SAXSdb — 8ua9

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

Envelope glycoprotein E1

Eastern equine encephalitis virus

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 × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain A； UniProt 802–1242 Chain B； UniProt 325–742 Chain D； UniProt 1–261 Chain E； UniProt 802–1242 Chain F； UniProt 325–742 Chain H； UniProt 1–261 Chain I； UniProt 802–1242 Chain J； UniProt 325–742 Chain L； UniProt 1–261 Chain M； UniProt 802–1242 Chain N； UniProt 325–742 Chain P； UniProt 1–261	Fragment：UNP residues 325-744	Structural polyprotein × 4 （P08768） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.00 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 8UA9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 720 PDB declaration: 720-meric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 4.20 Å
6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 4.20 Å
6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 4.20 Å
6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 72 PDB declaration: 72-meric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 4.20 Å
6XO4 CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 4.20 Å
6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 1200 PDB declaration: 1200-meric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 8.50 Å
6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 8.50 Å
6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 100 PDB declaration: 100-meric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 8.50 Å
6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 120 PDB declaration: 120-meric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 8.50 Å
6XOB CryoEM structure of Eastern Equine Encephalitis (EEEV) VLP with Fab EEEV-143. Deposited 2020-07-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；blot time 2.5s blot force 9	Resolution 8.50 Å
8DWO Cryo-EM Structure of Eastern Equine Encephalitis Virus in complex with SKE26 Fab Deposited 2022-08-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain F 802–1242（441 aa） Chain G 325–744（420 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
8UA4 Structure of eastern equine encephalitis virus VLP in complex with VLDLR LA1 Deposited 2023-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain A 802–1242（441 aa） Chain B 325–744（420 aa） Chain C 1–261（261 aa） Chain D 802–1242（441 aa） Chain E 325–744（420 aa） Chain F 1–261（261 aa） Chain G 802–1242（441 aa） Chain H 325–744（420 aa） Chain I 1–261（261 aa） Chain J 802–1242（441 aa） Chain K 325–744（420 aa） Chain L 1–261（261 aa）	Mutation：K67N Mutation：K67N Mutation：K67N Mutation：K67N	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å
8UFA Eastern equine encephalitis virus (PE-6) VLP (asymmetric unit) Deposited 2023-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain B 325–738（414 aa） Fragment：UNP residues 325-738 Chain D 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain E 325–738（414 aa） Fragment：UNP residues 325-738 Chain G 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain H 325–738（414 aa） Fragment：UNP residues 325-738 Chain J 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain K 325–738（414 aa） Fragment：UNP residues 325-738	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.86 Å
8UFB Eastern equine encephalitis virus (PE-6) VLP in complex with full-length VLDLR (asymmetric unit) Deposited 2023-10-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric	Chain A 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain B 325–738（414 aa） Fragment：UNP residues 325-738 Chain D 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain E 325–738（414 aa） Fragment：UNP residues 325-738 Chain G 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain H 325–738（414 aa） Fragment：UNP residues 325-738 Chain J 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain K 325–738（414 aa） Fragment：UNP residues 325-738	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 12	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.89 Å
8UFC Eastern equine encephalitis virus (PE-6) VLP in complex with VLDLR LA(1-2) (asymmetric unit) Deposited 2023-10-04	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: hexadecameric	Chain A 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain B 325–738（414 aa） Fragment：UNP residues 325-738 Chain D 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain E 325–738（414 aa） Fragment：UNP residues 325-738 Chain G 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain H 325–738（414 aa） Fragment：UNP residues 325-738 Chain J 802–1242（441 aa） Fragment：UNP residues 802-1242 Chain K 325–738（414 aa） Fragment：UNP residues 325-738	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å

