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	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 240 PDB declaration: 240-MERIC（240） Consistent with protein copy count	Chain A； UniProt 119–267 Chain B； UniProt 119–267 Chain C； UniProt 119–267 Chain D； UniProt 119–267	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
2	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 119–267 Chain B； UniProt 119–267 Chain C； UniProt 119–267 Chain D； UniProt 119–267	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
3	Protein homooligomer Homooligomer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain A； UniProt 119–267 Chain B； UniProt 119–267 Chain C； UniProt 119–267 Chain D； UniProt 119–267	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
4	Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 119–267 Chain B； UniProt 119–267 Chain C； UniProt 119–267 Chain D； UniProt 119–267	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å
5	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 119–267 Chain B； UniProt 119–267 Chain C； UniProt 119–267 Chain D； UniProt 119–267	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.6 cryo-EM vitrification conditions：Cryogen ETHANE；PLUNGE VITRIFICATION SAMPLES PREPARED AS THIN LAYERS OF VITREOUS ICE MAINTAINED AT NEAR LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE WITH A GATAN 626-0300 CRYOTRANSFER HOLDER.	Resolution 9.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1DYL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1I9W CRYSTAL STRUCTURE OF THE FUSION GLYCOPROTEIN E1 FROM SEMLIKI FOREST VIRUS Deposited 2001-03-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 816–1205（390 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；294 K；PEG 8K, pH 8.0, VAPOR DIFFUSION, temperature 294K	Resolution 3.00 Å R-free 0.344
1RER Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus. Deposited 2003-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain B 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain C 816–1206（391 aa） Fragment：Spike glycoprotein E1	Not recorded	BR BROMIDE ION × 3 HO HOLMIUM ATOM × 4 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP	Resolution 3.20 Å R-free 0.285
1RER Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus. Deposited 2003-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain B 816–1206（391 aa） Fragment：Spike glycoprotein E1 Chain C 816–1206（391 aa） Fragment：Spike glycoprotein E1	Not recorded	BR BROMIDE ION × 6 HO HOLMIUM ATOM × 8 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；PEG 400, NaBr, detergent DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP	Resolution 3.20 Å R-free 0.285
1VCP SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 119–267（149 aa）	Not recorded	HG MERCURY (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.	Resolution 3.00 Å
1VCP SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 119–267（149 aa）	Not recorded	HG MERCURY (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.	Resolution 3.00 Å
1VCP SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM I) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 119–267（149 aa）	Not recorded	HG MERCURY (II) ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions KHGI4 WAS REQUIRED TO OBTAIN BIG CRYSTALS. EACH OF THREE MONOMERS OF THE SEMLIKI FOREST VIRUS CORE PROTEIN BIND ONE MERCURY ATOM. THE HG ATOM FORMS A S-HG-S BOND WITH CYS 119 AND CYS 134. IN THE NATIVE STRUCTURE THERE IS A DISULFIDE BRIDGE BETWEEN CYS 119 AND CYS 134. THE S-HG DISTANCE WAS RESTRAINED TO 2.45 ANGSTROMS WHILE THE BOND ANGLE OF S-HG-S WAS RESTRAINED TO 180 DEGREES.	Resolution 3.00 Å
1VCQ SEMLIKI FOREST VIRUS CAPSID PROTEIN (CRYSTAL FORM II) Deposited 1996-03-04	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 119–267（149 aa） Chain B 119–267（149 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 3.10 Å
2ALA Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation. Deposited 2005-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 816–1206（391 aa） Fragment：Spike glycoprotein E1	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 8.1；293 K；PEG 8K, pH 8.1, EVAPORATION, temperature 293K	Resolution 3.00 Å R-free 0.319
2V33 High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus Deposited 2007-06-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1107–1197（91 aa） Fragment：DOMAIN III OF SPIKE GLYCOPROTEIN E1, RESIDUES 1107-1197	Not recorded	NO3 NITRATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；25% PEG 8K, 0.2M NA ACETATE, 0.1M CACO PH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 1.55 Å R-free 0.226
2V33 High resolution crystal structure of domain III of E1 fusion glycoprotein of Semliki Forest Virus Deposited 2007-06-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1107–1197（91 aa） Fragment：DOMAIN III OF SPIKE GLYCOPROTEIN E1, RESIDUES 1107-1197	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；25% PEG 8K, 0.2M NA ACETATE, 0.1M CACO PH 6.5, VAPOR DIFFUSION, HANGING DROP	Resolution 1.55 Å R-free 0.226
8D87 Fitted crystal structure of the homotrimer of fusion glycoprotein E1 from SFV into subtomogram averaged CHIKV E1 glycoprotein density Deposited 2022-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 816–1206（391 aa） Fragment：SPIKE GLYCOPROTEIN E1 Chain B 816–1206（391 aa） Fragment：SPIKE GLYCOPROTEIN E1 Chain C 816–1206（391 aa） Fragment：SPIKE GLYCOPROTEIN E1	Not recorded	BR BROMIDE ION × 3 HO HOLMIUM ATOM × 4 PO4 PHOSPHATE ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 5.1；Hepes Buffer Saline cryo-EM vitrification conditions Cryogen ETHANE；blot for 7-8 seconds X-ray crystallization conditions pH 4；PEG 400, NABR, DETERGENT DDAO, HO3+, VAPOR DIFFUSION, HANGING DROP, PH 4, TEMPERATURE 277.0K	Resolution 27.20 Å R-free 0.285
8IHP Structure of Semliki Forest virus VLP in complex with the receptor VLDLR-LA3 Deposited 2023-02-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 334–755（422 aa） Chain B 816–1253（438 aa） Chain C 106–267（162 aa） Chain D 334–755（422 aa） Chain E 816–1253（438 aa） Chain F 106–267（162 aa） Chain G 334–755（422 aa） Chain H 816–1253（438 aa） Chain I 106–267（162 aa） Chain J 334–755（422 aa） Chain K 816–1253（438 aa） Chain L 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8UA8 Structure of Semliki Forest virus VLP in complex with VLDLR LA2 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain C 273–326（54 aa） Chain D 115–267（153 aa） Chain G 273–326（54 aa） Chain H 115–267（153 aa） Chain K 273–326（54 aa） Chain L 115–267（153 aa） Chain O 273–326（54 aa） Chain P 115–267（153 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
8X0K Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(2-fold) Deposited 2023-11-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 16 PDB declaration: 16-meric	Chain A 106–267（162 aa） Chain E 106–267（162 aa） Chain I 106–267（162 aa） Chain M 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8X0L Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(3-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 12 PDB declaration: 12-meric	Chain A 106–267（162 aa） Chain E 106–267（162 aa） Chain I 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8X0M Cryo-EM structure of Semliki Forest virus in complex with its receptor VLDLR(5-fold) Deposited 2023-11-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: 11-meric	Chain A 106–267（162 aa） Chain E 106–267（162 aa） Chain I 106–267（162 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
9KQR Cryo-EM Structure of Mature Semliki Forest Virus Deposited 2024-11-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: 12-meric	Chain a 816–1253（438 aa） Chain d 816–1253（438 aa） Chain g 816–1253（438 aa） Chain j 816–1253（438 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.73 Å

