6hbl

Echovirus 18 Open particle without three pentamers

Method: ELECTRON MICROSCOPY D_max: 267.2 Å Quality: GOOD

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

Echovirus 18 capsid protein 1

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 × 135 PDB declaration: 45-meric（45） Count mismatch; review required	Chain A； UniProt 569–855 Chain B； UniProt 70–329 Chain C； UniProt 330–568 Chain D； UniProt 569–855 Chain E； UniProt 70–329 Chain F； UniProt 330–568 Chain G； UniProt 569–855 Chain H； UniProt 70–329 Chain I； UniProt 330–568 Chain J； UniProt 569–855 Chain K； UniProt 70–329 Chain L； UniProt 330–568 Chain M； UniProt 569–855 Chain N； UniProt 70–329 Chain O； UniProt 330–568 Chain P； UniProt 569–855 Chain Q； UniProt 70–329 Chain R； UniProt 330–568 Chain S； UniProt 569–855 Chain T； UniProt 70–329 Chain U； UniProt 330–568 Chain V； UniProt 569–855 Chain W； UniProt 70–329 Chain X； UniProt 330–568 Chain Y； UniProt 569–855 Chain Z； UniProt 70–329 Chain a； UniProt 330–568 Chain b； UniProt 569–855 Chain c； UniProt 70–329 Chain d； UniProt 330–568 Chain e； UniProt 569–855 Chain f； UniProt 70–329 Chain g； UniProt 330–568 Chain h； UniProt 569–855 Chain i； UniProt 70–329 Chain j； UniProt 330–568 Chain k； UniProt 569–855 Chain l； UniProt 70–329 Chain m； UniProt 330–568 Chain n； UniProt 569–855 Chain o； UniProt 70–329 Chain p； UniProt 330–568 Chain q； UniProt 569–855 Chain r； UniProt 70–329 Chain s； UniProt 330–568	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.70 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 6HBL	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6HBG Echovirus 18 native particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 240 PDB declaration: 240-meric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa） Chain D 1–69（69 aa）	Not recorded	PLM PALMITIC ACID × 60 GUN GUANINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å R-free 0.325
6HBH Echovirus 18 A-particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 180 PDB declaration: 180-meric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å R-free 0.323
6HBH Echovirus 18 A-particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å R-free 0.323
6HBH Echovirus 18 A-particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å R-free 0.323
6HBH Echovirus 18 A-particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å R-free 0.323
6HBH Echovirus 18 A-particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.36 Å R-free 0.323
6HBJ Echovirus 18 empty particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 180 PDB declaration: 180-meric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å R-free 0.336
6HBJ Echovirus 18 empty particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å R-free 0.336
6HBJ Echovirus 18 empty particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å R-free 0.336
6HBJ Echovirus 18 empty particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å R-free 0.336
6HBJ Echovirus 18 empty particle Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 5.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å R-free 0.336
6HBK Echovirus 18 Open particle without one pentamer Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 165 PDB declaration: 165-meric	Chain A 569–855（287 aa） Chain B 70–328（259 aa） Chain C 330–568（239 aa） Chain D 569–855（287 aa） Chain E 70–328（259 aa） Chain F 330–568（239 aa） Chain G 569–855（287 aa） Chain H 70–328（259 aa） Chain I 330–568（239 aa） Chain J 569–855（287 aa） Chain K 70–328（259 aa） Chain L 330–568（239 aa） Chain M 569–855（287 aa） Chain N 70–328（259 aa） Chain O 330–568（239 aa） Chain P 569–855（287 aa） Chain Q 70–328（259 aa） Chain R 330–568（239 aa） Chain S 569–855（287 aa） Chain T 70–328（259 aa） Chain U 330–568（239 aa） Chain V 569–855（287 aa） Chain W 70–328（259 aa） Chain X 330–568（239 aa） Chain Y 569–855（287 aa） Chain Z 70–328（259 aa） Chain a 330–568（239 aa） Chain b 569–855（287 aa） Chain c 70–328（259 aa） Chain d 330–568（239 aa） Chain e 569–855（287 aa） Chain f 70–328（259 aa） Chain g 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
6HHT Echovirus 18 Open particle without two pentamers Deposited 2018-08-29	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 150 PDB declaration: 150-meric	Chain A1 569–855（287 aa） Chain A2 569–855（287 aa） Chain B1 70–329（260 aa） Chain B2 70–329（260 aa） Chain C1 330–568（239 aa） Chain C2 330–568（239 aa） Chain D1 569–855（287 aa） Chain D2 569–855（287 aa） Chain E1 70–329（260 aa） Chain E2 70–329（260 aa） Chain F1 330–568（239 aa） Chain F2 330–568（239 aa） Chain G1 569–855（287 aa） Chain G2 569–855（287 aa） Chain H1 70–329（260 aa） Chain H2 70–329（260 aa） Chain I1 330–568（239 aa） Chain I2 330–568（239 aa） Chain J1 569–855（287 aa） Chain J2 569–855（287 aa） Chain K1 70–329（260 aa） Chain K2 70–329（260 aa） Chain L1 330–568（239 aa） Chain L2 330–568（239 aa） Chain M1 569–855（287 aa） Chain M2 569–855（287 aa） Chain N1 70–329（260 aa） Chain N2 70–329（260 aa） Chain O1 330–568（239 aa） Chain O2 330–568（239 aa） Chain P1 569–855（287 aa） Chain P2 569–855（287 aa） Chain Q1 70–329（260 aa） Chain Q2 70–329（260 aa） Chain R1 330–568（239 aa） Chain R2 330–568（239 aa） Chain S1 569–855（287 aa） Chain S2 569–855（287 aa） Chain T1 70–329（260 aa） Chain T2 70–329（260 aa） Chain U1 330–568（239 aa） Chain U2 330–568（239 aa） Chain V1 569–855（287 aa） Chain V2 569–855（287 aa） Chain W1 70–329（260 aa） Chain W2 70–329（260 aa） Chain X1 330–568（239 aa） Chain X2 330–568（239 aa） Chain Y2 569–855（287 aa） Chain Z2 70–329（260 aa） Chain a2 330–568（239 aa） Chain b2 569–855（287 aa） Chain c2 70–329（260 aa） Chain d2 330–568（239 aa） Chain e2 569–855（287 aa） Chain f2 70–329（260 aa） Chain g2 330–568（239 aa） Chain h2 569–855（287 aa） Chain i2 70–329（260 aa） Chain j2 330–568（239 aa） Chain k2 569–855（287 aa） Chain l2 70–329（260 aa） Chain m2 330–568（239 aa） Chain n2 569–855（287 aa） Chain o2 70–329（260 aa） Chain p2 330–568（239 aa） Chain q2 569–855（287 aa） Chain r2 70–329（260 aa） Chain s2 330–568（239 aa） Chain t2 569–855（287 aa） Chain u2 70–329（260 aa） Chain v2 330–568（239 aa） Chain w2 569–855（287 aa） Chain x2 70–329（260 aa） Chain y2 330–568（239 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.05 Å
7B5F Structure of echovirus 18 in complex with neonatal Fc receptor Deposited 2020-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: Hexameric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa） Chain D 1–69（69 aa）	Not recorded	PLM PALMITIC ACID × 1 GUN GUANINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.3；Mixed in 1:1 volume ratio {20 mM Tris (pH=7.2), 100 mM NaCl} and {8 mM Na2HPO4, 2 mM KH2PO4 (pH=7.4), 137 mM NaCl, 2.7 mM KCl}=PBS cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å R-free 0.311

