SAXSdb — 6pwb

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

Flagellin B1 (FlaB1)

OrganismNot specified

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 × 163 PDB declaration: 163-meric（163） Consistent with protein copy count	Chain AG； UniProt 8–272 Chain AH； UniProt 8–272 Chain AI； UniProt 8–272 Chain AR； UniProt 8–272 Chain BA； UniProt 8–272 Chain BB； UniProt 8–272 Chain BC； UniProt 8–272 Chain BD； UniProt 8–272 Chain BL； UniProt 8–272 Chain BM； UniProt 8–272 Chain BS； UniProt 8–272 Chain BT； UniProt 8–272 Chain BU； UniProt 8–272 Chain BV； UniProt 8–272 Chain BW； UniProt 8–272 Chain BX； UniProt 8–272 Chain BY； UniProt 8–272 Chain CG； UniProt 8–272 Chain CH； UniProt 8–272 Chain CL； UniProt 8–272 Chain CM； UniProt 8–272 Chain CN； UniProt 8–272 Chain CO； UniProt 8–272 Chain CP； UniProt 8–272 Chain CQ； UniProt 8–272 Chain CR； UniProt 8–272 Chain CS； UniProt 8–272 Chain CT； UniProt 8–272 Chain DB； UniProt 8–272 Chain DC； UniProt 8–272 Chain DG； UniProt 8–272 Chain DH； UniProt 8–272 Chain DI； UniProt 8–272 Chain DJ； UniProt 8–272 Chain DK； UniProt 8–272 Chain DL； UniProt 8–272 Chain DM； UniProt 8–272 Chain DN； UniProt 8–272 Chain DO； UniProt 8–272 Chain DW； UniProt 8–272 Chain DX； UniProt 8–272 Chain EB； UniProt 8–272 Chain EC； UniProt 8–272 Chain ED； UniProt 8–272 Chain EE； UniProt 8–272 Chain EF； UniProt 8–272 Chain EG； UniProt 8–272 Chain EH； UniProt 8–272 Chain EI； UniProt 8–272 Chain EJ； UniProt 8–272 Chain ER； UniProt 8–272 Chain ES； UniProt 8–272 Chain EW； UniProt 8–272 Chain EX； UniProt 8–272 Chain EY； UniProt 8–272 Chain EZ； UniProt 8–272 Chain FA； UniProt 8–272 Chain FB； UniProt 8–272 Chain FC； UniProt 8–272 Chain FD； UniProt 8–272 Chain FE； UniProt 8–272 Chain FM； UniProt 8–272 Chain FN； UniProt 8–272 Chain FR； UniProt 8–272 Chain FS； UniProt 8–272 Chain FT； UniProt 8–272 Chain FU； UniProt 8–272 Chain FV； UniProt 8–272 Chain FW； UniProt 8–272 Chain FX； UniProt 8–272 Chain GH； UniProt 8–272 Chain GI； UniProt 8–272 Chain GM； UniProt 8–272 Chain GN； UniProt 8–272 Chain GO； UniProt 8–272 Chain GP； UniProt 8–272 Chain GQ； UniProt 8–272 Chain GR； UniProt 8–272 Chain HC； UniProt 8–272 Chain HH； UniProt 8–272 Chain HI； UniProt 8–272 Chain HJ； UniProt 8–272 Chain HK； UniProt 8–272 Chain HL； UniProt 8–272	Not recorded	Flagellar coiling protein A (FcpA) × 47 （B0STJ8） Flagellar coiling protein B (FcpB) × 32 （B0SR03）	ELECTRON MICROSCOPY cryo-EM buffer：pH 6.8；Tris-HCl or ddH20, pH6.8 with <1% sodium azide as a preservative. FIDUCIAL MARKERS: Prior to vitrification, 1 uL of 6x concentrated Gold Tracer beads (10 nm colloidal gold) were mixed with 2 uL of purified flagella. To each grid, 3 uL of this mixture were applied. cryo-EM vitrification conditions：Cryogen ETHANE；2 minute incubation time; blot time of 6-7.5 seconds; and blot offset of -2 mm	Resolution 9.83 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 6PWB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9X7K core filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric	Chain A 1–281（281 aa） Chain B 1–281（281 aa） Chain C 1–281（281 aa） Chain D 1–281（281 aa） Chain E 1–281（281 aa） Chain F 1–281（281 aa） Chain G 1–281（281 aa） Chain H 1–281（281 aa） Chain I 1–281（281 aa） Chain J 1–281（281 aa） Chain K 1–281（281 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.35 Å
9X7L core filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain Deposited 2025-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric	Chain A 1–281（281 aa） Chain B 1–281（281 aa） Chain C 1–281（281 aa） Chain D 1–281（281 aa） Chain E 1–281（281 aa） Chain F 1–281（281 aa） Chain G 1–281（281 aa） Chain H 1–281（281 aa） Chain I 1–281（281 aa） Chain J 1–281（281 aa） Chain K 1–281（281 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
9X7M core filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain Deposited 2025-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric	Chain A 1–281（281 aa） Chain B 1–281（281 aa） Chain C 1–281（281 aa） Chain D 1–281（281 aa） Chain E 1–281（281 aa） Chain F 1–281（281 aa） Chain G 1–281（281 aa） Chain H 1–281（281 aa） Chain I 1–281（281 aa） Chain J 1–281（281 aa） Chain K 1–281（281 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å

