SAXSdb — 9c8i

▼

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

VP1

Human enterovirus D68

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 heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric（240） Consistent with protein copy count	Chain A； UniProt 565–859	Not recorded	VP2 × 60 （A0A6B7FIF3） VP3 × 60 （A0A1L7H9D2） VP4 × 60 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 565–859	Not recorded	VP2 × 1 （A0A6B7FIF3） VP3 × 1 （A0A1L7H9D2） VP4 × 1 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain A； UniProt 565–859	Not recorded	VP2 × 5 （A0A6B7FIF3） VP3 × 5 （A0A1L7H9D2） VP4 × 5 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 565–859	Not recorded	VP2 × 6 （A0A6B7FIF3） VP3 × 6 （A0A1L7H9D2） VP4 × 6 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 565–859	Not recorded	VP2 × 1 （A0A6B7FIF3） VP3 × 1 （A0A1L7H9D2） VP4 × 1 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 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 9C8I	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain A 565–859（295 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 565–859（295 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain A 565–859（295 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 565–859（295 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 565–859（295 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å

1 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A5B9NJ24_HED68
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–295； UniProt 565–859

VP2

Human enterovirus D68

UniProt A0A6B7FIF3

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 heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric（240） Consistent with protein copy count	Chain B； UniProt 70–317	Not recorded	VP1 × 60 （A0A5B9NJ24） VP3 × 60 （A0A1L7H9D2） VP4 × 60 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 70–317	Not recorded	VP1 × 1 （A0A5B9NJ24） VP3 × 1 （A0A1L7H9D2） VP4 × 1 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain B； UniProt 70–317	Not recorded	VP1 × 5 （A0A5B9NJ24） VP3 × 5 （A0A1L7H9D2） VP4 × 5 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain B； UniProt 70–317	Not recorded	VP1 × 6 （A0A5B9NJ24） VP3 × 6 （A0A1L7H9D2） VP4 × 6 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain B； UniProt 70–317	Not recorded	VP1 × 1 （A0A5B9NJ24） VP3 × 1 （A0A1L7H9D2） VP4 × 1 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 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 9C8I	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain B 70–317（248 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 70–317（248 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain B 70–317（248 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain B 70–317（248 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 70–317（248 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å

1 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A6B7FIF3_HED68
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–248； UniProt 70–317

VP3

Human enterovirus D68

UniProt A0A1L7H9D2

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 heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric（240） Consistent with protein copy count	Chain C； UniProt 318–564	Not recorded	VP1 × 60 （A0A5B9NJ24） VP2 × 60 （A0A6B7FIF3） VP4 × 60 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 318–564	Not recorded	VP1 × 1 （A0A5B9NJ24） VP2 × 1 （A0A6B7FIF3） VP4 × 1 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain C； UniProt 318–564	Not recorded	VP1 × 5 （A0A5B9NJ24） VP2 × 5 （A0A6B7FIF3） VP4 × 5 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain C； UniProt 318–564	Not recorded	VP1 × 6 （A0A5B9NJ24） VP2 × 6 （A0A6B7FIF3） VP4 × 6 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 318–564	Not recorded	VP1 × 1 （A0A5B9NJ24） VP2 × 1 （A0A6B7FIF3） VP4 × 1 （A0A4P8L6Q8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 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 9C8I	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
11LT Cryo-EM structure of EV-D68 B3 VLP bound by neutralizing antibody 1E11 Deposited 2026-03-03	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.63 Å
11OV Cryo-EM structure of EV-D68 B3 VLP bound by neutralizing antibody 5H03 Deposited 2026-03-06	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
9C8F Cryo-EM Structure of EV-D68 B3 A-Particle Deposited 2024-06-12	Different oligomeric state Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 318–564（247 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å

3 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A1L7H9D2_HED68
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–247； UniProt 318–564

VP4

Human enterovirus D68

UniProt A0A4P8L6Q8

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 heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric（240） Consistent with protein copy count	Chain D； UniProt 1–69	Not recorded	VP1 × 60 （A0A5B9NJ24） VP2 × 60 （A0A6B7FIF3） VP3 × 60 （A0A1L7H9D2）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain D； UniProt 1–69	Not recorded	VP1 × 1 （A0A5B9NJ24） VP2 × 1 （A0A6B7FIF3） VP3 × 1 （A0A1L7H9D2）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric（20） Consistent with protein copy count	Chain D； UniProt 1–69	Not recorded	VP1 × 5 （A0A5B9NJ24） VP2 × 5 （A0A6B7FIF3） VP3 × 5 （A0A1L7H9D2）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain D； UniProt 1–69	Not recorded	VP1 × 6 （A0A5B9NJ24） VP2 × 6 （A0A6B7FIF3） VP3 × 6 （A0A1L7H9D2）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain D； UniProt 1–69	Not recorded	VP1 × 1 （A0A5B9NJ24） VP2 × 1 （A0A6B7FIF3） VP3 × 1 （A0A1L7H9D2）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	A0A4P8L6Q8_HED68
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–69； UniProt 1–69

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9c8i
Deposition date deposition_date	2024-06-12
Structure title title	Cryo-EM Structure of EV-D68 B3 Inactivated Virus Particle
Keywords keywords	EV-D68, B3 subclade, VLP, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
Experimental Method method	ELECTRON MICROSCOPY

