SAXSdb — 6hht

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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 × 150 PDB declaration: 150-meric（150） Consistent with protein copy count	Chain A1； UniProt 569–855 Chain A2； UniProt 569–855 Chain B1； UniProt 70–329 Chain B2； UniProt 70–329 Chain C1； UniProt 330–568 Chain C2； UniProt 330–568 Chain D1； UniProt 569–855 Chain D2； UniProt 569–855 Chain E1； UniProt 70–329 Chain E2； UniProt 70–329 Chain F1； UniProt 330–568 Chain F2； UniProt 330–568 Chain G1； UniProt 569–855 Chain G2； UniProt 569–855 Chain H1； UniProt 70–329 Chain H2； UniProt 70–329 Chain I1； UniProt 330–568 Chain I2； UniProt 330–568 Chain J1； UniProt 569–855 Chain J2； UniProt 569–855 Chain K1； UniProt 70–329 Chain K2； UniProt 70–329 Chain L1； UniProt 330–568 Chain L2； UniProt 330–568 Chain M1； UniProt 569–855 Chain M2； UniProt 569–855 Chain N1； UniProt 70–329 Chain N2； UniProt 70–329 Chain O1； UniProt 330–568 Chain O2； UniProt 330–568 Chain P1； UniProt 569–855 Chain P2； UniProt 569–855 Chain Q1； UniProt 70–329 Chain Q2； UniProt 70–329 Chain R1； UniProt 330–568 Chain R2； UniProt 330–568 Chain S1； UniProt 569–855 Chain S2； UniProt 569–855 Chain T1； UniProt 70–329 Chain T2； UniProt 70–329 Chain U1； UniProt 330–568 Chain U2； UniProt 330–568 Chain V1； UniProt 569–855 Chain V2； UniProt 569–855 Chain W1； UniProt 70–329 Chain W2； UniProt 70–329 Chain X1； UniProt 330–568 Chain X2； UniProt 330–568 Chain Y2； UniProt 569–855 Chain Z2； UniProt 70–329 Chain a2； UniProt 330–568 Chain b2； UniProt 569–855 Chain c2； UniProt 70–329 Chain d2； UniProt 330–568 Chain e2； UniProt 569–855 Chain f2； UniProt 70–329 Chain g2； UniProt 330–568 Chain h2； UniProt 569–855 Chain i2； UniProt 70–329 Chain j2； UniProt 330–568 Chain k2； UniProt 569–855 Chain l2； UniProt 70–329 Chain m2； UniProt 330–568 Chain n2； UniProt 569–855 Chain o2； UniProt 70–329 Chain p2； UniProt 330–568 Chain q2； UniProt 569–855 Chain r2； UniProt 70–329 Chain s2； UniProt 330–568 Chain t2； UniProt 569–855 Chain u2； UniProt 70–329 Chain v2； UniProt 330–568 Chain w2； UniProt 569–855 Chain x2； UniProt 70–329 Chain y2； UniProt 330–568	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 6 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.05 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 6HHT	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
6HBL Echovirus 18 Open particle without three pentamers Deposited 2018-08-10	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 135 PDB declaration: 45-meric	Chain A 569–855（287 aa） Chain B 70–329（260 aa） Chain C 330–568（239 aa） Chain D 569–855（287 aa） Chain E 70–329（260 aa） Chain F 330–568（239 aa） Chain G 569–855（287 aa） Chain H 70–329（260 aa） Chain I 330–568（239 aa） Chain J 569–855（287 aa） Chain K 70–329（260 aa） Chain L 330–568（239 aa） Chain M 569–855（287 aa） Chain N 70–329（260 aa） Chain O 330–568（239 aa） Chain P 569–855（287 aa） Chain Q 70–329（260 aa） Chain R 330–568（239 aa） Chain S 569–855（287 aa） Chain T 70–329（260 aa） Chain U 330–568（239 aa） Chain V 569–855（287 aa） Chain W 70–329（260 aa） Chain X 330–568（239 aa） Chain Y 569–855（287 aa） Chain Z 70–329（260 aa） Chain a 330–568（239 aa） Chain b 569–855（287 aa） Chain c 70–329（260 aa） Chain d 330–568（239 aa） Chain e 569–855（287 aa） Chain f 70–329（260 aa） Chain g 330–568（239 aa） Chain h 569–855（287 aa） Chain i 70–329（260 aa） Chain j 330–568（239 aa） Chain k 569–855（287 aa） Chain l 70–329（260 aa） Chain m 330–568（239 aa） Chain n 569–855（287 aa） Chain o 70–329（260 aa） Chain p 330–568（239 aa） Chain q 569–855（287 aa） Chain r 70–329（260 aa） Chain s 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 3.70 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 A1； PDBConstruct 1–287； UniProt 569–855 Author chain A2； PDBConstruct 1–287； UniProt 569–855 Author chain D1； PDBConstruct 1–287； UniProt 569–855 Author chain D2； PDBConstruct 1–287； UniProt 569–855 Author chain G1； PDBConstruct 1–287； UniProt 569–855 Author chain G2； PDBConstruct 1–287； UniProt 569–855 Author chain J1； PDBConstruct 1–287； UniProt 569–855 Author chain J2； PDBConstruct 1–287； UniProt 569–855 Author chain M1； PDBConstruct 1–287； UniProt 569–855 Author chain M2； PDBConstruct 1–287； UniProt 569–855 Author chain P1； PDBConstruct 1–287； UniProt 569–855 Author chain P2； PDBConstruct 1–287； UniProt 569–855 Author chain S1； PDBConstruct 1–287； UniProt 569–855 Author chain S2； PDBConstruct 1–287； UniProt 569–855 Author chain V1； PDBConstruct 1–287； UniProt 569–855 Author chain V2； PDBConstruct 1–287； UniProt 569–855 Author chain Y2； PDBConstruct 1–287； UniProt 569–855 Author chain b2； PDBConstruct 1–287； UniProt 569–855 Author chain e2； PDBConstruct 1–287； UniProt 569–855 