SAXSdb — 9m5t

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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 × 44 PDB declaration: 44-meric（44） Consistent with protein copy count	Chain AA； UniProt 1–495 Chain AB； UniProt 1–495 Chain AC； UniProt 1–495 Chain AD； UniProt 1–495 Chain AE； UniProt 1–495 Chain AF； UniProt 1–495 Chain AG； UniProt 1–495 Chain AH； UniProt 1–495 Chain AI； UniProt 1–495 Chain AJ； UniProt 1–495 Chain AK； UniProt 1–495 Chain BA； UniProt 1–495 Chain BB； UniProt 1–495 Chain BC； UniProt 1–495 Chain BD； UniProt 1–495 Chain BE； UniProt 1–495 Chain BF； UniProt 1–495 Chain BG； UniProt 1–495 Chain BH； UniProt 1–495 Chain BI； UniProt 1–495 Chain BJ； UniProt 1–495 Chain BK； UniProt 1–495 Chain CA； UniProt 1–495 Chain CB； UniProt 1–495 Chain CC； UniProt 1–495 Chain CD； UniProt 1–495 Chain CE； UniProt 1–495 Chain CF； UniProt 1–495 Chain CG； UniProt 1–495 Chain CH； UniProt 1–495 Chain CI； UniProt 1–495 Chain CJ； UniProt 1–495 Chain CK； UniProt 1–495 Chain DA； UniProt 1–495 Chain DB； UniProt 1–495 Chain DC； UniProt 1–495 Chain DD； UniProt 1–495 Chain DE； UniProt 1–495 Chain DF； UniProt 1–495 Chain DG； UniProt 1–495 Chain DH； UniProt 1–495 Chain DI； UniProt 1–495 Chain DJ； UniProt 1–495 Chain DK； UniProt 1–495	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.02 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 9M5T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1IO1 CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN Deposited 2000-12-28	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–450（398 aa） Fragment：F41 L-TYPE (RESIDUES 54-451)	Mutation：G426A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；289 K；PEG 6000, NaCl, Glycerol, Iso-Propanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 2.00 Å R-free 0.266
1UCU R-type straight flagellar filament made of full-length flagellin Deposited 2003-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–494（494 aa）	Mutation：A449V	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL；pH 7.8；150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL	Resolution 4.00 Å
3A5X L-type straight flagellar filament made of full-length flagellin Deposited 2009-08-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–495（494 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL；pH 7.8；150MM NACL, 2MM MGCL2, 20MM TRIS-HCL, 2-5% GLYCEROL cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
5YUD Flagellin derivative in complex with the NLR protein NAIP5 Deposited 2017-11-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 452–495（44 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.28 Å
6CH3 Crystal structure of the cytoplasmic domain of FlhA and FliS-FliC complex Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 455–495（41 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；tascimate	Resolution 2.68 Å R-free 0.258
8FML Cryo-EM structure of NLR family apoptosis inhibitory protein 5 (NAIP5) in complex with a full-length flagellin (FliC) ligand Deposited 2022-12-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–495（495 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å
9IWQ Salmonella enterica serovar Typhimurium FliC(G426A)delta(204-292) forming the L-type straight filament Deposited 2024-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–495（494 aa）	Mutation：G426A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.08 Å
9M67 the flagellar filament cap FliD in complex with FliC Deposited 2025-03-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–495（495 aa） Chain B 1–495（495 aa） Chain C 1–495（495 aa） Chain D 1–495（495 aa） Chain E 1–495（495 aa） Chain F 1–495（495 aa） Chain G 1–495（495 aa） Chain H 1–495（495 aa） Chain I 1–495（495 aa） Chain J 1–495（495 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9M6H structure of FliD-FliC at a 10:10 stoichiometry Deposited 2025-03-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: 20-meric	Chain B 54–454（401 aa） Chain D 54–454（401 aa） Chain F 54–454（401 aa） Chain H 54–454（401 aa） Chain J 54–454（401 aa） Chain L 54–454（401 aa） Chain N 54–454（401 aa） Chain P 54–454（401 aa） Chain R 54–454（401 aa） Chain T 54–454（401 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.27 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FLIC_SALTY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain AA； PDBConstruct 1–495； UniProt 1–495 Author chain AB； PDBConstruct 1–495； UniProt 1–495 Author chain AC； PDBConstruct 1–495； UniProt 1–495 Author chain AD； PDBConstruct 1–495； UniProt 1–495 Author chain AE； PDBConstruct 1–495； UniProt 1–495 Author chain AF； PDBConstruct 1–495； UniProt 1–495 Author chain AG； PDBConstruct 1–495； UniProt 1–495 Author chain AH； PDBConstruct 1–495； UniProt 1–495 Author chain AI； PDBConstruct 1–495； UniProt 1–495 Author chain AJ； PDBConstruct 1–495； UniProt 1–495 Author chain AK； PDBConstruct 1–495； UniProt 1–495 Author chain BA； PDBConstruct 1–495； UniProt 1–495 Author chain BB； PDBConstruct 1–495； UniProt 1–495 Author chain BC； PDBConstruct 1–495； UniProt 1–495 Author chain BD； PDBConstruct 1–495； UniProt 1–495 Author chain BE； PDBConstruct 1–495； UniProt 1–495 Author chain BF； PDBConstruct 1–495； UniProt 1–495 Author chain BG； PDBConstruct 1–495； UniProt 1–495 Author chain BH； PDBConstruct 1–495； UniProt 1–495 Author chain BI； PDBConstruct 1–495； UniProt 1–495 Author chain BJ； PDBConstruct 1–495； UniProt 1–495 Author chain BK； PDBConstruct 1–495； UniProt 1–495 Author chain CA； PDBConstruct 1–495； UniProt 1–495 Author chain CB； PDBConstruct 1–495； UniProt 1–495 Author chain CC； PDBConstruct 1–495； UniProt 1–495 Author chain CD； PDBConstruct 1–495； UniProt 1–495 Author chain CE； PDBConstruct 1–495； UniProt 1–495 Author chain CF； PDBConstruct 1–495； UniProt 1–495 Author chain CG； PDBConstruct 1–495； UniProt 1–495 Author chain CH； PDBConstruct 1–495； UniProt 1–495 Author chain CI； PDBConstruct 1–495； UniProt 1–495 Author chain CJ； PDBConstruct 1–495； UniProt 1–495 Author chain CK； PDBConstruct 1–495； UniProt 1–495 Author chain DA； PDBConstruct 1–495； UniProt 1–495 Author chain DB； PDBConstruct 1–495； UniProt 1–495 Author chain DC； PDBConstruct 1–495； UniProt 1–495 Author chain DD； PDBConstruct 1–495； UniProt 1–495 Author chain DE； PDBConstruct 1–495； UniProt 1–495 Author chain DF； PDBConstruct 1–495； UniProt 1–495 Author chain DG； PDBConstruct 1–495； UniProt 1–495 Author chain DH； PDBConstruct 1–495； UniProt 1–495 Author chain DI； PDBConstruct 1–495； UniProt 1–495 Author chain DJ； PDBConstruct 1–495； UniProt 1–495 Author chain DK； PDBConstruct 1–495； UniProt 1–495