▼

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

Radius of gyration Rg (Guinier) rg_guinier	28.42 Å
Radius of gyration Rg (electron density) rg_electron	27.51 Å
Forward intensity I(0) i0	128465000.00
Molecular weight molecular_weight	89703.0 kDa
Excluded volume excluded_volume	112120 Å³
Envelope volume envelope_volume	131090 Å³
Hydration-shell volume shell_volume	38495 Å³
Envelope diameter envelope_diameter	95.6 Å
Shell Rg shell_rg	35.91 Å
Envelope Rg envelope_rg	28.33 Å
Shape Rg shape_rg	27.50 Å
Total Rg total_rg	28.33 Å
Total atoms total_atoms	6312
Residues n_residues	809
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

▼

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

Maximum dimension Dmax dmax	90.8 Å
Rg (real space) rg_real	28.36 Å
Rg uncertainty (real space) rg_real_error	0.53 Å
I(0) (real space) i0_real	1.2850e+08
I(0) uncertainty (real space) i0_real_error	1.8340e+06
Rg (reciprocal space) rg_reciprocal	28.38 Å
I(0) (reciprocal space) i0_reciprocal	128500000.0000
Solution quality estimate total_estimate	0.6839
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.1 Å
Skewness Skewness skewness	0.335
Kurtosis Kurtosis kurtosis	-0.298
Angular range angular_range	— – 0.2800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	24630000.0000
Real-space data points n_real_points	57
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 0.109; Positv: 1.000; Valcen: 1.000; Smooth: 0.890

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	VP1
Molecular weight formula_weight	32795.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	6312

IESIIKTATDTVKSEINAELGVVPSLNAVETGATSNTEPEEAIQTRTVINQHGVSETLVENFLSRAALVSKRSFEYKDHTSSTAQTDKNFFKWTINTRSFVQLRRKLELFTYLRFDAEITILTTVAVNGSNNNTYVGLPDLTLQAMFVPTGALTPEKQDSFHWQSGSNASVFFKISDPPARMTIPFMCINSAYSVFYDGFAGFEKTGLYGINPADTIGNLCVRIVNEHQPVGFTVTVRVYMKPKHIKAWAPRPPRTLPYMSIANANYKGKERAPNALNAIIGNRDSVKTMPHNIV

来源 Source

来源生物 organism	Human enterovirus D68
通用名 common_name	EV68, EV-68
NCBI Class编号 ncbi_taxonomy_id	42789
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	VP2
Molecular weight formula_weight	27568.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SPSAEACGYSDRVLQLKLGNSAIVTQEAANYCCAYGEWPNYLPDHEAVAIDKPTQPETATDRFYTLRSVKWEATSTGWWWKLPDALNNIGMFGQNVQHHYLYRSGFLIHVQCNATKFHQGALLVVAIPEHQRGAHNTTTSPGFDDIMKGEAGGTFNHPYVLDDGTSLACATIFPHQWINLRTNNSATIVLPWMNAAPMDFPLRHNQWTLAIIPVVPLGTRTMSSMVPITVSIAPMCCEFNGLRHAITQ

来源 Source

来源生物 organism	Human enterovirus D68
通用名 common_name	EV68, EV-68
NCBI Class编号 ncbi_taxonomy_id	42789
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	VP3
Molecular weight formula_weight	27170.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

GVPTYLLPGSGQFLTTDDHSSAPVLPCFNPTPEMHIPGQVRNMLEVVQVESMMEINNTESAVGMERLKVDISALTDVDQLLFNIPLDIQLDGPLRNTLVGNISRYYTHWSGSLEMTFMFCGSFMATGKLILCYTPPGGSCPTTRETAMLGTHIVWDFGLQSSITLIIPWISGSHYRMFNNDAKSTNANVGYVTCFMQTNLIVPSESSDTCSLIGFIAAKDDFSLRLMRDSPDIGQIDHLHGAEAAYQ

来源 Source

来源生物 organism	Human enterovirus D68
通用名 common_name	EV68, EV-68
NCBI Class编号 ncbi_taxonomy_id	42789
宿主生物 host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	VP4
Molecular weight formula_weight	7454.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MGAQVTRQQTGTHENANVATNGSHITYNQINFYKDSYAASASKQDFSQDPSKFTEPVVEGLKAGAPVLK

来源 Source

来源生物 organism	Human enterovirus D68
通用名 common_name	EV68, EV-68
NCBI Class编号 ncbi_taxonomy_id	42789
宿主生物 host_organism	Homo sapiens

▶

8. Citations (1)

▶

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	—

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

Resolution resolution	2.73 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	1700

fit	/app/data/saxs_computation/c8/9c8i/9c8i.fit
pddf	/app/data/pr_computation/c8/9c8i/9c8i.pr.out
profile	/app/data/saxs_computation/c8/9c8i/9c8i.dat

Cryo-EM Structure of EV-D68 B3 Inactivated Virus Particle

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

VP1

State in the Current Structure

Other States of the Same Protein in the Database

VP2

State in the Current Structure

Other States of the Same Protein in the Database

VP3

State in the Current Structure

Other States of the Same Protein in the Database

VP4

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)