SAXSdb — 6ch2

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

Flagellar biosynthesis protein FlhA

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 360–692	Fragment：unp residues 360-692	Flagellar hook-associated protein 2,Flagellar protein FliT × 1 （P16328,P0A1N3） 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
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 360–692	Fragment：unp residues 360-692	Flagellar hook-associated protein 2,Flagellar protein FliT × 1 （P16328,P0A1N3） 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
3	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 360–692	Fragment：unp residues 360-692	Flagellar hook-associated protein 2,Flagellar protein FliT × 1 （P16328,P0A1N3）	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

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 6CH2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3A5I Structure of the cytoplasmic domain of FlhA Deposited 2009-08-07	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 328–692（365 aa） Fragment：FlhAc, UNP residues 328-692	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；10-15% PEG300, 4-6% PEG8000, 0.1M Tris-HCl, 0.5mM EDTA, 10-15% glycerol, pH8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.80 Å R-free 0.290
3A5I Structure of the cytoplasmic domain of FlhA Deposited 2009-08-07	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 328–692（365 aa） Fragment：FlhAc, UNP residues 328-692	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；10-15% PEG300, 4-6% PEG8000, 0.1M Tris-HCl, 0.5mM EDTA, 10-15% glycerol, pH8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.80 Å R-free 0.290
6AI0 Structure of the 328-692 fragment of FlhA (orthorhombic form) Deposited 2018-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Not recorded	MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M HEPES NaOH pH 7.5, 10% (w/v) PEG-8000, 0.4M Ca(OAc)2	Resolution 2.40 Å R-free 0.277
6AI0 Structure of the 328-692 fragment of FlhA (orthorhombic form) Deposited 2018-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Not recorded	MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1M HEPES NaOH pH 7.5, 10% (w/v) PEG-8000, 0.4M Ca(OAc)2	Resolution 2.40 Å R-free 0.277
6AI1 Structure of the 328-692 fragment of FlhA (D456V) Deposited 2018-08-21	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 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Mutation：D456V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG-400, 0.1M HEPES pH 7.5, 0.25M NaCl	Resolution 3.50 Å R-free 0.241
6AI1 Structure of the 328-692 fragment of FlhA (D456V) Deposited 2018-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Mutation：D456V	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG-400, 0.1M HEPES pH 7.5, 0.25M NaCl	Resolution 3.50 Å R-free 0.241
6AI2 Structure of the 328-692 fragment of FlhA (F459A) Deposited 2018-08-21	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 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Mutation：F459A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.2；293 K；20% (w/v) PEG 3350, 0.15M K2HPO4	Resolution 3.30 Å R-free 0.257
6AI2 Structure of the 328-692 fragment of FlhA (F459A) Deposited 2018-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Mutation：F459A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.2；293 K；20% (w/v) PEG 3350, 0.15M K2HPO4	Resolution 3.30 Å R-free 0.257
6AI3 Structure of the 328-692 fragment of FlhA (T490M) Deposited 2018-08-21	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 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Mutation：T490M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES NaOH pH 7.5, 27% (w/v) PEG 400, 0.23M NaCl	Resolution 3.30 Å R-free 0.258
6AI3 Structure of the 328-692 fragment of FlhA (T490M) Deposited 2018-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 328–692（365 aa） Fragment：cytoplasmic fragment, residues 328-692	Mutation：T490M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES NaOH pH 7.5, 27% (w/v) PEG 400, 0.23M NaCl	Resolution 3.30 Å R-free 0.258
6CH1 Crystal structure of the cytoplasmic domain of FlhA in monomeric form Deposited 2018-02-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 360–692（333 aa） Fragment：UNP residues 360-692	Not recorded	EDO 1,2-ETHANEDIOL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；tri-ammonium citrate, PEG3350	Resolution 1.90 Å R-free 0.237
6CH3 Crystal structure of the cytoplasmic domain of FlhA and FliS-FliC complex Deposited 2018-02-21	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 360–690（331 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
7CTN Structure of the 328-692 fragment of FlhA (E351A/D356A) Deposited 2020-08-19	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 328–692（365 aa）	Mutation：E351A/D356A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1M Tirs HCl pH 8.5, 20 % (w/v) PEG 8000, 0.2M MgCl2	Resolution 2.80 Å R-free 0.290
7CTN Structure of the 328-692 fragment of FlhA (E351A/D356A) Deposited 2020-08-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 328–692（365 aa）	Mutation：E351A/D356A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1M Tirs HCl pH 8.5, 20 % (w/v) PEG 8000, 0.2M MgCl2	Resolution 2.80 Å R-free 0.290

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FLHA_SALTY
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–334； UniProt 360–692 Author chain B； PDBConstruct 2–334； UniProt 360–692 Author chain C； PDBConstruct 2–334； UniProt 360–692

Flagellar hook-associated protein 2,Flagellar protein FliT

Salmonella typhi

UniProt P0A1N3

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 1–122	Fragment：unp residues 1-122; 428-467	Flagellar biosynthesis protein FlhA × 1 （P40729） 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
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 1–122	Fragment：unp residues 1-122; 428-467	Flagellar biosynthesis protein FlhA × 1 （P40729） 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
3	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 1–122	Fragment：unp residues 1-122; 428-467	Flagellar biosynthesis protein FlhA × 1 （P40729）	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

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	FLIT_SALTI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 58–179； UniProt 1–122 Author chain E； PDBConstruct 58–179； UniProt 1–122 Author chain F； PDBConstruct 58–179； UniProt 1–122