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

View Construct and Data Evidence

UniProt name	B0SSZ5_LEPBP
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain AG； PDBConstruct 1–265； UniProt 8–272 Author chain AH； PDBConstruct 1–265； UniProt 8–272 Author chain AI； PDBConstruct 1–265； UniProt 8–272 Author chain AR； PDBConstruct 1–265； UniProt 8–272 Author chain BA； PDBConstruct 1–265； UniProt 8–272 Author chain BB； PDBConstruct 1–265； UniProt 8–272 Author chain BC； PDBConstruct 1–265； UniProt 8–272 Author chain BD； PDBConstruct 1–265； UniProt 8–272 Author chain BL； PDBConstruct 1–265； UniProt 8–272 Author chain BM； PDBConstruct 1–265； UniProt 8–272 Author chain BS； PDBConstruct 1–265； UniProt 8–272 Author chain BT； PDBConstruct 1–265； UniProt 8–272 Author chain BU； PDBConstruct 1–265； UniProt 8–272 Author chain BV； PDBConstruct 1–265； UniProt 8–272 Author chain BW； PDBConstruct 1–265； UniProt 8–272 Author chain BX； PDBConstruct 1–265； UniProt 8–272 Author chain BY； PDBConstruct 1–265； UniProt 8–272 Author chain CG； PDBConstruct 1–265； UniProt 8–272 Author chain CH； PDBConstruct 1–265； UniProt 8–272 Author chain CL； PDBConstruct 1–265； UniProt 8–272 Author chain CM； PDBConstruct 1–265； UniProt 8–272 Author chain CN； PDBConstruct 1–265； UniProt 8–272 Author chain CO； PDBConstruct 1–265； UniProt 8–272 Author chain CP； PDBConstruct 1–265； UniProt 8–272 Author chain CQ； PDBConstruct 1–265； UniProt 8–272 Author chain CR； PDBConstruct 1–265； UniProt 8–272 Author chain CS； PDBConstruct 1–265； UniProt 8–272 Author chain CT； PDBConstruct 1–265； UniProt 8–272 Author chain DB； PDBConstruct 1–265； UniProt 8–272 Author chain DC； PDBConstruct 1–265； UniProt 8–272 Author chain DG； PDBConstruct 1–265； UniProt 8–272 Author chain DH； PDBConstruct 1–265； UniProt 8–272 Author chain DI； PDBConstruct 1–265； UniProt 8–272 Author chain DJ； PDBConstruct 1–265； UniProt 8–272 Author chain DK； PDBConstruct 1–265； UniProt 8–272 Author chain DL； PDBConstruct 1–265； UniProt 8–272 Author chain DM； PDBConstruct 1–265； UniProt 8–272 Author chain DN； PDBConstruct 1–265； UniProt 8–272 Author chain DO； PDBConstruct 1–265； UniProt 8–272 Author chain DW； PDBConstruct 1–265； UniProt 8–272 Author chain DX； PDBConstruct 1–265； UniProt 8–272 Author chain EB； PDBConstruct 1–265； UniProt 8–272 Author chain EC； PDBConstruct 1–265； UniProt 8–272 Author chain ED； PDBConstruct 1–265； UniProt 8–272 Author chain EE； PDBConstruct 1–265； UniProt 8–272 Author chain EF； PDBConstruct 1–265； UniProt 8–272 Author chain EG； PDBConstruct 1–265； UniProt 8–272 Author chain EH； PDBConstruct 1–265； UniProt 8–272 Author chain EI； PDBConstruct 1–265； UniProt 8–272 Author chain EJ； PDBConstruct 1–265； UniProt 8–272 Author chain ER； PDBConstruct 1–265； UniProt 8–272 Author chain ES； PDBConstruct 1–265； UniProt 8–272 Author chain EW； PDBConstruct 1–265； UniProt 8–272 Author chain EX； PDBConstruct 1–265； UniProt 8–272 Author chain EY； PDBConstruct 1–265； UniProt 8–272 Author chain EZ； PDBConstruct 1–265； UniProt 8–272 Author chain FA； PDBConstruct 1–265； UniProt 8–272 Author chain FB； PDBConstruct 1–265； UniProt 8–272 Author chain FC； PDBConstruct 1–265； UniProt 8–272 Author chain FD； PDBConstruct 1–265； UniProt 8–272 Author chain FE； PDBConstruct 1–265； UniProt 8–272 Author chain FM； PDBConstruct 1–265； UniProt 8–272 Author chain FN； PDBConstruct 1–265； UniProt 8–272 Author chain FR； PDBConstruct 1–265； UniProt 8–272 Author chain FS； PDBConstruct 1–265； UniProt 8–272 Author chain FT； PDBConstruct 1–265； UniProt 8–272 Author chain FU； PDBConstruct 1–265； UniProt 8–272 Author chain FV； PDBConstruct 1–265； UniProt 8–272 Author chain FW； PDBConstruct 1–265； UniProt 8–272 Author chain FX； PDBConstruct 1–265； UniProt 8–272 Author chain GH； PDBConstruct 1–265； UniProt 8–272 Author chain GI； PDBConstruct 1–265； UniProt 8–272 Author chain GM； PDBConstruct 1–265； UniProt 8–272 Author chain GN； PDBConstruct 1–265； UniProt 8–272 Author chain GO； PDBConstruct 1–265； UniProt 8–272 Author chain GP； PDBConstruct 1–265； UniProt 8–272 Author chain GQ； PDBConstruct 1–265； UniProt 8–272 Author chain GR； PDBConstruct 1–265； UniProt 8–272 Author chain HC； PDBConstruct 1–265； UniProt 8–272 Author chain HH； PDBConstruct 1–265； UniProt 8–272 Author chain HI； PDBConstruct 1–265； UniProt 8–272 Author chain HJ； PDBConstruct 1–265； UniProt 8–272 Author chain HK； PDBConstruct 1–265； UniProt 8–272 Author chain HL； PDBConstruct 1–265； UniProt 8–272

