SAXSdb — 1dyl

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

NUCLEOCAPSID PROTEIN

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 240	No other associated polymer	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	No other associated polymer	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 20	No other associated polymer	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 24	No other associated polymer	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 4	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	POLS_SFV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–149； UniProt 119–267 Author chain B； PDBConstruct 1–149； UniProt 119–267 Author chain C； PDBConstruct 1–149； UniProt 119–267 Author chain D； PDBConstruct 1–149； UniProt 119–267

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	1dyl
Deposition date deposition_date	2000-02-02
Structure title title	9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY
Keywords keywords	;VIRUS/VIRAL PROTEIN, ALPHAVIRUS, SFV, CRYO-EM, IMAGE RECONSTRUCTION, ENVELOPED VIRUS, CAPSID PROTEIN, ICOSAHEDRAL VIRUS, VIRUS-VIRAL PROTEIN complex ;; VIRUS/VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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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.

1dyl__assembly_1__model_1

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

Download this curve (.dat)

1dyl__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1dyl__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	0.00 Å
Rg (electron density)	182.70 Å
Total Rg	183.00 Å
Atom count	273780
Residues	35760
Excluded volume	4837800 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1dyl__assembly_1__model_1`	240-MERIC （240）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1dyl__assembly_2__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3	1	`1dyl__assembly_3__model_1`	eicosameric （20）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
4	1	`1dyl__assembly_4__model_1`	24-meric （24）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
5	1	`1dyl__assembly_5__model_1`	tetrameric （4）	Excluded	—	—
	Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (1)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1dyla_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1dylb_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1dylc_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

Domain ID domain_id	d1dyld_
Class class	i — Low resolution protein structures
Fold Fold fold	i.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamily	i.6.1 — Viruses and virus-receptor complexes
Family Family family	i.6.1.1 — Viruses and virus-receptor complexes

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

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

Resolution resolution	9.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	9.00 Å
Resolution测定Method resolution_method	;MODEL-BASED, POLAR-FOURIER- TRANSFORMATION (FULLER ET AL. 1996, J.STRUC.BIOL. 116, 48-55; BAKER AND CHENG 1996, J.STRUC.BIOL. 116, 120- 130) MODEL-BASED CROSS COMMOM LINES SEARCH AND REFINEMENT (CROWTHER ET AL. 1970, NATURE (LONDON) 226, 421- 425; FULLER ET AL. 1996, J.STRUC.BIOL. 11 48-55;FERLENGHI ET AL. 1998, J.MOL.BIOL. 283, 71-81) ;
颗粒数 num_particles	5267

Description description	NUCLEOCAPSID PROTEIN
Molecular weight formula_weight	16252.4 kDa
Source method src_method	nat
Copy count entity_count	4

9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY

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

NUCLEOCAPSID PROTEIN

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

1dyl__assembly_1__model_1

1dyl__assembly_1__model_1 | I(q)

1dyl__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

7. Citations (1)

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	4563

9 ANGSTROM RESOLUTION CRYO-EM RECONSTRUCTION STRUCTURE OF SEMLIKI FOREST VIRUS (SFV) AND FITTING OF THE CAPSID PROTEIN STRUCTURE IN THE EM DENSITY

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

NUCLEOCAPSID PROTEIN

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

1dyl__assembly_1__model_1

1dyl__assembly_1__model_1 | I(q)

1dyl__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

7. Citations (1)