Flagellar hook-associated protein 2,Flagellar protein FliT

Salmonella typhi

UniProt P16328

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 428–467	Fragment：unp residues 1-122; 428-467	Flagellar biosynthesis protein FlhA × 1 （P40729） 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
2	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 428–467	Fragment：unp residues 1-122; 428-467	Flagellar biosynthesis protein FlhA × 1 （P40729） 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
3	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 428–467	Fragment：unp residues 1-122; 428-467	Flagellar biosynthesis protein FlhA × 1 （P40729）	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

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 6CH2	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 oligomeric state 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 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
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 1–467（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
9M68 the flagellar filament cap FliD in complex with FlgL 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 × 10 PDB declaration: decameric	Chain A 19–433（415 aa） Chain B 19–433（415 aa） Chain D 19–433（415 aa） Chain G 19–433（415 aa） Chain I 19–433（415 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 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 mutation/modification Different oligomeric state Different experimental method Different experimental conditions 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 mutation/modification Different oligomeric state Different experimental method 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 mutation/modification Different oligomeric state Different experimental method 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FLID_SALTY
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 5–44； UniProt 428–467 Author chain E； PDBConstruct 5–44； UniProt 428–467 Author chain F； PDBConstruct 5–44； UniProt 428–467

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	6ch2
Deposition date deposition_date	2018-02-21
Structure title title	Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex
Keywords keywords	flagellar, 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	45.69 Å
Radius of gyration Rg (electron density) rg_electron	46.04 Å
Forward intensity I(0) i0	372764000.00
Molecular weight molecular_weight	158950.0 kDa
Excluded volume excluded_volume	199830 Å³
Envelope volume envelope_volume	290210 Å³
Hydration-shell volume shell_volume	57019 Å³
Envelope diameter envelope_diameter	197.1 Å
Shell Rg shell_rg	46.24 Å
Envelope Rg envelope_rg	45.69 Å
Shape Rg shape_rg	46.02 Å
Total Rg total_rg	46.11 Å
Total atoms total_atoms	11173
Residues n_residues	1426
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	186.7 Å
Rg (real space) rg_real	46.17 Å
Rg uncertainty (real space) rg_real_error	3.15 Å
I(0) (real space) i0_real	3.7280e+08
I(0) uncertainty (real space) i0_real_error	8.3870e+06
Rg (reciprocal space) rg_reciprocal	45.70 Å
I(0) (reciprocal space) i0_reciprocal	372600000.0000
Solution quality estimate total_estimate	0.7655
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	48.0 Å
Skewness Skewness skewness	0.672
Kurtosis Kurtosis kurtosis	0.450
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	29200000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.466; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.576; Smooth: 0.975

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Flagellar biosynthesis protein FlhA
Molecular weight formula_weight	36740.3 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	11214

GEDSLGMEVGYRLIPMVDFQQDGELLGRIRSIRKKFAQDMGFLPPVVHIRDNMDLQPARYRILMKGVEIGSGDAYPGRWLAINPGTAAGTLPGEKTVDPAFGLDAIWIESALKEQAQIQGFTVVEASTVVATHLNHLIGQFSAELFGRQEAQQLLDRVSQEMPKLTEDLVPGVVTLTTLHKVLQNLLAEKVPIRDMRTILETLAEHAPLQSDPHELTAVVRVALGRAITQQWFPGNEEVQVIGLDTALERLLLQALQGGGGLEPGLADRLLAQTQEALSRQEMLGAPPVLLVNHALRPLLSRFLRRSLPQLVVLSNLELSDNRHIRMTATIGGK

来源 Source

来源生物 organism	Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
NCBI Class编号 ncbi_taxonomy_id	99287
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Flagellar hook-associated protein 2,Flagellar protein FliT
Molecular weight formula_weight	19555.0 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

GAHMSIDETVARYKAQFTQLDTMMSKLNNTSSYLTQQFTAMNKSGGSGGSGSGGSGGMTSTVEFINRWQRIALLSQSLLELAQRGEWDLLLQQEVSYLQSIETVMEKQTPPGITRSIQDMVAGYIKQTLDNEQLLKGLLQQRLDELSSLIGQSTRQKSLNNAYGRLSGMLLVPDAPGAS

来源 Source

来源生物 organism	Salmonella typhi
NCBI Class编号 ncbi_taxonomy_id	90370
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	41

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7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id	6ch2A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	60 — FHIPEP family, domain 1

Domain ID domain_id	6ch2B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	60 — FHIPEP family, domain 1

Domain ID domain_id	6ch2C01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	60 — FHIPEP family, domain 1

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8. Citations (1)

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Unit-cell length a length_a	49.110 Å
Unit-cell length b length_b	77.590 Å
Unit-cell length c length_c	119.270 Å
Unit-cell angle α angle_alpha	86.88 °
Unit-cell angle β angle_beta	89.00 °
Unit-cell angle γ angle_gamma	84.27 °
Molecules per unit cell Z z_pdb	3

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

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	39.695 Å
R factor r_factor	0.2348
R_work r_work	0.2334
R_free r_free	0.2662

fit	/app/data/saxs_computation/ch/6ch2/6ch2.fit
pddf	/app/data/pr_computation/ch/6ch2/6ch2.pr.out
profile	/app/data/saxs_computation/ch/6ch2/6ch2.dat

Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex

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

Flagellar biosynthesis protein FlhA

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar hook-associated protein 2,Flagellar protein FliT

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar hook-associated protein 2,Flagellar protein FliT

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)