SAXSdb — 8e8s

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

Capsid protein VP1

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 heterocomplex Heteromer Protein × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain 1； UniProt 25–301	Not recorded	Capsid protein VP2 × 60 （A0A0K1U2R1） Capsid protein VP3 × 60 （A0A0K1U2R1） Capsid protein VP4 × 60 （D0QXH8） 9H2 Fab heavy chain × 60 9H2 Fab light chain × 60 PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 1； UniProt 25–301	Not recorded	Capsid protein VP2 × 1 （A0A0K1U2R1） Capsid protein VP3 × 1 （A0A0K1U2R1） Capsid protein VP4 × 1 （D0QXH8） 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 1； UniProt 25–301	Not recorded	Capsid protein VP2 × 5 （A0A0K1U2R1） Capsid protein VP3 × 5 （A0A0K1U2R1） Capsid protein VP4 × 5 （D0QXH8） 9H2 Fab heavy chain × 5 9H2 Fab light chain × 5 PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain 1； UniProt 25–301	Not recorded	Capsid protein VP2 × 6 （A0A0K1U2R1） Capsid protein VP3 × 6 （A0A0K1U2R1） Capsid protein VP4 × 6 （D0QXH8） 9H2 Fab heavy chain × 6 9H2 Fab light chain × 6 PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 1； UniProt 25–301	Not recorded	Capsid protein VP2 × 1 （A0A0K1U2R1） Capsid protein VP3 × 1 （A0A0K1U2R1） Capsid protein VP4 × 1 （D0QXH8） 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 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 8E8S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9H93 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain A 1–301（301 aa）	Mutation：VP1 V107I, VP1 F134L, VP1 V183L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.40 Å
9H94 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC5a) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain A 1–301（301 aa）	Mutation：VP1 T41I, VP1 F134L, VP1 Y159F	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.10 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q8QNU4_9ENTO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain 1； PDBConstruct 1–277； UniProt 25–301

Capsid protein VP2

OrganismNot specified

UniProt A0A0K1U2R1

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 × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain 2； UniProt 79–340 Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 60 （Q8QNU4） Capsid protein VP4 × 60 （D0QXH8） 9H2 Fab heavy chain × 60 9H2 Fab light chain × 60 PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 2； UniProt 79–340 Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 1 （Q8QNU4） Capsid protein VP4 × 1 （D0QXH8） 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 2； UniProt 79–340 Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 5 （Q8QNU4） Capsid protein VP4 × 5 （D0QXH8） 9H2 Fab heavy chain × 5 9H2 Fab light chain × 5 PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain 2； UniProt 79–340 Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 6 （Q8QNU4） Capsid protein VP4 × 6 （D0QXH8） 9H2 Fab heavy chain × 6 9H2 Fab light chain × 6 PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 2； UniProt 79–340 Chain 3； UniProt 341–575	Not recorded	Capsid protein VP1 × 1 （Q8QNU4） Capsid protein VP4 × 1 （D0QXH8） 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 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 8E8S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9H93 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC6b) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain C 341–578（238 aa）	Mutation：VP3 Q178L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.40 Å
9H94 Poliovirus type 2 (strain MEF-1) stabilised virus-like particle (PV2 SC5a) from a yeast expression system. Deposited 2024-10-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 180 PDB declaration: 180-meric	Chain C 341–578（238 aa）	Mutation：VP3 L85F, VP3 Q178L	SPH SPHINGOSINE × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 7；1 x DPBS, 20 mM EDTA, pH 7.0 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；3ul of sample double blotted for 3.5 seconds with -15 blot force on FEI Vitrobot mark IV.	Resolution 2.10 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different construct Different mutation/modification Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-meric	Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different construct Different mutation/modification Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different construct Different mutation/modification Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different construct Different mutation/modification Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different construct Different mutation/modification Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 3 341–575（235 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

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

View Construct and Data Evidence

UniProt name	A0A0K1U2R1_9ENTO
Isoform	—
PDB entities	2, 3
Chains and sequence ranges	Author chain 2； PDBConstruct 1–262； UniProt 79–340 Author chain 3； PDBConstruct 1–235； UniProt 341–575

Capsid protein VP4

OrganismNot specified

UniProt D0QXH8

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 × 360 PDB declaration: 360-meric（360） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 60 （Q8QNU4） Capsid protein VP2 × 60 （A0A0K1U2R1） Capsid protein VP3 × 60 （A0A0K1U2R1） 9H2 Fab heavy chain × 60 9H2 Fab light chain × 60 PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
2	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 1 （Q8QNU4） Capsid protein VP2 × 1 （A0A0K1U2R1） Capsid protein VP3 × 1 （A0A0K1U2R1） 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
3	Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric（30） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 5 （Q8QNU4） Capsid protein VP2 × 5 （A0A0K1U2R1） Capsid protein VP3 × 5 （A0A0K1U2R1） 9H2 Fab heavy chain × 5 9H2 Fab light chain × 5 PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
4	Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric（36） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 6 （Q8QNU4） Capsid protein VP2 × 6 （A0A0K1U2R1） Capsid protein VP3 × 6 （A0A0K1U2R1） 9H2 Fab heavy chain × 6 9H2 Fab light chain × 6 PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.73 Å
5	Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain 4； UniProt 2–69	Not recorded	Capsid protein VP1 × 1 （Q8QNU4） Capsid protein VP2 × 1 （A0A0K1U2R1） Capsid protein VP3 × 1 （A0A0K1U2R1） 9H2 Fab heavy chain × 1 9H2 Fab light chain × 1 PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 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 8E8S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-meric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 60	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-meric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å
9OCL PV2-10D2 Complex Deposited 2025-04-24	Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain 4 2–69（68 aa）	Not recorded	PLM PALMITIC ACID × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.65 Å

