SAXSdb — 9m68

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

Flagellar hook-associated protein 2

Salmonella enterica subsp. enterica serovar 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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 19–433 Chain B； UniProt 19–433 Chain D； UniProt 19–433 Chain G； UniProt 19–433 Chain I； UniProt 19–433	Not recorded	Flagellar hook-associated protein 3 × 5 （P16326）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.40 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 9M68	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5GNA Crystal Structure of flagellin assembly related protein Deposited 2016-07-20	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 401–467（67 aa） Fragment：UNP RESIDUES 401-467	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；296 K；5% PEG 400, 10% isopropanol, 0.2 M magnesium chloride, 0.1 M Tris-HCl pH 8.0	Resolution 2.30 Å R-free 0.229
5KRW Recognition and targeting mechanisms by chaperones in flagella assembly and operation Deposited 2016-07-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 428–467（40 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；305 K；Ionic strength (raw mmCIF value) 120；Pressure 1 NMR sample composition 1 mM [U-99% 13C; U-99% 15N; U-99% 2H] FliT-FliD_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.5 mM EDTA, 5 mM beta-mercaptoethanol, 0.05 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM U[15N,2H] 1H-13C-ILVMAT-methyl FliT-FliD_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.5 mM EDTA, 5 mM beta-mercaptoethanol, 0.05 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 13C; U-99% 15N] FliT-FliD_fusion, 20 mM potassium phosphate, 100 mM potassium chloride, 0.5 mM EDTA, 5 mM beta-mercaptoethanol, 0.05 % sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21	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 D 428–467（40 aa） Fragment：unp residues 1-122; 428-467	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；CaCl2, PEG8000, Sodium cacodylate	Resolution 2.70 Å R-free 0.266
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 428–467（40 aa） Fragment：unp residues 1-122; 428-467	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；CaCl2, PEG8000, Sodium cacodylate	Resolution 2.70 Å R-free 0.266
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 428–467（40 aa） Fragment：unp residues 1-122; 428-467	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；CaCl2, PEG8000, Sodium cacodylate	Resolution 2.70 Å R-free 0.266
9M67 the flagellar filament cap FliD in complex with FliC Deposited 2025-03-07	Different construct Different mutation/modification Different oligomeric state	Assembly 1 Insufficient information Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa） Chain E 1–467（467 aa） Chain F 1–467（467 aa） Chain G 1–467（467 aa） Chain H 1–467（467 aa） Chain I 1–467（467 aa） Chain J 1–467（467 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 A 21–450（430 aa） Chain C 21–450（430 aa） Chain E 21–450（430 aa） Chain G 21–450（430 aa） Chain I 21–450（430 aa） Chain K 21–450（430 aa） Chain M 21–450（430 aa） Chain O 21–450（430 aa） Chain Q 21–450（430 aa） Chain S 21–450（430 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
9M6I structure of the FliD cap Deposited 2025-03-07	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa） Chain E 1–467（467 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å
9U4R Structure of the intial complex in filament assembly at 3.23 angstroms resolution, conformation 2. Deposited 2025-03-20	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 73 PDB declaration: 73-meric	Chain AA 1–467（467 aa） Chain AB 1–467（467 aa） Chain AC 1–467（467 aa） Chain AD 1–467（467 aa） Chain AE 1–467（467 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.23 Å
9U7Y Structure of the tip region of the intial complex in bacterial flagellar filament assembly at 3.68 angstroms resolution, conformation 3. Deposited 2025-03-25	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain AA 1–467（467 aa） Chain AB 1–467（467 aa） Chain AC 1–467（467 aa） Chain AD 1–467（467 aa） Chain AE 1–467（467 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.68 Å

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FLID_SALTY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–415； UniProt 19–433 Author chain B； PDBConstruct 1–415； UniProt 19–433 Author chain D； PDBConstruct 1–415； UniProt 19–433 Author chain G； PDBConstruct 1–415； UniProt 19–433 Author chain I； PDBConstruct 1–415； UniProt 19–433

Flagellar hook-associated protein 3

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt P16326

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain C； UniProt 51–273 Chain E； UniProt 51–273 Chain F； UniProt 51–273 Chain H； UniProt 51–273 Chain J； UniProt 51–273	Not recorded	Flagellar hook-associated protein 2 × 5 （P16328）	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.40 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 9M68	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2D4X Crystal structure of a 26K fragment of HAP3 (FlgL) Deposited 2005-10-25	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 40–286（247 aa） Fragment：FL26	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 4.2；277 K；10-20% PEG 8000, 0.2M magnesium chloride, 0.1M Phosphate-citrate, pH 4.2, VAPOR DIFFUSION, temperature 277K	Resolution 1.90 Å R-free 0.258
9U4R Structure of the intial complex in filament assembly at 3.23 angstroms resolution, conformation 2. Deposited 2025-03-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 73 PDB declaration: 73-meric	Chain BA 1–317（317 aa） Chain BB 1–317（317 aa） Chain BC 1–317（317 aa） Chain BD 1–317（317 aa） Chain BE 1–317（317 aa） Chain BG 1–317（317 aa） Chain BH 1–317（317 aa） Chain BI 1–317（317 aa） Chain BJ 1–317（317 aa） Chain BK 1–317（317 aa） Chain BL 1–317（317 aa） Chain BM 1–317（317 aa） Chain BN 1–317（317 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.23 Å
9U7Y Structure of the tip region of the intial complex in bacterial flagellar filament assembly at 3.68 angstroms resolution, conformation 3. Deposited 2025-03-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-meric	Chain BA 1–317（317 aa） Chain BB 1–317（317 aa） Chain BC 1–317（317 aa） Chain BD 1–317（317 aa） Chain BE 1–317（317 aa） Chain BF 1–317（317 aa） Chain BG 1–317（317 aa） Chain BH 1–317（317 aa） Chain BI 1–317（317 aa） Chain BJ 1–317（317 aa） Chain BK 1–317（317 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.68 Å