7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q88678_EEEV
Isoform	—
PDB entities	1, 2, 4
Chains and sequence ranges	Author chain A； PDBConstruct 1–441； UniProt 802–1242 Author chain E； PDBConstruct 1–441； UniProt 802–1242 Author chain I； PDBConstruct 1–441； UniProt 802–1242 Author chain M； PDBConstruct 1–441； UniProt 802–1242 Author chain B； PDBConstruct 1–418； UniProt 325–742 Author chain F； PDBConstruct 1–418； UniProt 325–742 Author chain J； PDBConstruct 1–418； UniProt 325–742 Author chain N； PDBConstruct 1–418； UniProt 325–742 Author chain D； PDBConstruct 1–260； UniProt 1–261 Author chain H； PDBConstruct 1–260； UniProt 1–261 Author chain L； PDBConstruct 1–260； UniProt 1–261 Author chain P； PDBConstruct 1–260； UniProt 1–261

Structural polyprotein

Eastern equine encephalitis virus

UniProt P08768

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 × 16 PDB declaration: hexadecameric（16） Consistent with protein copy count	Chain C； UniProt 263–316 Chain G； UniProt 263–316 Chain K； UniProt 263–316 Chain O； UniProt 263–316	Not recorded	Envelope glycoprotein E1 × 4 （Q88678） Structural polyprotein × 4 （Q88678） Capsid protein × 4 （Q88678） NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.2 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.00 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 8UA9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8UA4 Structure of eastern equine encephalitis virus VLP in complex with VLDLR LA1 Deposited 2023-09-20	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 17 PDB declaration: heptadecameric	Chain M 260–322（63 aa） Chain N 260–322（63 aa） Chain O 260–322（63 aa） Chain P 260–322（63 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å

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

View Construct and Data Evidence

UniProt name	POLS_EEEV
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–54； UniProt 263–316 Author chain G； PDBConstruct 1–54； UniProt 263–316 Author chain K； PDBConstruct 1–54； UniProt 263–316 Author chain O； PDBConstruct 1–54； UniProt 263–316

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	8ua9
Deposition date deposition_date	2023-09-20
Structure title title	Structure of eastern equine encephalitis virus VLP unliganded quasi-threefold spike protein
Keywords keywords	Eastern Equine Encephalitis Virus, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
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	65.62 Å
Radius of gyration Rg (electron density) rg_electron	65.22 Å
Forward intensity I(0) i0	3148860000.00
Molecular weight molecular_weight	471040.0 kDa
Excluded volume excluded_volume	588300 Å³
Envelope volume envelope_volume	1015100 Å³
Hydration-shell volume shell_volume	129680 Å³
Envelope diameter envelope_diameter	211.4 Å
Shell Rg shell_rg	67.92 Å
Envelope Rg envelope_rg	62.38 Å
Shape Rg shape_rg	65.18 Å
Total Rg total_rg	65.42 Å
Total atoms total_atoms	33106
Residues n_residues	4256
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	208.6 Å
Rg (real space) rg_real	65.32 Å
Rg uncertainty (real space) rg_real_error	1.54 Å
I(0) (real space) i0_real	3.1490e+09
I(0) uncertainty (real space) i0_real_error	5.7890e+07
Rg (reciprocal space) rg_reciprocal	65.83 Å
I(0) (reciprocal space) i0_reciprocal	3152000000.0000
Solution quality estimate total_estimate	0.8709
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	78.2 Å
Skewness Skewness skewness	0.104
Kurtosis Kurtosis kurtosis	-0.625
Angular range angular_range	— – 0.1200 Å⁻¹
Current regularization parameter α current_alpha	0.0002
Highest regularization parameter α highest_alpha	132100000.0000
Real-space data points n_real_points	25
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.473

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Envelope glycoprotein E1
Molecular weight formula_weight	47984.2 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,E,I,M
Atom count atom_count	33106