Flagellar coiling protein A (FcpA)

OrganismNot specified

UniProt B0STJ8

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 × 163 PDB declaration: 163-meric（163） Consistent with protein copy count	Chain AL； UniProt 55–291 Chain AM； UniProt 55–291 Chain AU； UniProt 55–291 Chain BE； UniProt 55–291 Chain BF； UniProt 55–291 Chain BG； UniProt 55–291 Chain BH； UniProt 55–291 Chain BN； UniProt 55–291 Chain BP； UniProt 55–291 Chain BZ； UniProt 55–291 Chain CA； UniProt 55–291 Chain CB； UniProt 55–291 Chain CC； UniProt 55–291 Chain CI； UniProt 55–291 Chain CK； UniProt 55–291 Chain CU； UniProt 55–291 Chain CV； UniProt 55–291 Chain CW； UniProt 55–291 Chain CX； UniProt 55–291 Chain DD； UniProt 55–291 Chain DF； UniProt 55–291 Chain DP； UniProt 55–291 Chain DQ； UniProt 55–291 Chain DR； UniProt 55–291 Chain DS； UniProt 55–291 Chain DY； UniProt 55–291 Chain EA； UniProt 55–291 Chain EK； UniProt 55–291 Chain EL； UniProt 55–291 Chain EM； UniProt 55–291 Chain EN； UniProt 55–291 Chain ET； UniProt 55–291 Chain EV； UniProt 55–291 Chain FF； UniProt 55–291 Chain FG； UniProt 55–291 Chain FH； UniProt 55–291 Chain FI； UniProt 55–291 Chain FO； UniProt 55–291 Chain FQ； UniProt 55–291 Chain GA； UniProt 55–291 Chain GB； UniProt 55–291 Chain GC； UniProt 55–291 Chain GJ； UniProt 55–291 Chain GL； UniProt 55–291 Chain GV； UniProt 55–291 Chain GW； UniProt 55–291 Chain HE； UniProt 55–291	Not recorded	Flagellin B1 (FlaB1) × 84 （B0SSZ5） Flagellar coiling protein B (FcpB) × 32 （B0SR03）	ELECTRON MICROSCOPY cryo-EM buffer：pH 6.8；Tris-HCl or ddH20, pH6.8 with <1% sodium azide as a preservative. FIDUCIAL MARKERS: Prior to vitrification, 1 uL of 6x concentrated Gold Tracer beads (10 nm colloidal gold) were mixed with 2 uL of purified flagella. To each grid, 3 uL of this mixture were applied. cryo-EM vitrification conditions：Cryogen ETHANE；2 minute incubation time; blot time of 6-7.5 seconds; and blot offset of -2 mm	Resolution 9.83 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 6PWB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6NQW Flagellar protein FcpA from Leptospira biflexa - hexagonal form Deposited 2019-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 34–300（267 aa）	Not recorded	GOL GLYCEROL × 40 PO4 PHOSPHATE ION × 12 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；293 K；PEG 8000, Na/K phosphate, NaCl	Resolution 1.90 Å R-free 0.219
6NQX Flagellar protein FcpA from Leptospira biflexa / primitive monoclinic form Deposited 2019-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 34–300（267 aa） Fragment：residues 34-300 Chain B 34–300（267 aa） Fragment：residues 34-300 Chain C 34–300（267 aa） Fragment：residues 34-300 Chain D 34–300（267 aa） Fragment：residues 34-300	Not recorded	GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 4000, TrisHCl	Resolution 2.95 Å R-free 0.222
6NQY Flagellar protein FcpA from Leptospira biflexa / ab-centered monoclinic form Deposited 2019-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 34–300（267 aa） Fragment：residues 34-300 Chain B 34–300（267 aa） Fragment：residues 34-300	Not recorded	GOL GLYCEROL × 4 IOD IODIDE ION × 29 PEG DI(HYDROXYETHYL)ETHER × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 400, TrisHCl	Resolution 2.50 Å R-free 0.221
