SAXSdb — 9v96

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

Flagellin

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 × 38 PDB declaration: 38-meric（38） Consistent with protein copy count	Chain A； UniProt 1–463 Chain B； UniProt 1–463 Chain C； UniProt 1–463 Chain D； UniProt 1–463 Chain E； UniProt 1–463 Chain G； UniProt 1–463 Chain H； UniProt 1–463 Chain I； UniProt 1–463 Chain J； UniProt 1–463 Chain K； UniProt 1–463 Chain L； UniProt 1–463 Chain M； UniProt 1–463 Chain N； UniProt 1–463 Chain O； UniProt 1–463 Chain P； UniProt 1–463 Chain R； UniProt 1–463 Chain S； UniProt 1–463 Chain T； UniProt 1–463 Chain U； UniProt 1–463 Chain V； UniProt 1–463 Chain W； UniProt 1–463 Chain X； UniProt 1–463 Chain Y； UniProt 1–463 Chain Z； UniProt 1–463 Chain a； UniProt 1–463 Chain b； UniProt 1–463 Chain d； UniProt 1–463 Chain e； UniProt 1–463 Chain f； UniProt 1–463 Chain g； UniProt 1–463 Chain i； UniProt 1–463 Chain j； UniProt 1–463 Chain k； UniProt 1–463 Chain l； UniProt 1–463 Chain m； UniProt 1–463 Chain n； UniProt 1–463 Chain o； UniProt 1–463 Chain p； UniProt 1–463	Not recorded	NA SODIUM ION × 38	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 3.14 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 9V96	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9XTB Cryo-EM structure of ArlA2 filament of Haloarcula marismortui Deposited 2025-11-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 28 PDB declaration: 28-meric	Chain A 1–463（463 aa） Chain B 1–463（463 aa） Chain C 1–463（463 aa） Chain D 1–463（463 aa） Chain G 1–463（463 aa） Chain H 1–463（463 aa） Chain J 1–463（463 aa） Chain K 1–463（463 aa） Chain L 1–463（463 aa） Chain N 1–463（463 aa） Chain O 1–463（463 aa） Chain R 1–463（463 aa） Chain S 1–463（463 aa） Chain T 1–463（463 aa） Chain V 1–463（463 aa） Chain W 1–463（463 aa） Chain X 1–463（463 aa） Chain Z 1–463（463 aa） Chain a 1–463（463 aa） Chain b 1–463（463 aa） Chain d 1–463（463 aa） Chain e 1–463（463 aa） Chain f 1–463（463 aa） Chain i 1–463（463 aa） Chain j 1–463（463 aa） Chain m 1–463（463 aa） Chain n 1–463（463 aa） Chain o 1–463（463 aa）	Not recorded	NA SODIUM ION × 28	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.00 Å