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

View Construct and Data Evidence

UniProt name	D0QXH8_9ENTO
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain 4； PDBConstruct 1–68； UniProt 2–69

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8e8s
Deposition date deposition_date	2022-08-25
Structure title title	9H2 Fab-poliovirus 2 complex
Keywords keywords	Complex, Fab, poliovirus, neutralizing, VIRUS-IMMUNE SYSTEM complex; VIRUS/IMMUNE SYSTEM
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	32.93 Å
Radius of gyration Rg (electron density) rg_electron	32.04 Å
Forward intensity I(0) i0	214498000.00
Molecular weight molecular_weight	117100.0 kDa
Excluded volume excluded_volume	146300 Å³
Envelope volume envelope_volume	185420 Å³
Hydration-shell volume shell_volume	47036 Å³
Envelope diameter envelope_diameter	110.5 Å
Shell Rg shell_rg	39.92 Å
Envelope Rg envelope_rg	32.34 Å
Shape Rg shape_rg	32.01 Å
Total Rg total_rg	32.77 Å
Total atoms total_atoms	8245
Residues n_residues	1059
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	102.9 Å
Rg (real space) rg_real	32.82 Å
Rg uncertainty (real space) rg_real_error	0.66 Å
I(0) (real space) i0_real	2.1450e+08
I(0) uncertainty (real space) i0_real_error	3.3050e+06
Rg (reciprocal space) rg_reciprocal	32.87 Å
I(0) (reciprocal space) i0_reciprocal	214500000.0000
Solution quality estimate total_estimate	0.9019
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	38.6 Å
Skewness Skewness skewness	0.239
Kurtosis Kurtosis kurtosis	-0.501
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	42760000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.893

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Capsid protein VP1
Molecular weight formula_weight	30663.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1
Atom count atom_count	8245

NNLPDTQSSGPAHSKETPALTAVETGATNPLVPSDTVQTRHVIQKRTRSESTVESFFARGACVAIIEVDNDAPTKRASKLFSVWKITYKDTVQLRRKLEFFTYSRFDMEFTFVVTSNYTDANNGHALNQVYQIMYIPPGAPIPGKWNDYTWQTSSNPSVFYTYGAPPARISVPYVGIANAYSHFYDGFAKVPLAGQASTEGDSLYGAASLNDFGSLAVRVVNDHNPTKLTSKIRVYMKPKHVRVWCPRPPRAVPYYGPGVDYKDGLAPLPGKGLTTY

Entity 2 Entity 2 polymer

Description description	Capsid protein VP2
Molecular weight formula_weight	29045.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	2

SVRVMQLTLGNSTITTQEAANSVVAYGRWPEYIKDSEANPVDQPTEPDVAACRFYTLDTVTWRKESRGWWWKLPDALKDMGLFGQNMFYHYLGRAGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSTTHMFTKYENANPGEKGGEFKGSFTLDTNATNPARNFCPVDYLFGSGVLAGNAFVYPHQIINLRTNNCATLVLPYVNSLSIDSMTKHNNWGIAILPLAPLDFATESSTEIPITLTIAPMCCEFNGLRNITVPRTQ

Entity 3 Entity 3 polymer

Description description	Capsid protein VP3
Molecular weight formula_weight	26115.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	3

GLPVLNTPGSNQYLTADNYQSPCAIPEFDVTPPIDIPGEVRNMMELAEIDTMIPLNLTNQRKNTMDMYRVELNDAAHSDTPILCLSLSPASDPRLAHTMLGEILNYYTHWAGSLKFTFLFCGSMMATGKLLVSYAPPGAEAPKSRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTINDSFTEGGYISMFYQTRVVVPLSTPRKMDILGFVSACNDFSVRLLRDTTHISQEA

Entity 4 Entity 4 polymer

Description description	Capsid protein VP4
Molecular weight formula_weight	7347.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	4

GAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFAQDPSKFTEPIKDVLIKTAPTLN

Entity 5 Entity 5 polymer

Description description	9H2 Fab heavy chain
Molecular weight formula_weight	14052.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

LVQSGAELKKPGASVKFSCQASGFTFTTYDIHWVRQAPGQGLEWMGMISPSRDSTIYAQKFQGRVTMTSDTSTSTVYMELTSLRSEDTALYYCATASRPSAWVFRSLYTYYYMDVWGTGTTVTVSS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 6 Entity 6 polymer

Description description	9H2 Fab light chain
Molecular weight formula_weight	11738.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L

QSALTQPASVSGSPGQSITISCTGTITDIGYYNYVSWYQQHPGKAPKLIIFDVTNRPSGVSDRFSGSKSGNTASLTISGLQAEDEGDYYCFSHRSNNIRVFGGGTKLTVL

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 7 Entity 7 non-polymer

Description description	PALMITIC ACID
Molecular weight formula_weight	256.4 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	8e8s201
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	8e8sH01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	8e8sL01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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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	2.73 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	11599

fit	/app/data/saxs_computation/e8/8e8s/8e8s.fit
pddf	/app/data/pr_computation/e8/8e8s/8e8s.pr.out
profile	/app/data/saxs_computation/e8/8e8s/8e8s.dat

9H2 Fab-poliovirus 2 complex

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

Capsid protein VP1

State in the Current Structure

Other States of the Same Protein in the Database

Capsid protein VP2

State in the Current Structure

Other States of the Same Protein in the Database

Capsid protein 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 (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

来源 Source

Entity 6 Entity 6 polymer

Polymer Polymer

来源 Source

Entity 7 Entity 7 non-polymer

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)