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

View Construct and Data Evidence

UniProt name	FLGL_SALTY
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–223； UniProt 51–273 Author chain E； PDBConstruct 1–223； UniProt 51–273 Author chain F； PDBConstruct 1–223； UniProt 51–273 Author chain H； PDBConstruct 1–223； UniProt 51–273 Author chain J； PDBConstruct 1–223； UniProt 51–273

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	9m68
Deposition date deposition_date	2025-03-07
Structure title title	the flagellar filament cap FliD in complex with FlgL
Keywords keywords	Complex, STRUCTURAL PROTEIN; STRUCTURAL 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	53.60 Å
Radius of gyration Rg (electron density) rg_electron	52.59 Å
Forward intensity I(0) i0	1747200000.00
Molecular weight molecular_weight	338420.0 kDa
Excluded volume excluded_volume	420270 Å³
Envelope volume envelope_volume	737470 Å³
Hydration-shell volume shell_volume	114170 Å³
Envelope diameter envelope_diameter	149.5 Å
Shell Rg shell_rg	61.42 Å
Envelope Rg envelope_rg	48.66 Å
Shape Rg shape_rg	52.59 Å
Total Rg total_rg	52.87 Å
Total atoms total_atoms	23750
Residues n_residues	3190
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	138.1 Å
Rg (real space) rg_real	53.15 Å
Rg uncertainty (real space) rg_real_error	0.51 Å
I(0) (real space) i0_real	1.7470e+09
I(0) uncertainty (real space) i0_real_error	2.6170e+07
Rg (reciprocal space) rg_reciprocal	53.97 Å
I(0) (reciprocal space) i0_reciprocal	1749000000.0000
Solution quality estimate total_estimate	0.8424
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	81.0 Å
Skewness Skewness skewness	-0.212
Kurtosis Kurtosis kurtosis	-0.561
Angular range angular_range	— – 0.1450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	160100000.0000
Real-space data points n_real_points	30
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.984; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Flagellar hook-associated protein 2
Molecular weight formula_weight	44168.1 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,D,G,I
Atom count atom_count	23750

LTDLTKNEKGRLTPITKQQSANSAKLTAYGTLKSALEKFQTANTALNKADLFKSTVASSTTEDLKVSTTAGAAAGTYKINVTQLAAAQSLATKTTFATTKEQLGDTSVTSRTIKIEQPGRKEPLEIKLDKGDTSMEAIRDAINDADSGIAASIVKVKENEFQLVLTANSGTDNTMKITVEGDTKLNDLLAYDSTTNTGNMQELVKAENAKLNVNGIDIERQSNTVTDAPQGITLTLTKKVTDATVTVTKDDTKAKEAIKSWVDAYNSLVDTFSSLTKYTAVEPGEEASDKNGALLGDSVVRTIQTGIRAQFANSGSNSAFKTMAEIGITQDGTSGKLKIDDDKLTKVLKDNTAAARELLVGDGKETGITTKIATEVKSYLADDGIIDNAQDNVNATLKSLTKQYLSVSNSIDETV

来源 Source

来源生物 organism	Salmonella enterica subsp. enterica serovar Typhimurium
NCBI Class编号 ncbi_taxonomy_id	90371
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Flagellar hook-associated protein 3
Molecular weight formula_weight	23633.1 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,C,E,H,J

VLSQAQAQNSQYALARTFATQKVSLEESVLSQVTTAIQTAQEKIVYAGNGTLSDDDRASLATDLQGIRDQLMNLANSTDGNGRYIFAGYKTEAAPFDQATGGYHGGEKSVTQQVDSARTMVIGHTGAQIFNSITSNAVPEPDGSDSEKNLFVMLDTAIAALKTPVEGNNVEKEKAAAAIDKTNRGLKNSLNNVLTVRAELGTQLSELSTLDSLGSDRALGQKL

来源 Source

来源生物 organism	Salmonella enterica subsp. enterica serovar Typhimurium
NCBI Class编号 ncbi_taxonomy_id	90371
宿主生物 host_organism	Escherichia coli

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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	3.400 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.40 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	453039

fit	/app/data/saxs_computation/m6/9m68/9m68.fit
pddf	/app/data/pr_computation/m6/9m68/9m68.pr.out
profile	/app/data/saxs_computation/m6/9m68/9m68.dat

the flagellar filament cap FliD in complex with FlgL

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

Flagellar hook-associated protein 2

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar hook-associated protein 3

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)