6 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q8V635_9ENTO
Isoform	—
PDB entities	1, 2, 3
Chains and sequence ranges	Author chain A； PDBConstruct 1–287； UniProt 569–855 Author chain D； PDBConstruct 1–287； UniProt 569–855 Author chain G； PDBConstruct 1–287； UniProt 569–855 Author chain J； PDBConstruct 1–287； UniProt 569–855 Author chain M； PDBConstruct 1–287； UniProt 569–855 Author chain P； PDBConstruct 1–287； UniProt 569–855 Author chain S； PDBConstruct 1–287； UniProt 569–855 Author chain V； PDBConstruct 1–287； UniProt 569–855 Author chain Y； PDBConstruct 1–287； UniProt 569–855 Author chain b； PDBConstruct 1–287； UniProt 569–855 Author chain e； PDBConstruct 1–287； UniProt 569–855 Author chain h； PDBConstruct 1–287； UniProt 569–855 Author chain k； PDBConstruct 1–287； UniProt 569–855 Author chain n； PDBConstruct 1–287； UniProt 569–855 Author chain q； PDBConstruct 1–287； UniProt 569–855 Author chain B； PDBConstruct 1–260； UniProt 70–329 Author chain E； PDBConstruct 1–260； UniProt 70–329 Author chain H； PDBConstruct 1–260； UniProt 70–329 Author chain K； PDBConstruct 1–260； UniProt 70–329 Author chain N； PDBConstruct 1–260； UniProt 70–329 Author chain Q； PDBConstruct 1–260； UniProt 70–329 Author chain T； PDBConstruct 1–260； UniProt 70–329 Author chain W； PDBConstruct 1–260； UniProt 70–329 Author chain Z； PDBConstruct 1–260； UniProt 70–329 Author chain c； PDBConstruct 1–260； UniProt 70–329 Author chain f； PDBConstruct 1–260； UniProt 70–329 Author chain i； PDBConstruct 1–260； UniProt 70–329 Author chain l； PDBConstruct 1–260； UniProt 70–329 Author chain o； PDBConstruct 1–260； UniProt 70–329 Author chain r； PDBConstruct 1–260； UniProt 70–329 Author chain C； PDBConstruct 1–239； UniProt 330–568 Author chain F； PDBConstruct 1–239； UniProt 330–568 Author chain I； PDBConstruct 1–239； UniProt 330–568 Author chain L； PDBConstruct 1–239； UniProt 330–568 Author chain O； PDBConstruct 1–239； UniProt 330–568 Author chain R； PDBConstruct 1–239； UniProt 330–568 Author chain U； PDBConstruct 1–239； UniProt 330–568 Author chain X； PDBConstruct 1–239； UniProt 330–568 Author chain a； PDBConstruct 1–239； UniProt 330–568 Author chain d； PDBConstruct 1–239； UniProt 330–568 Author chain g； PDBConstruct 1–239； UniProt 330–568 Author chain j； PDBConstruct 1–239； UniProt 330–568 Author chain m； PDBConstruct 1–239； UniProt 330–568 Author chain p； PDBConstruct 1–239； UniProt 330–568 Author chain s； PDBConstruct 1–239； UniProt 330–568

