SAXSdb — 2ww6

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

FIBRITIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	TETRAETHYLENE GLYCOL × 1 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q76VI8_BPT2
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–27； UniProt 458–484 Author chain B； PDBConstruct 1–27； UniProt 458–484 Author chain C； PDBConstruct 1–27； UniProt 458–484

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	2ww6
Deposition date deposition_date	2009-10-22
Structure title title	foldon containing D-amino acids in turn positions
Keywords keywords	D-AMINO ACIDS, CHAPERONE, VIRAL PROTEIN; CHAPERONE
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.

2ww6__assembly_1__model_1

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

Download this curve (.dat)

2ww6__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ww6__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	13.18 Å
Rg (electron density)	11.67 Å
Total Rg	13.26 Å
Atom count	680
Residues	75
Excluded volume	12306 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ww6__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 (3)

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Unit-cell length a length_a	29.830 Å
Unit-cell length b length_b	29.830 Å
Unit-cell length c length_c	75.080 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	9

Space group space_group	P 32
Space-group number int_tables_number	145
Crystal system crystal_system	—

Resolution resolution	0.980 Å
Low-resolution limit resolution_low	17.980 Å
R factor r_factor	0.1298
R_work r_work	0.1292
R_free r_free	0.1471

Description description	FIBRITIN
Molecular weight formula_weight	3130.6 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	915

foldon containing D-amino acids in turn positions

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

FIBRITIN

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

2ww6__assembly_1__model_1

2ww6__assembly_1__model_1 | I(q)

2ww6__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	1

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	179

foldon containing D-amino acids in turn positions

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

FIBRITIN

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

2ww6__assembly_1__model_1

2ww6__assembly_1__model_1 | I(q)

2ww6__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Citations (1)