Author chain h2； PDBConstruct 1–287； UniProt 569–855 Author chain k2； PDBConstruct 1–287； UniProt 569–855 Author chain n2； PDBConstruct 1–287； UniProt 569–855 Author chain q2； PDBConstruct 1–287； UniProt 569–855 Author chain t2； PDBConstruct 1–287； UniProt 569–855 Author chain w2； PDBConstruct 1–287； UniProt 569–855 Author chain B1； PDBConstruct 1–260； UniProt 70–329 Author chain B2； PDBConstruct 1–260； UniProt 70–329 Author chain E1； PDBConstruct 1–260； UniProt 70–329 Author chain E2； PDBConstruct 1–260； UniProt 70–329 Author chain H1； PDBConstruct 1–260； UniProt 70–329 Author chain H2； PDBConstruct 1–260； UniProt 70–329 Author chain K1； PDBConstruct 1–260； UniProt 70–329 Author chain K2； PDBConstruct 1–260； UniProt 70–329 Author chain N1； PDBConstruct 1–260； UniProt 70–329 Author chain N2； PDBConstruct 1–260； UniProt 70–329 Author chain Q1； PDBConstruct 1–260； UniProt 70–329 Author chain Q2； PDBConstruct 1–260； UniProt 70–329 Author chain T1； PDBConstruct 1–260； UniProt 70–329 Author chain T2； PDBConstruct 1–260； UniProt 70–329 Author chain W1； PDBConstruct 1–260； UniProt 70–329 Author chain W2； PDBConstruct 1–260； UniProt 70–329 Author chain Z2； PDBConstruct 1–260； UniProt 70–329 Author chain c2； PDBConstruct 1–260； UniProt 70–329 Author chain f2； PDBConstruct 1–260； UniProt 70–329 Author chain i2； PDBConstruct 1–260； UniProt 70–329 Author chain l2； PDBConstruct 1–260； UniProt 70–329 Author chain o2； PDBConstruct 1–260； UniProt 70–329 Author chain r2； PDBConstruct 1–260； UniProt 70–329 Author chain u2； PDBConstruct 1–260； UniProt 70–329 Author chain x2； PDBConstruct 1–260； UniProt 70–329 Author chain C1； PDBConstruct 1–239； UniProt 330–568 Author chain C2； PDBConstruct 1–239； UniProt 330–568 Author chain F1； PDBConstruct 1–239； UniProt 330–568 Author chain F2； PDBConstruct 1–239； UniProt 330–568 Author chain I1； PDBConstruct 1–239； UniProt 330–568 Author chain I2； PDBConstruct 1–239； UniProt 330–568 Author chain L1； PDBConstruct 1–239； UniProt 330–568 Author chain L2； PDBConstruct 1–239； UniProt 330–568 Author chain O1； PDBConstruct 1–239； UniProt 330–568 Author chain O2； PDBConstruct 1–239； UniProt 330–568 Author chain R1； PDBConstruct 1–239； UniProt 330–568 Author chain R2； PDBConstruct 1–239； UniProt 330–568 Author chain U1； PDBConstruct 1–239； UniProt 330–568 Author chain U2； PDBConstruct 1–239； UniProt 330–568 Author chain X1； PDBConstruct 1–239； UniProt 330–568 Author chain X2； PDBConstruct 1–239； UniProt 330–568 Author chain a2； PDBConstruct 1–239； UniProt 330–568 Author chain d2； PDBConstruct 1–239； UniProt 330–568 Author chain g2； PDBConstruct 1–239； UniProt 330–568 Author chain j2； PDBConstruct 1–239； UniProt 330–568 Author chain m2； PDBConstruct 1–239； UniProt 330–568 Author chain p2； PDBConstruct 1–239； UniProt 330–568 Author chain s2； PDBConstruct 1–239； UniProt 330–568 Author chain v2； PDBConstruct 1–239； UniProt 330–568 Author chain y2； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6hht
Deposition date deposition_date	2018-08-29
Structure title title	Echovirus 18 Open particle without two pentamers
Keywords keywords	echovirus, echovirus 18, open particle, O-particle, enterovirus, picornavirus, VIRUS, genome release; 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	— Å
Radius of gyration Rg (electron density) rg_electron	124.40 Å
Forward intensity I(0) i0	45365900000.00
Molecular weight molecular_weight	1848500.0 kDa
Excluded volume excluded_volume	2318600 Å³
Envelope volume envelope_volume	5375800 Å³
Hydration-shell volume shell_volume	372020 Å³
Envelope diameter envelope_diameter	330.2 Å
Shell Rg shell_rg	126.70 Å
Envelope Rg envelope_rg	110.40 Å
Shape Rg shape_rg	124.30 Å
Total Rg total_rg	124.40 Å
Total atoms total_atoms	129900
Residues n_residues	17000
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	348.7 Å
Rg (real space) rg_real	125.40 Å
Rg uncertainty (real space) rg_real_error	1.42 Å
I(0) (real space) i0_real	4.4840e+10
I(0) uncertainty (real space) i0_real_error	8.9190e+08
Rg (reciprocal space) rg_reciprocal	122.50 Å
I(0) (reciprocal space) i0_reciprocal	44670000000.0000
Solution quality estimate total_estimate	0.9040
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	145.3 Å
Skewness Skewness skewness	-0.054
Kurtosis Kurtosis kurtosis	-0.984
Angular range angular_range	— – 0.0600 Å⁻¹
Current regularization parameter α current_alpha	1.2010
Highest regularization parameter α highest_alpha	566200000.0000
Real-space data points n_real_points	13
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.996; Stabil: 0.928; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; 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	25