9X7S sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain Deposited 2025-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain B 1–300（300 aa） Chain K 1–300（300 aa） Chain N 1–300（300 aa） Chain Q 1–300（300 aa） Chain Z 1–300（300 aa） Chain c 1–300（300 aa） Chain f 1–300（300 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
9X7V Sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain Deposited 2025-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain B 1–300（300 aa） Chain K 1–300（300 aa） Chain N 1–300（300 aa） Chain Q 1–300（300 aa） Chain Z 1–300（300 aa） Chain c 1–300（300 aa） Chain f 1–300（300 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9X80 sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain K 1–300（300 aa） Chain N 1–300（300 aa） Chain Q 1–300（300 aa） Chain Z 1–300（300 aa） Chain c 1–300（300 aa） Chain f 1–300（300 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	B0STJ8_LEPBP
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain AL； PDBConstruct 1–237； UniProt 55–291 Author chain AM； PDBConstruct 1–237； UniProt 55–291 Author chain AU； PDBConstruct 1–237； UniProt 55–291 Author chain BE； PDBConstruct 1–237； UniProt 55–291 Author chain BF； PDBConstruct 1–237； UniProt 55–291 Author chain BG； PDBConstruct 1–237； UniProt 55–291 Author chain BH； PDBConstruct 1–237； UniProt 55–291 Author chain BN； PDBConstruct 1–237； UniProt 55–291 Author chain BP； PDBConstruct 1–237； UniProt 55–291 Author chain BZ； PDBConstruct 1–237； UniProt 55–291 Author chain CA； PDBConstruct 1–237； UniProt 55–291 Author chain CB； PDBConstruct 1–237； UniProt 55–291 Author chain CC； PDBConstruct 1–237； UniProt 55–291 Author chain CI； PDBConstruct 1–237； UniProt 55–291 Author chain CK； PDBConstruct 1–237； UniProt 55–291 Author chain CU； PDBConstruct 1–237； UniProt 55–291 Author chain CV； PDBConstruct 1–237； UniProt 55–291 Author chain CW； PDBConstruct 1–237； UniProt 55–291 Author chain CX； PDBConstruct 1–237； UniProt 55–291 Author chain DD； PDBConstruct 1–237； UniProt 55–291 Author chain DF； PDBConstruct 1–237； UniProt 55–291 Author chain DP； PDBConstruct 1–237； UniProt 55–291 Author chain DQ； PDBConstruct 1–237； UniProt 55–291 Author chain DR； PDBConstruct 1–237； UniProt 55–291 Author chain DS； PDBConstruct 1–237； UniProt 55–291 Author chain DY； PDBConstruct 1–237； UniProt 55–291 Author chain EA； PDBConstruct 1–237； UniProt 55–291 Author chain EK； PDBConstruct 1–237； UniProt 55–291 Author chain EL； PDBConstruct 1–237； UniProt 55–291 Author chain EM； PDBConstruct 1–237； UniProt 55–291 Author chain EN； PDBConstruct 1–237； UniProt 55–291 Author chain ET； PDBConstruct 1–237； UniProt 55–291 Author chain EV； PDBConstruct 1–237； UniProt 55–291 Author chain FF； PDBConstruct 1–237； UniProt 55–291 Author chain FG； PDBConstruct 1–237； UniProt 55–291 Author chain FH； PDBConstruct 1–237； UniProt 55–291 Author chain FI； PDBConstruct 1–237； UniProt 55–291 Author chain FO； PDBConstruct 1–237； UniProt 55–291 Author chain FQ； PDBConstruct 1–237； UniProt 55–291 Author chain GA； PDBConstruct 1–237； UniProt 55–291 Author chain GB； PDBConstruct 1–237； UniProt 55–291 Author chain GC； PDBConstruct 1–237； UniProt 55–291 Author chain GJ； PDBConstruct 1–237； UniProt 55–291 Author chain GL； PDBConstruct 1–237； UniProt 55–291 Author chain GV； PDBConstruct 1–237； UniProt 55–291 Author chain GW； PDBConstruct 1–237； UniProt 55–291 Author chain HE； PDBConstruct 1–237； UniProt 55–291