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

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. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	34.99 Å
Radius of gyration Rg (electron density) rg_electron	35.02 Å
Forward intensity I(0) i0	69599700.00
Molecular weight molecular_weight	64833.0 kDa
Excluded volume excluded_volume	80630 Å³
Envelope volume envelope_volume	111940 Å³
Hydration-shell volume shell_volume	29546 Å³
Envelope diameter envelope_diameter	121.3 Å
Shell Rg shell_rg	37.49 Å
Envelope Rg envelope_rg	34.54 Å
Shape Rg shape_rg	34.99 Å
Total Rg total_rg	35.31 Å
Total atoms total_atoms	4563
Residues n_residues	596
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	117.3 Å
Rg (real space) rg_real	35.14 Å
Rg uncertainty (real space) rg_real_error	1.34 Å
I(0) (real space) i0_real	6.9600e+07
I(0) uncertainty (real space) i0_real_error	1.2790e+06
Rg (reciprocal space) rg_reciprocal	35.05 Å
I(0) (reciprocal space) i0_reciprocal	69590000.0000
Solution quality estimate total_estimate	0.8303
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	49.5 Å
Skewness Skewness skewness	0.319
Kurtosis Kurtosis kurtosis	-0.483
Angular range angular_range	— – 0.2250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	6672000.0000
Real-space data points n_real_points	46
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.665

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. 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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8. Citations (1)

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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测定方法 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

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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

fit	/app/data/saxs_computation/dy/1dyl/1dyl.fit
pddf	/app/data/pr_computation/dy/1dyl/1dyl.pr.out
profile	/app/data/saxs_computation/dy/1dyl/1dyl.dat