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A1,V1,S1,P1,M1,J1,G1,D1,A2,w2,t2,q2,n2,k2,h2,e2,b2,Y2,V2,S2,P2,M2,J2,G2,D2
Atom count atom_count	129900

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	25

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	W1,T1,Q1,N1,K1,H1,E1,B1,x2,u2,r2,o2,l2,i2,f2,c2,Z2,W2,T2,Q2,N2,K2,H2,E2,B2

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	25

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X1,U1,R1,O1,L1,I1,F1,C1,y2,v2,s2,p2,m2,j2,g2,d2,a2,X2,U2,R2,O2,L2,I2,F2,C2

GVPVLNTPGSNQFLTSDDYQSPSAMPQFDETPEMHIPGEVRNLMEIAEVDSVVPVNNVTGKTKSMDAYQIPVGTGNTDKTKPIFSFQMDPGYSSVLKRTLLGEMLNYYAHWSGSVKLTFLFCGSAMATGKLLISYSPPGASVPTSRKDAMLGTHIVWDIGLQSSCVLCVPWISQSHYRMVQQDPYTSAGYITCWYQTNIVVPPGAPTSCDVLCFASACNDFSVRLLRDTPFMAQPGKLQ

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8. Citations (1)

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Resolution resolution	4.05 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	7635

fit	/app/data/saxs_computation/hh/6hht/6hht.fit
pddf	/app/data/pr_computation/hh/6hht/6hht.pr.out
profile	/app/data/saxs_computation/hh/6hht/6hht.dat

Echovirus 18 Open particle without two 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

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)