SAXSdb — 4bv4

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

PROTEIN SPAETZLE C-106

DROSOPHILA MELANOGASTER

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3 其他Polymer 1	PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA × 1 （P08953,Q4G1L2） ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)]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 × 4 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SPZ_DROME
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain L； PDBConstruct 2–107； UniProt 221–326 Author chain M； PDBConstruct 2–107； UniProt 221–326

PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA

EPTATRETUS BURGERI

UniProt P08953

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3 其他Polymer 1	PROTEIN SPAETZLE C-106 × 2 （P48607） ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)]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 × 4 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	TOLL_DROME
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain R； PDBConstruct 1–370； UniProt 28–397

PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA

EPTATRETUS BURGERI

UniProt Q4G1L2

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 3 其他Polymer 1	PROTEIN SPAETZLE C-106 × 2 （P48607） ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)]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 × 4 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q4G1L2_EPTBU
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain R； PDBConstruct 373–441； UniProt 133–201

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	4bv4
Deposition date deposition_date	2013-06-24
Structure title title	Structure and allostery in Toll-Spatzle recognition
Keywords keywords	CYTOKINE RECOGNITION, EMBRYONIC DEVELOPMENT, IMMUNE SYSTEM, INNATE IMMUNITY, LEUCINE-RICH REPEATS, CYSTINE-KNOT, GLYCOPROTEIN; IMMUNE SYSTEM
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

4bv4__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4bv4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4bv4__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	28.27 Å
Rg (electron density)	27.62 Å
Total Rg	28.34 Å
Atom count	4720
Residues	574
Excluded volume	83898 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4bv4__assembly_1__model_1`	trimeric （3）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	PROTEIN SPAETZLE C-106
Molecular weight formula_weight	11992.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,M
Atom count atom_count	4830

GVGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCCKCALKTG

Source Source

Source organism organism	DROSOPHILA MELANOGASTER
Common name common_name	FRUIT FLY
NCBI taxonomy ID ncbi_taxonomy_id	7227
Host organism host_organism	SPODOPTERA FRUGIPERDA

Entity 2 Entity 2 polymer

Description description	PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA
Molecular weight formula_weight	50749.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R

SFGRDACSEMSIDGLCQCAPIMSEYEIICPANAENPTFRLTIQPKDYVQIMCNLTDTTDYQQLPKKLRIGEVDRVQMRRCMLPGHTPIASILDYLGIVSPTTLIFESDNLGMNITRQHLDRLHGLKRFRFTTRRLTHIPANLLTDMRNLSHLELRANIEEMPSHLFDDLENLESIEFGSNKLRQMPRGIFGKMPKLKQLNLWSNQLHNLTKHDFEGATSVLGIDIHDNGIEQLPHDVFAHLTNVTDINLSANLFRSLPQGLFDHNKHLNEVRLMNNRVPLATLPSRLFANQPELQILRLRAELQSLPGDLFEHSTQITNISLGDNLLKTLPATLLEHQVNLLSLDLSNNRLTHLPDSLFAHTTNLTDLRLASNQLKSVPDGIFDRLTSLQKIWLHTNPWDCSCPRIDYLSRWLNKNSQKEQGSAKCSGSGKPVRSIICPTTGENLY

Source Source

Source organism organism	EPTATRETUS BURGERI
Common name common_name	INSHORE HAGFISH
NCBI taxonomy ID ncbi_taxonomy_id	7764
Host organism host_organism	SPODOPTERA FRUGIPERDA

Entity 3 Entity 3 branched

Description description	;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	1397.2 kDa
Source method src_method	man
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	4

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	104

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6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	4bv4L00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	4bv4M00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily	10 — Cystine-knot cytokines

Domain ID domain_id	4bv4R00
Class class	3 — Alpha Beta
Architecture architecture	80 — Alpha-Beta Horseshoe
Topology topology	10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily	10 — Ribonuclease Inhibitor

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Unit-cell length a length_a	198.310 Å
Unit-cell length b length_b	57.110 Å
Unit-cell length c length_c	70.500 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.76 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.350 Å
Low-resolution limit resolution_low	49.120 Å
R factor r_factor	0.1967
R_work r_work	0.1950
R_free r_free	0.2271

Structure and allostery in Toll-Spatzle recognition

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

PROTEIN SPAETZLE C-106

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA

State in the Current Structure

Other States of the Same Protein in the Database

PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4bv4__assembly_1__model_1

4bv4__assembly_1__model_1 | I(q)

4bv4__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 branched

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (1)

Structure and allostery in Toll-Spatzle recognition

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

PROTEIN SPAETZLE C-106

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

PROTEIN TOLL, VARIABLE LYMPHOCYTE RECEPTOR B CHIMERA

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4bv4__assembly_1__model_1

4bv4__assembly_1__model_1 | I(q)

4bv4__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 branched

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (1)