SAXSdb — 6ch3

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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 360–690	Not recorded	Flagellar secretion chaperone FliS,Flagellin × 1 （P26609,P06179）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；tascimate	Resolution 2.68 Å R-free 0.258

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 6CH3	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
6CH2 Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex Deposited 2018-02-21	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 360–692（333 aa） Fragment：unp residues 360-692	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 360–692（333 aa） Fragment：unp residues 360-692	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 experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 360–692（333 aa） Fragment：unp residues 360-692	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
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 16 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 1–331； UniProt 360–690

Flagellar secretion chaperone FliS,Flagellin

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

UniProt P06179

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 B； UniProt 455–495	Not recorded	Flagellar biosynthesis protein FlhA × 1 （P40729）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；tascimate	Resolution 2.68 Å R-free 0.258

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 6CH3	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 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 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 oligomeric state 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 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
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 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 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 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	2
Chains and sequence ranges	Author chain B； PDBConstruct 158–198； UniProt 455–495

Flagellar secretion chaperone FliS,Flagellin

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

UniProt P26609

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 B； UniProt 1–135	Not recorded	Flagellar biosynthesis protein FlhA × 1 （P40729）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；tascimate	Resolution 2.68 Å R-free 0.258

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	FLIS_SALTY
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–135； UniProt 1–135

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	6ch3
Deposition date deposition_date	2018-02-21
Structure title title	Crystal structure of the cytoplasmic domain of FlhA and FliS-FliC 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	27.69 Å
Radius of gyration Rg (electron density) rg_electron	26.81 Å
Forward intensity I(0) i0	47026300.00
Molecular weight molecular_weight	53457.0 kDa
Excluded volume excluded_volume	67205 Å³
Envelope volume envelope_volume	86258 Å³
Hydration-shell volume shell_volume	27610 Å³
Envelope diameter envelope_diameter	93.6 Å
Shell Rg shell_rg	33.20 Å
Envelope Rg envelope_rg	26.49 Å
Shape Rg shape_rg	26.80 Å
Total Rg total_rg	27.54 Å
Total atoms total_atoms	3759
Residues n_residues	486
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	88.0 Å
Rg (real space) rg_real	27.67 Å
Rg uncertainty (real space) rg_real_error	0.53 Å
I(0) (real space) i0_real	4.7030e+07
I(0) uncertainty (real space) i0_real_error	6.9750e+05
Rg (reciprocal space) rg_reciprocal	27.68 Å
I(0) (reciprocal space) i0_reciprocal	47030000.0000
Solution quality estimate total_estimate	0.9082
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	34.0 Å
Skewness Skewness skewness	0.263
Kurtosis Kurtosis kurtosis	-0.495
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11320000.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.969

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Flagellar biosynthesis protein FlhA
Molecular weight formula_weight	36497.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3765

EDSLGMEVGYRLIPMVDFQQDGELLGRIRSIRKKFAQDMGFLPPVVHIRDNMDLQPARYRILMKGVEIGSGDAYPGRWLAINPGTAAGTLPGEKTVDPAFGLDAIWIESALKEQAQIQGFTVVEASTVVATHLNHLIGQFSAELFGRQEAQQLLDRVSQEMPKLTEDLVPGVVTLTTLHKVLQNLLAEKVPIRDMRTILETLAEHAPLQSDPHELTAVVRVALGRAITQQWFPGNEEVQVIGLDTALERLLLQALQGGGGLEPGLADRLLAQTQEALSRQEMLGAPPVLLVNHALRPLLSRFLRRSLPQLVVLSNLELSDNRHIRMTATIG

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 secretion chaperone FliS,Flagellin
Molecular weight formula_weight	20925.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MYTASGIKAYAQVSVESAVMSASPHQLIEMLFDGANSALVRARLFLEQGDVVAKGEALSKAINIIDNGLKAGLDQEKGGEIATNLSELYDYMIRRLLQANLRNDAQAIEEVERLLSNIAEAWKQISPKASFQESRGTASGAGGSEGGGSEGGTSGATEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR

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 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	6

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	6ch3A01
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	73.298 Å
Unit-cell length b length_b	88.623 Å
Unit-cell length c length_c	117.327 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.680 Å
Low-resolution limit resolution_low	34.982 Å
R factor r_factor	0.2345
R_work r_work	0.2332
R_free r_free	0.2576

fit	/app/data/saxs_computation/ch/6ch3/6ch3.fit
pddf	/app/data/pr_computation/ch/6ch3/6ch3.pr.out
profile	/app/data/saxs_computation/ch/6ch3/6ch3.dat

Crystal structure of the cytoplasmic domain of FlhA and FliS-FliC 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 secretion chaperone FliS,Flagellin

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar secretion chaperone FliS,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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)