SAXSdb — 2af5

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

Engineered Outer Surface Protein A (OspA) with the inserted two beta-hairpins

Borrelia burgdorferi

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	OSPA1_BORBU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 6–109； UniProt 28–131 Author chain A； PDBConstruct 156–297； UniProt 132–273

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	2af5
Deposition date deposition_date	2005-07-25
Structure title title	2.5A X-ray Structure of Engineered OspA protein
Keywords keywords	SINGLE-LAYER BETA-SHEET, BETA-HAIRPIN, REPEAT PROTEIN, De Novo Protein, Immune System; De Novo Protein, 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.

2af5__assembly_1__model_1

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

Download this curve (.dat)

2af5__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2af5__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	28.55 Å
Rg (electron density)	28.42 Å
Total Rg	28.89 Å
Atom count	2223
Residues	292
Excluded volume	39714 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2af5__assembly_1__model_1`	monomeric （1）	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) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	2af5A01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	128 — Lipocalin
Homologous superfamily homologous superfamily	160 — C1 set domains (antibody constant domain-like)

Domain ID domain_id	2af5A02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	930 — Outer Surface Protein A; domain 3
Homologous superfamily homologous superfamily	1 —

Domain ID domain_id	2af5A03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	930 — Outer Surface Protein A; domain 3
Homologous superfamily homologous superfamily	1 —

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Unit-cell length a length_a	48.547 Å
Unit-cell length b length_b	55.330 Å
Unit-cell length c length_c	70.361 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	104.08 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2457
R_work r_work	0.2424
R_free r_free	0.2756

Description description	Engineered Outer Surface Protein A (OspA) with the inserted two beta-hairpins
Molecular weight formula_weight	32292.3 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	2279

2.5A X-ray Structure of Engineered OspA protein

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

Engineered Outer Surface Protein A (OspA) with the inserted two beta-hairpins

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

2af5__assembly_1__model_1

2af5__assembly_1__model_1 | I(q)

2af5__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

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (2)

Source organism organism	Borrelia burgdorferi
Common name common_name	Lyme disease spirochete
NCBI taxonomy ID ncbi_taxonomy_id	139
Host organism host_organism	Escherichia coli BL21(DE3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	52

2.5A X-ray Structure of Engineered OspA protein

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

Engineered Outer Surface Protein A (OspA) with the inserted two beta-hairpins

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

2af5__assembly_1__model_1

2af5__assembly_1__model_1 | I(q)

2af5__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

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

7. Citations (2)