Flagellar coiling protein B (FcpB)

OrganismNot specified

UniProt B0SR03

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 × 163 PDB declaration: 163-meric（163） Consistent with protein copy count	Chain AO； UniProt 37–257 Chain BI； UniProt 37–257 Chain BJ； UniProt 37–257 Chain BK； UniProt 37–257 Chain BO； UniProt 37–257 Chain CD； UniProt 37–257 Chain CE； UniProt 37–257 Chain CF； UniProt 37–257 Chain CJ； UniProt 37–257 Chain CY； UniProt 37–257 Chain CZ； UniProt 37–257 Chain DA； UniProt 37–257 Chain DE； UniProt 37–257 Chain DT； UniProt 37–257 Chain DU； UniProt 37–257 Chain DV； UniProt 37–257 Chain DZ； UniProt 37–257 Chain EO； UniProt 37–257 Chain EP； UniProt 37–257 Chain EQ； UniProt 37–257 Chain EU； UniProt 37–257 Chain FJ； UniProt 37–257 Chain FK； UniProt 37–257 Chain FL； UniProt 37–257 Chain FP； UniProt 37–257 Chain GE； UniProt 37–257 Chain GF； UniProt 37–257 Chain GG； UniProt 37–257 Chain GK； UniProt 37–257 Chain GZ； UniProt 37–257 Chain HB； UniProt 37–257 Chain HF； UniProt 37–257	Not recorded	Flagellin B1 (FlaB1) × 84 （B0SSZ5） Flagellar coiling protein A (FcpA) × 47 （B0STJ8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 6.8；Tris-HCl or ddH20, pH6.8 with <1% sodium azide as a preservative. FIDUCIAL MARKERS: Prior to vitrification, 1 uL of 6x concentrated Gold Tracer beads (10 nm colloidal gold) were mixed with 2 uL of purified flagella. To each grid, 3 uL of this mixture were applied. cryo-EM vitrification conditions：Cryogen ETHANE；2 minute incubation time; blot time of 6-7.5 seconds; and blot offset of -2 mm	Resolution 9.83 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 6PWB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9LRY Straight and symmetrical filament of the spirochete periplasmic flagella of Leptospira biflexa Deposited 2025-02-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–277（277 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9X7S sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain Deposited 2025-10-17	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain L 1–277（277 aa） Chain O 1–277（277 aa） Chain R 1–277（277 aa） Chain a 1–277（277 aa） Chain d 1–277（277 aa） Chain g 1–277（277 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.83 Å
9X80 sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain L 1–277（277 aa） Chain O 1–277（277 aa） Chain R 1–277（277 aa） Chain a 1–277（277 aa） Chain d 1–277（277 aa） Chain g 1–277（277 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å

