SAXSdb — 1io1

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

PHASE 1 FLAGELLIN

Salmonella typhimurium

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 53–450	Fragment：F41 L-TYPE (RESIDUES 54-451) Mutation：G426A	No other associated polymer	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

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 1IO1	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1UCU R-type straight flagellar filament made of full-length flagellin Deposited 2003-04-22	Different construct Different mutation/modification Different experimental method 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 experimental method 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 method 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 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 method 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 experimental method 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
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 method 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 experimental method 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 method 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 A； PDBConstruct 1–398； UniProt 53–450

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	1io1
Deposition date deposition_date	2000-12-28
Structure title title	CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN
Keywords keywords	beta-folium, flagellin, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	34.25 Å
Radius of gyration Rg (electron density) rg_electron	34.85 Å
Forward intensity I(0) i0	30376900.00
Molecular weight molecular_weight	40985.0 kDa
Excluded volume excluded_volume	50396 Å³
Envelope volume envelope_volume	69406 Å³
Hydration-shell volume shell_volume	20192 Å³
Envelope diameter envelope_diameter	135.2 Å
Shell Rg shell_rg	33.68 Å
Envelope Rg envelope_rg	34.71 Å
Shape Rg shape_rg	34.83 Å
Total Rg total_rg	34.80 Å
Total atoms total_atoms	2880
Residues n_residues	395
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	126.3 Å
Rg (real space) rg_real	34.86 Å
Rg uncertainty (real space) rg_real_error	2.01 Å
I(0) (real space) i0_real	3.0380e+07
I(0) uncertainty (real space) i0_real_error	5.7670e+05
Rg (reciprocal space) rg_reciprocal	34.48 Å
I(0) (reciprocal space) i0_reciprocal	30370000.0000
Solution quality estimate total_estimate	0.7109
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.0 Å
Skewness Skewness skewness	0.646
Kurtosis Kurtosis kurtosis	-0.235
Angular range angular_range	— – 0.2300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1742000.0000
Real-space data points n_real_points	47
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.418; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.206; Smooth: 0.778

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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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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1io1a_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.32 — Phase 1 flagellin
Superfamily Superfamily superfamily	e.32.1 — Phase 1 flagellin
Family Family family	e.32.1.1 — Phase 1 flagellin

CATH v4.4 (3 domains)

Domain ID domain_id	1io1A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1330 — f41 fragment of flagellin, N-terminal domain
Homologous superfamily homologous superfamily	10 — f41 fragment of flagellin, N-terminal domain

Domain ID domain_id	1io1A02
Class class	2 — Mainly Beta
Architecture architecture	170 — Beta Complex
Topology topology	280 — f41 fragment of flagellin, middle domain
Homologous superfamily homologous superfamily	10 — f41 fragment of flagellin, middle domain

Domain ID domain_id	1io1A03
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	220 — f41 fragment of flagellin, C-terminal domain
Homologous superfamily homologous superfamily	10 — f41 fragment of flagellin, C-terminal domain

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8. Citations (1)

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Unit-cell length a length_a	51.750 Å
Unit-cell length b length_b	36.440 Å
Unit-cell length c length_c	118.350 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.15 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	0.2340
R_free r_free	0.2660

Description description	PHASE 1 FLAGELLIN
Molecular weight formula_weight	41352.0 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	3234

CRYSTAL STRUCTURE OF F41 FRAGMENT OF FLAGELLIN

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

PHASE 1 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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Salmonella typhimurium
NCBI Class编号 ncbi_taxonomy_id	602
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	354

fit	/app/data/saxs_computation/io/1io1/1io1.fit
pddf	/app/data/pr_computation/io/1io1/1io1.pr.out
profile	/app/data/saxs_computation/io/1io1/1io1.dat