SAXSdb — 9iwq

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

Flagellin

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2–495	Mutation：G426A	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.08 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 9IWQ	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 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 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 mutation/modification 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 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
9M5T Structure of the flagellar filament in short-length at 3.02 angstroms resolution Deposited 2025-03-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 44 PDB declaration: 44-meric	Chain AA 1–495（495 aa） Chain AB 1–495（495 aa） Chain AC 1–495（495 aa） Chain AD 1–495（495 aa） Chain AE 1–495（495 aa） Chain AF 1–495（495 aa） Chain AG 1–495（495 aa） Chain AH 1–495（495 aa） Chain AI 1–495（495 aa） Chain AJ 1–495（495 aa） Chain AK 1–495（495 aa） Chain BA 1–495（495 aa） Chain BB 1–495（495 aa） Chain BC 1–495（495 aa） Chain BD 1–495（495 aa） Chain BE 1–495（495 aa） Chain BF 1–495（495 aa） Chain BG 1–495（495 aa） Chain BH 1–495（495 aa） Chain BI 1–495（495 aa） Chain BJ 1–495（495 aa） Chain BK 1–495（495 aa） Chain CA 1–495（495 aa） Chain CB 1–495（495 aa） Chain CC 1–495（495 aa） Chain CD 1–495（495 aa） Chain CE 1–495（495 aa） Chain CF 1–495（495 aa） Chain CG 1–495（495 aa） Chain CH 1–495（495 aa） Chain CI 1–495（495 aa） Chain CJ 1–495（495 aa） Chain CK 1–495（495 aa） Chain DA 1–495（495 aa） Chain DB 1–495（495 aa） Chain DC 1–495（495 aa） Chain DD 1–495（495 aa） Chain DE 1–495（495 aa） Chain DF 1–495（495 aa） Chain DG 1–495（495 aa） Chain DH 1–495（495 aa） Chain DI 1–495（495 aa） Chain DJ 1–495（495 aa） Chain DK 1–495（495 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.02 Å
9M67 the flagellar filament cap FliD in complex with FliC Deposited 2025-03-07	Different construct Different mutation/modification Different oligomeric state 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 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 A； PDBConstruct 1–405； UniProt 2–495

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	9iwq
Deposition date deposition_date	2024-07-25
最后修订 last_revision	2024-08-07
Structure title title	Salmonella enterica serovar Typhimurium FliC(G426A)delta(204-292) forming the L-type straight filament
Keywords keywords	flagellin, tail, flagella, filament, MOTOR PROTEIN; MOTOR PROTEIN
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	41.52 Å
Radius of gyration Rg (electron density) rg_electron	43.60 Å
Forward intensity I(0) i0	30033200.00
Molecular weight molecular_weight	40647.0 kDa
Excluded volume excluded_volume	49867 Å³
Envelope volume envelope_volume	77717 Å³
Hydration-shell volume shell_volume	19064 Å³
Envelope diameter envelope_diameter	160.1 Å
Shell Rg shell_rg	36.37 Å
Envelope Rg envelope_rg	44.78 Å
Shape Rg shape_rg	43.54 Å
Total Rg total_rg	43.28 Å
Total atoms total_atoms	5683
Residues n_residues	387
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	154.4 Å
Rg (real space) rg_real	42.72 Å
Rg uncertainty (real space) rg_real_error	2.60 Å
I(0) (real space) i0_real	3.0030e+07
I(0) uncertainty (real space) i0_real_error	6.0850e+05
Rg (reciprocal space) rg_reciprocal	41.53 Å
I(0) (reciprocal space) i0_reciprocal	29990000.0000
Solution quality estimate total_estimate	0.5997
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	24.4 Å
Skewness Skewness skewness	0.778
Kurtosis Kurtosis kurtosis	-0.241
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1253000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.108; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.022; Smooth: 0.445

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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	—

Resolution resolution	2.08 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	726742

Description description	Flagellin
Molecular weight formula_weight	42587.6 kDa
Mutation mutation	G426A
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5683

Salmonella enterica serovar Typhimurium FliC(G426A)delta(204-292) forming the L-type straight filament

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

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
NCBI Class编号 ncbi_taxonomy_id	99287
宿主生物 host_organism	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

fit	/app/data/saxs_computation/iw/9iwq/9iwq.fit
pddf	/app/data/pr_computation/iw/9iwq/9iwq.pr.out
profile	/app/data/saxs_computation/iw/9iwq/9iwq.dat