3l5w

Crystal structure of the complex between IL-13 and C836 FAB

Method: X-RAY DIFFRACTION D_max: 148.8 Å Quality: GOOD

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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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain I； UniProt 35–146	Fragment：UNP residues 35-146	C836 LIGHT CHAIN × 1 C836 HEAVY CHAIN × 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
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain J； UniProt 35–146	Fragment：UNP residues 35-146	C836 LIGHT CHAIN × 1 C836 HEAVY CHAIN × 1 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

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 3L5W	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 oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	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	Different construct 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 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
1IK0 Solution Structure of Human IL-13 Deposited 2001-05-01	Different construct 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 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 ligand/ion 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 ligand/ion 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
3L5X Crystal structure of the complex between IL-13 and H2L6 FAB Deposited 2009-12-22	Different ligand/ion 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 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 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 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 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 ligand/ion 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 ligand/ion 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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	IL13_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain I； PDBConstruct 2–113； UniProt 35–146 Author chain J； PDBConstruct 2–113； UniProt 35–146

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3l5w
Deposition date deposition_date	2009-12-22
Structure title title	Crystal structure of the complex between IL-13 and C836 FAB
Keywords keywords	;immunoglobulin fold, alpha-helical bundle, Cytokine, Disulfide bond, Glycoprotein, Polymorphism, Secreted, MONOCLONAL ANTIBODY, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	41.33 Å
Radius of gyration Rg (electron density) rg_electron	41.46 Å
Forward intensity I(0) i0	197559000.00
Molecular weight molecular_weight	114820.0 kDa
Excluded volume excluded_volume	143910 Å³
Envelope volume envelope_volume	197560 Å³
Hydration-shell volume shell_volume	41690 Å³
Envelope diameter envelope_diameter	157.1 Å
Shell Rg shell_rg	43.76 Å
Envelope Rg envelope_rg	41.18 Å
Shape Rg shape_rg	41.42 Å
Total Rg total_rg	41.75 Å
Total atoms total_atoms	8079
Residues n_residues	1057
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	148.8 Å
Rg (real space) rg_real	41.63 Å
Rg uncertainty (real space) rg_real_error	1.90 Å
I(0) (real space) i0_real	1.9760e+08
I(0) uncertainty (real space) i0_real_error	4.1000e+06
Rg (reciprocal space) rg_reciprocal	41.33 Å
I(0) (reciprocal space) i0_reciprocal	197500000.0000
Solution quality estimate total_estimate	0.8387
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	47.0 Å
Skewness Skewness skewness	0.537
Kurtosis Kurtosis kurtosis	-0.046
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13860000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.770; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.869; Smooth: 0.721

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	C836 LIGHT CHAIN
Molecular weight formula_weight	23503.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,A
Atom count atom_count	8510

DVQITQSPSYLAASPGETITLNCRASKSISKYLAWYQEKPGKTNKLLIYSGSTLQSGIPSRFSGSGSGTDFTLTISSLEPEDFAMYFCQQHNEYPYTFGGGTKLEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

来源 Source

来源生物 organism	Mus musculus, Homo sapiens
宿主生物 host_organism	Cricetulus griseus

Entity 2 Entity 2 polymer

Description description	C836 HEAVY CHAIN
Molecular weight formula_weight	24780.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,B

QVTLKESGPGILQPSQTLSLTCSFSGFSLSTYGMGVGWIRQPSGKGLEWLAHIWWDDVKRYNPALKSRLTISKDTSGSQVFLKIASVDTSDTATYYCARMGSDYDVWFDYWGQGTLVTVSAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCHHHHHH

来源 Source

来源生物 organism	Mus musculus, Homo sapiens
宿主生物 host_organism	Cricetulus griseus

Entity 3 Entity 3 polymer

Description description	Interleukin-13
Molecular weight formula_weight	12490.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,J

MGPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGRFN

来源 Source

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

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	426

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7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d3l5wa1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3l5wa2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.2 — C1 set domains (antibody constant domain-like)

Domain ID domain_id	d3l5wb_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3l5wh_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3l5wi_
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	d3l5wj_
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	d3l5wl1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3l5wl2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (10 domains)

Domain ID domain_id	3l5wA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wA02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wB02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wH02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wI00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	3l5wJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1250 — Growth Hormone; Chain: A;
Homologous superfamily homologous superfamily	10 —

Domain ID domain_id	3l5wL01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3l5wL02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	76.620 Å
Unit-cell length b length_b	65.560 Å
Unit-cell length c length_c	118.740 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.02 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2080
R_work r_work	0.2050
R_free r_free	0.2530

fit	/app/data/saxs_computation/l5/3l5w/3l5w.fit
pddf	/app/data/pr_computation/l5/3l5w/3l5w.pr.out
profile	/app/data/saxs_computation/l5/3l5w/3l5w.dat

Crystal structure of the complex between IL-13 and C836 FAB

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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (8 domains)

CATH v4.4 (10 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)