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.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6hbl
Deposition date deposition_date	2018-08-10
Structure title title	Echovirus 18 Open particle without three pentamers
Keywords keywords	echovirus, echovirus 18, open particle, O-particle, enterovirus, picornavirus, VIRUS; VIRUS
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	94.69 Å
Radius of gyration Rg (electron density) rg_electron	94.37 Å
Forward intensity I(0) i0	16441200000.00
Molecular weight molecular_weight	1109100.0 kDa
Excluded volume excluded_volume	1391100 Å³
Envelope volume envelope_volume	2425600 Å³
Hydration-shell volume shell_volume	215230 Å³
Envelope diameter envelope_diameter	278.5 Å
Shell Rg shell_rg	93.72 Å
Envelope Rg envelope_rg	88.58 Å
Shape Rg shape_rg	94.36 Å
Total Rg total_rg	94.42 Å
Total atoms total_atoms	77940
Residues n_residues	10200
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	267.2 Å
Rg (real space) rg_real	94.39 Å
Rg uncertainty (real space) rg_real_error	1.54 Å
I(0) (real space) i0_real	1.6440e+10
I(0) uncertainty (real space) i0_real_error	3.5410e+08
Rg (reciprocal space) rg_reciprocal	94.63 Å
I(0) (reciprocal space) i0_reciprocal	16430000000.0000
Solution quality estimate total_estimate	0.8465
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	133.6 Å
Skewness Skewness skewness	0.019
Kurtosis Kurtosis kurtosis	-0.900
Angular range angular_range	— – 0.0800 Å⁻¹
Current regularization parameter α current_alpha	0.0025
Highest regularization parameter α highest_alpha	288700000.0000
Real-space data points n_real_points	17
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 1.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Echovirus 18 capsid protein 1
Molecular weight formula_weight	32564.4 kDa
Source method src_method	nat
Copy count entity_count	15