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	9m5t
Deposition date deposition_date	2025-03-06
Structure title title	Structure of the flagellar filament in short-length at 3.02 angstroms resolution
Keywords keywords	flagellum, FliC, fibril, 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	97.19 Å
Radius of gyration Rg (electron density) rg_electron	97.48 Å
Forward intensity I(0) i0	79216600000.00
Molecular weight molecular_weight	2266100.0 kDa
Excluded volume excluded_volume	2785100 Å³
Envelope volume envelope_volume	5173400 Å³
Hydration-shell volume shell_volume	412820 Å³
Envelope diameter envelope_diameter	374.0 Å
Shell Rg shell_rg	107.30 Å
Envelope Rg envelope_rg	98.01 Å
Shape Rg shape_rg	97.49 Å
Total Rg total_rg	97.51 Å
Total atoms total_atoms	159148
Residues n_residues	21747
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	262.1 Å
Rg (real space) rg_real	92.97 Å
Rg uncertainty (real space) rg_real_error	0.58 Å
I(0) (real space) i0_real	7.5800e+10
I(0) uncertainty (real space) i0_real_error	1.3640e+09
Rg (reciprocal space) rg_reciprocal	97.31 Å
I(0) (reciprocal space) i0_reciprocal	79250000000.0000
Solution quality estimate total_estimate	0.9113
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	114.7 Å
Skewness Skewness skewness	0.246
Kurtosis Kurtosis kurtosis	-0.421
Angular range angular_range	— – 0.0800 Å⁻¹
Current regularization parameter α current_alpha	0.4479
Highest regularization parameter α highest_alpha	20920000000.0000
Real-space data points n_real_points	17
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.003; Oscil: 0.983; Stabil: 0.985; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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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	triclinic

Resolution resolution	3.02 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	498897

Description description	Flagellin
Molecular weight formula_weight	51654.3 kDa
Source method src_method	nat
Copy count entity_count	44

Polymer type type	polypeptide(L)
Chain IDs strand_id	AA,AB,AC,AD,AE,AF,AG,AH,AI,AJ,AK,BA,BB,BC,BD,BE,BF,BG,BH,BI,BJ,BK,CA,CB,CC,CD,CE,CF,CG,CH,CI,CJ,CK,DA,DB,DC,DD,DE,DF,DG,DH,DI,DJ,DK
Atom count atom_count	159148

Structure of the flagellar filament in short-length at 3.02 angstroms resolution

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/m5/9m5t/9m5t.fit
pddf	/app/data/pr_computation/m5/9m5t/9m5t.pr.out
profile	/app/data/saxs_computation/m5/9m5t/9m5t.dat