YEHTAVMPNKVGIPYKALVERPGYAPVHLQIQLVNTRIIPSTNLEYITCKYKTKVPSPVVKCCGATQCTSKPHPDYQCQVFSGVYPFMWGGAYCFCDTENTQMSEAYVERSEECSIDHAKAYKVHTGTVQAMVNITYGSVSWRSADVYVNGETPAKIGDAKLIIGPLSSAWSPFDNKVVVYGHEVYNYDFPEYGTGKAGSFGDLQSRTSTSNDLYANTNLKLQRPQAGIVHTPFTQVPSGFERWKKDKGAPLNDVAPFGCSIALEPLRAENCAVGSIPISIDIPDAAFTRISETPTVSDLECKITECTYAFDFGGIATVAYKSSKAGNCPIHSPSGVAVIKENDVTLAESGSFTFHFSTANIHPAFKLQVCTSAVTCKGDCKPPKDHIVDYPAQHTESFTSAISATAWSWIKVLVGGTSAFIVLGLIATAVVALVLFFHRH

来源 Source

来源生物 organism	Eastern equine encephalitis virus
NCBI Class编号 ncbi_taxonomy_id	11021
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Structural polyprotein
Molecular weight formula_weight	46818.7 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,F,J,N

DLDTHFTQYKLARPYIADCPNCGHSRCDSPIAIEEVRGDAHAGVIRIQTSAMFGLKTDGVDLAYMSFMNGKTQKSIKIDNLHVRTSAPCSLVSHHGYYILAQCPPGDTVTVGFHDGPNRHTCTVAHKVEFRPVGREKYRHPPEHGVELPCNRYTHKRADQGHYVEMHQPGLVADHSLLSIHSAKVKITVPSGAQVKYYCKCPDVRKGITSSDHTTTCTDVKQCRAYLIDNKKWVYNSGRLPRGEGDTFKGKLHVPFVPVKAKCIATLAPEPLVEHKHRTLILHLHPDHPTLLTTRSLGSDANPTRQWIERPTTVNFTVTGEGLEYTWGNHPPKRVWAQESGEGNPHGWPHEVVVYYYNRYPLTTIIGLCTCVAIIMVSCVTSVWLLCRTRNLCITPYKLAPNAQVPILLALLCCIKPT

来源 Source

来源生物 organism	Eastern equine encephalitis virus
NCBI Class编号 ncbi_taxonomy_id	11021
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	Structural polyprotein
Molecular weight formula_weight	6147.1 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,G,K,O

TVMCVLANITFPCDQPPCMPCCYEKNPHETLTMLEQNYDSRAYDQLLDAAVKCN

来源 Source

来源生物 organism	Eastern equine encephalitis virus
NCBI Class编号 ncbi_taxonomy_id	11021
宿主生物 host_organism	Homo sapiens

Entity 4 Entity 4 polymer

Description description	Capsid protein
Molecular weight formula_weight	29212.9 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,H,L,P

MFPYPTLNYPPMAPINPMAYRDPNPPRRRWRPFRPPLAAQIEDLRRSIANLTLKQRAPNPPAGPPAKRKKPAPSLSLRRKKKRPPPPAKKQKRKPKPGKRQRMCMKLESDKTFPIMLNGQVNGYACVVGGRVFKPLHVEGRIDNEQLAAIKLKKASIYDLEYGDVPQCMKSDTLQYTSDKPPGFYNWHHGAVQYENNRFTVPRGVGGKGDSGRPILDNKGRVVAIVLGGVNEGSRTALSVVTWNQKGVTVKDTPEGSEPW

来源 Source

来源生物 organism	Eastern equine encephalitis virus
NCBI Class编号 ncbi_taxonomy_id	11021
宿主生物 host_organism	Homo sapiens

Entity 5 Entity 5 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	9

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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	—

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

Resolution resolution	3.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	432897

fit	/app/data/saxs_computation/ua/8ua9/8ua9.fit
pddf	/app/data/pr_computation/ua/8ua9/8ua9.pr.out
profile	/app/data/saxs_computation/ua/8ua9/8ua9.dat

Structure of eastern equine encephalitis virus VLP unliganded quasi-threefold spike protein

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

Envelope glycoprotein E1

State in the Current Structure

Other States of the Same Protein in the Database

Structural polyprotein

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 (5)

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

Entity 5 Entity 5 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)