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

View Construct and Data Evidence

UniProt name	B0SR03_LEPBP
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain AO； PDBConstruct 1–221； UniProt 37–257 Author chain BI； PDBConstruct 1–221； UniProt 37–257 Author chain BJ； PDBConstruct 1–221； UniProt 37–257 Author chain BK； PDBConstruct 1–221； UniProt 37–257 Author chain BO； PDBConstruct 1–221； UniProt 37–257 Author chain CD； PDBConstruct 1–221； UniProt 37–257 Author chain CE； PDBConstruct 1–221； UniProt 37–257 Author chain CF； PDBConstruct 1–221； UniProt 37–257 Author chain CJ； PDBConstruct 1–221； UniProt 37–257 Author chain CY； PDBConstruct 1–221； UniProt 37–257 Author chain CZ； PDBConstruct 1–221； UniProt 37–257 Author chain DA； PDBConstruct 1–221； UniProt 37–257 Author chain DE； PDBConstruct 1–221； UniProt 37–257 Author chain DT； PDBConstruct 1–221； UniProt 37–257 Author chain DU； PDBConstruct 1–221； UniProt 37–257 Author chain DV； PDBConstruct 1–221； UniProt 37–257 Author chain DZ； PDBConstruct 1–221； UniProt 37–257 Author chain EO； PDBConstruct 1–221； UniProt 37–257 Author chain EP； PDBConstruct 1–221； UniProt 37–257 Author chain EQ； PDBConstruct 1–221； UniProt 37–257 Author chain EU； PDBConstruct 1–221； UniProt 37–257 Author chain FJ； PDBConstruct 1–221； UniProt 37–257 Author chain FK； PDBConstruct 1–221； UniProt 37–257 Author chain FL； PDBConstruct 1–221； UniProt 37–257 Author chain FP； PDBConstruct 1–221； UniProt 37–257 Author chain GE； PDBConstruct 1–221； UniProt 37–257 Author chain GF； PDBConstruct 1–221； UniProt 37–257 Author chain GG； PDBConstruct 1–221； UniProt 37–257 Author chain GK； PDBConstruct 1–221； UniProt 37–257 Author chain GZ； PDBConstruct 1–221； UniProt 37–257 Author chain HB； PDBConstruct 1–221； UniProt 37–257 Author chain HF； PDBConstruct 1–221； UniProt 37–257

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	6pwb
Deposition date deposition_date	2019-07-22
Structure title title	Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging
Keywords keywords	bacterial flagella, FcpA, FcpB, FlaA, FlaB, Leptospira, 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	— Å
Radius of gyration Rg (electron density) rg_electron	139.30 Å
Forward intensity I(0) i0	174619000000.00
Molecular weight molecular_weight	2203000.0 kDa
Excluded volume excluded_volume	2167000 Å³
Envelope volume envelope_volume	8299100 Å³
Hydration-shell volume shell_volume	520550 Å³
Envelope diameter envelope_diameter	524.4 Å
Shell Rg shell_rg	118.50 Å
Envelope Rg envelope_rg	136.50 Å
Shape Rg shape_rg	139.30 Å
Total Rg total_rg	139.20 Å
Total atoms total_atoms	157148
Residues n_residues	39287
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	396.9 Å
Rg (real space) rg_real	131.20 Å
Rg uncertainty (real space) rg_real_error	1.88 Å
I(0) (real space) i0_real	1.6730e+11
I(0) uncertainty (real space) i0_real_error	4.0500e+09
Rg (reciprocal space) rg_reciprocal	119.00 Å
I(0) (reciprocal space) i0_reciprocal	163200000000.0000
Solution quality estimate total_estimate	0.8900
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	144.3 Å
Skewness Skewness skewness	0.513
Kurtosis Kurtosis kurtosis	-0.429
Angular range angular_range	— – 0.0550 Å⁻¹
Current regularization parameter α current_alpha	1.1340
Highest regularization parameter α highest_alpha	110100000000.0000
Real-space data points n_real_points	12
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.012; Oscil: 0.902; Stabil: 0.982; Sysdev: 1.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.010

