SAXSdb — 2vsg

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

VARIANT SURFACE GLYCOPROTEIN ILTAT 1.24

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	VSI4_TRYBB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–358； UniProt 24–381 Author chain B； PDBConstruct 1–358； UniProt 24–381

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	2vsg
Deposition date deposition_date	1998-11-19
Structure title title	A Structural Motif in the Variant Surface Glycoproteins of Trypanosoma Brucei
Keywords keywords	VSG, TRYPANOSOME, ANTIGENIC VARIATION, MEMBRANE PROTEIN; MEMBRANE PROTEIN
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.

2vsg__assembly_1__model_1

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

Download this curve (.dat)

2vsg__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2vsg__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.20 Å
Rg (electron density)	32.92 Å
Total Rg	33.23 Å
Atom count	5372
Residues	716
Excluded volume	95080 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2vsg__assembly_1__model_1`	dimeric （2）	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 (2)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2vsga_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.1 — Variant surface glycoprotein (N-terminal domain)
Family Family family	h.4.1.1 — Variant surface glycoprotein (N-terminal domain)

Domain ID domain_id	d2vsgb_
Class class	h — Coiled coil proteins
Fold Fold fold	h.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamily	h.4.1 — Variant surface glycoprotein (N-terminal domain)
Family Family family	h.4.1.1 — Variant surface glycoprotein (N-terminal domain)

CATH v4.4 (4 domains)

Domain ID domain_id	2vsgA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	150 — Variant Surface Glycoprotein; Chain A domain 1
Homologous superfamily homologous superfamily	10 — Variant Surface Glycoprotein, subunit A domain 1

Domain ID domain_id	2vsgA02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	470 — Variant Surface Glycoprotein, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Variant Surface Glycoprotein, subunit A, domain 2

Domain ID domain_id	2vsgB01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	150 — Variant Surface Glycoprotein; Chain A domain 1
Homologous superfamily homologous superfamily	10 — Variant Surface Glycoprotein, subunit A domain 1

Domain ID domain_id	2vsgB02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	470 — Variant Surface Glycoprotein, subunit A; domain 2
Homologous superfamily homologous superfamily	10 — Variant Surface Glycoprotein, subunit A, domain 2

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Unit-cell length a length_a	55.100 Å
Unit-cell length b length_b	98.800 Å
Unit-cell length c length_c	172.900 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	—
R_work r_work	0.2030
R_free r_free	—

Description description	VARIANT SURFACE GLYCOPROTEIN ILTAT 1.24
Molecular weight formula_weight	38286.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5455

A Structural Motif in the Variant Surface Glycoproteins of Trypanosoma Brucei

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

VARIANT SURFACE GLYCOPROTEIN ILTAT 1.24

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

2vsg__assembly_1__model_1

2vsg__assembly_1__model_1 | I(q)

2vsg__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (4)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	83

A Structural Motif in the Variant Surface Glycoproteins of Trypanosoma Brucei

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

VARIANT SURFACE GLYCOPROTEIN ILTAT 1.24

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

2vsg__assembly_1__model_1

2vsg__assembly_1__model_1 | I(q)

2vsg__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

7. Citations (4)