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,q,n,k,h,e,b,Y,V,S,P,M,J,G,D
Atom count atom_count	77940

GDNQDRTVANTQPSGPSNSTEIPALTAVETGHTSQVDPSDTIQTRHVVNFHSRSESTIENFMGRAACVFMDQYKINGEETSTDRFAVWTINIREMAQLRRKCEMFTYMRFDIEMTMVITSCQDQGTILDQDMPVLTHQIMYVPPGGPIPAKVDGYEWQTSTNPSVFWTEGNAPPRISIPFISVGNAYSSFYDGWSHFTQDGTYGYTTLNAMGKLYIRHVNRSSPHQITSTIRVYFKPKHIKAWVPRPPRLCPYINKRDVNFVVTEITDSRTSITDTPHPEHSVLATH

Entity 2 Entity 2 polymer

Description description	Echovirus 18 capsid protein 2
Molecular weight formula_weight	28802.3 kDa
Source method src_method	nat
Copy count entity_count	15

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	r,o,l,i,f,c,Z,W,T,Q,N,K,H,E,B

SPSAEECGYSDRVRSMTLGNSTITTQESANVVVGYGEWPSYLSDREATAEDQPTQPDVATCRFYTLESVQWEKTSPGWWWKFPEALKNMGLFGQNMHYHYLGRAGYTIHVQCNASKFHQGCLLVVCVPEAEMGCADTDTTFPATELTTEDTPHVFTSDSITGKKVQAAVCNAGMGVGVGNLTIFPHQWINLRTNNSATIVIPYINSVPMDNMFRHYNFTLMIIPFAPLNFTDGATAYVPITVTIAPMYAEYNGLRLASTQ

Entity 3 Entity 3 polymer

Description description	Echovirus 18 capsid protein 3
Molecular weight formula_weight	26143.8 kDa
Source method src_method	nat
Copy count entity_count	15

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	s,p,m,j,g,d,a,X,U,R,O,L,I,F,C

GVPVLNTPGSNQFLTSDDYQSPSAMPQFDETPEMHIPGEVRNLMEIAEVDSVVPVNNVTGKTKSMDAYQIPVGTGNTDKTKPIFSFQMDPGYSSVLKRTLLGEMLNYYAHWSGSVKLTFLFCGSAMATGKLLISYSPPGASVPTSRKDAMLGTHIVWDIGLQSSCVLCVPWISQSHYRMVQQDPYTSAGYITCWYQTNIVVPPGAPTSCDVLCFASACNDFSVRLLRDTPFMAQPGKLQ

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7. Fold Classification (SCOP + CATH) 45 domains

CATH v4.4 (45 domains)

Domain ID domain_id	6hblA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblE00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblF00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblG00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblI00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblJ00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblK00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblL00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblM00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblN00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblO00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblP00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblQ00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblR00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblS00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblT00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblU00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblV00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblW00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblX00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblY00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblZ00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hbla00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblb00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblc00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hbld00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hble00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblf00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblg00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblh00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hbli00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblj00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblk00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hbll00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblm00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hbln00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblo00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblp00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblq00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hblr00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	6hbls00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

▶

8. Citations (1)

▶

Resolution resolution	3.70 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	13635

Echovirus 18 Open particle without three pentamers

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

Echovirus 18 capsid protein 1

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 45 domains

CATH v4.4 (45 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/hb/6hbl/6hbl.fit
pddf	/app/data/pr_computation/hb/6hbl/6hbl.pr.out
profile	/app/data/saxs_computation/hb/6hbl/6hbl.dat