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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	Flagellin B1 (FlaB1)
Molecular weight formula_weight	29467.0 kDa
Source method src_method	nat
Copy count entity_count	84

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;AG,AH,AI,AR,BA,BB,BC,BD,BL,BM,CG,CH,BS,BT,BU,BV,BW,BX,BY,DB,DC,CL,CM,CN,CO,CP,CQ,CR,CS,CT,DG,DH,DI,DJ,DK,DL,DM,DN,DO,DW,DX,EB,EC,ED,EE,EF,EG,EH,EI,EJ,ER,ES,FA,FB,FC,FD,FE,FM,FN,EW,EX,EY,EZ,GH,GI,FR,FS,FT,FU,FV,FW,FX,HC,GM,GN,GO,GP,GQ,GR,HH,HI,HJ,HK,HL ;
Atom count atom_count	157148

AAINSHRVLKFQNEEVSKNMEKLSSGMRINRAGDDASGLAVSEKMRTQVNGLRQAERNTEDGMSLIQTTEGFLQESNDIIQRIRTLAIQSSNGIYTEEDRQMIQVEVSQLIDEVDRIASQAEFNKMNLLQGDFARGSRATSMWFHIGPNMHQRERVFIATMTARSLNLKGQSGELLSLSTADKSNDAIGTLDAALTRISKQRANLGAYFNRLEHAAKGLMNAYENTQASESRIRDADMAEETVAFTKNQILVQSGTAMLAQANVR

Entity 2 Entity 2 polymer

Description description	Flagellar coiling protein A (FcpA)
Molecular weight formula_weight	28931.0 kDa
Source method src_method	nat
Copy count entity_count	47

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	;AL,AM,AU,BE,BF,BG,BH,BN,BP,CA,CB,CC,CI,CK,BZ,DD,DF,CU,CV,CW,CX,EA,DP,DQ,DR,DS,DY,EK,EL,EM,EN,ET,EV,FF,FG,FH,FI,FO,FQ,GA,GB,GC,GJ,GL,HE,GV,GW ;

LTEDQKKKKKEIMEQESLWKNPDFKGYNKTFQELHQLSKTFANNQFRLALSNYQSGVNTIMKNRDWVEQYRKEEAEKKRLDEKWYWQKVDRKAREERVVYREKMKAKQDALNYFSKAINHLDEIKNPDLRERPEFKRLLSDVYRSWIMAEYDLQNLPQTIPILELYIEIDDNEKEYPAHKYLASAYSFEENMIKKTKGPDDMLFKYRYKKNVHLLRATELKYGKDSPEYKHIVNVIN

Entity 3 Entity 3 polymer

Description description	Flagellar coiling protein B (FcpB)
Molecular weight formula_weight	25539.7 kDa
Source method src_method	nat
Copy count entity_count	32

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	AO,BI,BJ,BK,BO,CD,CE,CF,CJ,DA,DE,CY,CZ,DT,DU,DV,DZ,EO,EP,EQ,EU,FJ,FK,FL,FP,GE,GF,GG,GK,HB,HF,GZ

SGKSMADTEKELDDNISEVNKRLRLHTVLFKMKVRTLPHKTVLYKGKPSADGERCEAADKQEAQDNTCLHLEVFDFVGSEDGKSSKNLGAKFKKMELFFEGSNNADPDPRKEQPRNLTKIRTYIYQNNFLLEDKVISVIADVAPNGEPAHNDKIELFYQHDDYPVWGTPETPSEKGVGKYILSNVENTKSNPIRNNFKKQFYFKNLDYFDKLFTKIFDYND

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8. Citations (4)

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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	9.83 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	10581

fit	/app/data/saxs_computation/pw/6pwb/6pwb.fit
pddf	/app/data/pr_computation/pw/6pwb/6pwb.pr.out
profile	/app/data/saxs_computation/pw/6pwb/6pwb.dat

Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging

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

Flagellin B1 (FlaB1)

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar coiling protein A (FcpA)

State in the Current Structure

Other States of the Same Protein in the Database

Flagellar coiling protein B (FcpB)

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)