4MM D4BC U-15N; 10MM PHOSPHATE BUFFER;100% D2O
Resolution not provided
1EGJ DOMAIN 4 OF THE BETA COMMON CHAIN IN COMPLEX WITH AN ANTIBODY Deposited 2000-02-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 338–438（101 aa） Fragment：DOMAIN 4
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；12% peg 4000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K
Resolution 2.80 Å R-free 0.288
1GH7 CRYSTAL STRUCTURE OF THE COMPLETE EXTRACELLULAR DOMAIN OF THE BETA-COMMON RECEPTOR OF IL-3, IL-5, AND GM-CSF Deposited 2000-11-27 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 25–437（413 aa） Fragment：EXTRACELLULAR DOMAIN
Chain B 25–437（413 aa） Fragment：EXTRACELLULAR DOMAIN
Mutation：N328Q Mutation：N328Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG MME 5000, Phosphate, pH 6.5, VAPOR DIFFUSION/HANGING DROP, temperature 277K
Resolution 3.00 Å R-free 0.307
2NA8 Transmembrane Structure of the Cytokine Receptor Common Subunit beta Deposited 2015-12-21 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 432–473（42 aa） Fragment：Helical transmembrane residues 432-473
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；313 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N; 80% 2H] protein, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
2NA9 Transmembrane Structure of the P441A Mutant of the Cytokine Receptor Common Subunit beta Deposited 2015-12-21 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 432–473（42 aa） Fragment：Helical transmembrane residues 432-473
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；313 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient
NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N; 80% 2H] protein, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
4NKQ Structure of a Cytokine Receptor Complex Deposited 2013-11-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 25–438（414 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；293 K；100mM HEPES buffer (pH 7.0), 6%(v/v) PEG3350, 0.2M proline, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.30 Å R-free 0.273
5DWU Beta common receptor in complex with a Fab Deposited 2015-09-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 17–240（224 aa）
Chain B 241–443（203 aa）
Mutation：N106Q NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.1 M Tris 8, 25% - 35% PEG200
Resolution 3.97 Å R-free 0.330
8TLD Structure of the IL-5 Signaling Complex Deposited 2023-07-26 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 × 5 PDB declaration: pentameric
Chain B 23–442（420 aa）
Chain E 23–442（420 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL3RB_HUMAN
Isoform —
PDB entities 2, 4
Chains and sequence ranges Author chain A； PDBConstruct 1–216； UniProt 25–240 Author chain C； PDBConstruct 1–216； UniProt 25–240 Author chain B； PDBConstruct 1–198； UniProt 241–438 Author chain D； PDBConstruct 1–198； UniProt 241–438

Interleukin-3

Homo sapiens

UniProt P08700

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain J； UniProt 31–144 Mutation：W13Y Interleukin-3 receptor subunit alpha × 1 （P26951） Cytokine receptor common subunit beta × 1 （P32927） Cytokine receptor common subunit beta × 1 （P32927） ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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
2 Other combination Heteromer Protein × 4 其他Polymer 3 PDB declaration: tetrameric（4） Consistent with protein copy count Chain I； UniProt 31–144 Mutation：W13Y Interleukin-3 receptor subunit alpha × 1 （P26951） Cytokine receptor common subunit beta × 1 （P32927） Cytokine receptor common subunit beta × 1 （P32927） beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 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

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 6NMY Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1JLI HUMAN INTERLEUKIN 3 (IL-3) MUTANT WITH TRUNCATION AT BOTH N-AND C-TERMINI AND 14 RESIDUE CHANGES, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1995-12-14 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 34–144（111 aa）
Mutation：DEL(1-13), V14A, N18I, T25H, Q29R, L32N, F37P, G42S, Q45M, N51R, R55T, E59L, N62V, S67H, Q69E, DEL(126-133) No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
5UV8 Interleukin-3 Receptor Complex Deposited 2017-02-19 Different construct Different mutation/modification Different oligomeric state 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 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 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

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL3_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain I； PDBConstruct 5–118； UniProt 31–144 Author chain J； PDBConstruct 5–118； UniProt 31–144

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.

SAXS scattering curve SAXS Profile

SAXS profile for 6nmy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6nmy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6nmy
Deposition date deposition_date2019-01-13
Structure title titleA Cytokine-receptor complex
Keywords keywordscytokine-receptor complex, receptor assembly, cell surface, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier46.98 Å
Radius of gyration Rg (electron density) rg_electron47.50 Å
Forward intensity I(0) i0536375000.00
Molecular weight molecular_weight184350.0 kDa
Excluded volume excluded_volume228460 ų
Envelope volume envelope_volume347750 ų
Hydration-shell volume shell_volume66360 ų
Envelope diameter envelope_diameter209.1 Å
Shell Rg shell_rg47.14 Å
Envelope Rg envelope_rg47.61 Å
Shape Rg shape_rg47.54 Å
Total Rg total_rg47.34 Å
Total atoms total_atoms12963
Residues n_residues1571
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax197.9 Å
Rg (real space) rg_real47.54 Å
Rg uncertainty (real space) rg_real_error3.56 Å
I(0) (real space) i0_real5.3640e+08
I(0) uncertainty (real space) i0_real_error1.3290e+07
Rg (reciprocal space) rg_reciprocal46.98 Å
I(0) (reciprocal space) i0_reciprocal536000000.0000
Solution quality estimate total_estimate0.7519
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary52.4 Å
Skewness Skewness skewness0.749
Kurtosis Kurtosis kurtosis0.776
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37510000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.361; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.829; Smooth: 0.859
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (9)

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7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id6nmyA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3850 —
Domain ID domain_id6nmyF02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyF03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyI00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
Domain ID domain_id6nmyJ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily10 —
Domain ID domain_id6nmyM01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily3850 —
Domain ID domain_id6nmyM02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6nmyM03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
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8. Citations (1)

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9. Files and Curves (10)