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

View Construct and Data Evidence

UniProt name	Q5V881_HALMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–463； UniProt 1–463 Author chain B； PDBConstruct 1–463； UniProt 1–463 Author chain C； PDBConstruct 1–463； UniProt 1–463 Author chain D； PDBConstruct 1–463； UniProt 1–463 Author chain E； PDBConstruct 1–463； UniProt 1–463 Author chain G； PDBConstruct 1–463； UniProt 1–463 Author chain H； PDBConstruct 1–463； UniProt 1–463 Author chain I； PDBConstruct 1–463； UniProt 1–463 Author chain J； PDBConstruct 1–463； UniProt 1–463 Author chain K； PDBConstruct 1–463； UniProt 1–463 Author chain L； PDBConstruct 1–463； UniProt 1–463 Author chain M； PDBConstruct 1–463； UniProt 1–463 Author chain N； PDBConstruct 1–463； UniProt 1–463 Author chain O； PDBConstruct 1–463； UniProt 1–463 Author chain P； PDBConstruct 1–463； UniProt 1–463 Author chain R； PDBConstruct 1–463； UniProt 1–463 Author chain S； PDBConstruct 1–463； UniProt 1–463 Author chain T； PDBConstruct 1–463； UniProt 1–463 Author chain U； PDBConstruct 1–463； UniProt 1–463 Author chain V； PDBConstruct 1–463； UniProt 1–463 Author chain W； PDBConstruct 1–463； UniProt 1–463 Author chain X； PDBConstruct 1–463； UniProt 1–463 Author chain Y； PDBConstruct 1–463； UniProt 1–463 Author chain Z； PDBConstruct 1–463； UniProt 1–463 Author chain a； PDBConstruct 1–463； UniProt 1–463 Author chain b； PDBConstruct 1–463； UniProt 1–463 Author chain d； PDBConstruct 1–463； UniProt 1–463 Author chain e； PDBConstruct 1–463； UniProt 1–463 Author chain f； PDBConstruct 1–463； UniProt 1–463 Author chain g； PDBConstruct 1–463； UniProt 1–463 Author chain i； PDBConstruct 1–463； UniProt 1–463 Author chain j； PDBConstruct 1–463； UniProt 1–463 Author chain k； PDBConstruct 1–463； UniProt 1–463 Author chain l； PDBConstruct 1–463； UniProt 1–463 Author chain m； PDBConstruct 1–463； UniProt 1–463 Author chain n； PDBConstruct 1–463； UniProt 1–463 Author chain o； PDBConstruct 1–463； UniProt 1–463 Author chain p； PDBConstruct 1–463； UniProt 1–463

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	9v96
Deposition date deposition_date	2025-05-30
Structure title title	Cryo-EM structure of the inner core of ArlA2 filament of Haloarcula marismortui
Keywords keywords	archaellum, haloarcheon, PROTEIN FIBRIL; PROTEIN FIBRIL
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	71.40 Å
Radius of gyration Rg (electron density) rg_electron	72.65 Å
Forward intensity I(0) i0	7024240000.00
Molecular weight molecular_weight	686450.0 kDa
Excluded volume excluded_volume	850500 Å³
Envelope volume envelope_volume	1266900 Å³
Hydration-shell volume shell_volume	154520 Å³
Envelope diameter envelope_diameter	322.7 Å
Shell Rg shell_rg	65.03 Å
Envelope Rg envelope_rg	73.12 Å
Shape Rg shape_rg	72.64 Å
Total Rg total_rg	72.56 Å
Total atoms total_atoms	48061
Residues n_residues	6687
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	210.4 Å
Rg (real space) rg_real	68.71 Å
Rg uncertainty (real space) rg_real_error	0.96 Å
I(0) (real space) i0_real	6.8800e+09
I(0) uncertainty (real space) i0_real_error	1.2320e+08
Rg (reciprocal space) rg_reciprocal	69.26 Å
I(0) (reciprocal space) i0_reciprocal	6988000000.0000
Solution quality estimate total_estimate	0.8289
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	66.9 Å
Skewness Skewness skewness	0.572
Kurtosis Kurtosis kurtosis	-0.286
Angular range angular_range	— – 0.1100 Å⁻¹
Current regularization parameter α current_alpha	0.0916
Highest regularization parameter α highest_alpha	3101000000.0000
Real-space data points n_real_points	23
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.798; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.149

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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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	3.14 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	309194

Description description	Flagellin
Molecular weight formula_weight	47382.5 kDa
Source method src_method	nat
Copy count entity_count	38

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,D,E,G,H,I,J,K,L,M,N,O,P,R,S,T,U,V,W,X,Y,Z,a,b,d,e,f,g,i,j,k,l,m,n,o,p,B
Atom count atom_count	48061

Cryo-EM structure of the inner core of ArlA2 filament of Haloarcula marismortui

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

Flagellin

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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	38

fit	/app/data/saxs_computation/v9/9v96/9v96.fit
pddf	/app/data/pr_computation/v9/9v96/9v96.pr.out
profile	/app/data/saxs_computation/v9/9v96/9v96.dat