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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 163	Flagellar coiling protein A (FcpA) × 47 （B0STJ8） Flagellar coiling protein B (FcpB) × 32 （B0SR03）	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 163	Flagellin B1 (FlaB1) × 84 （B0SSZ5） Flagellar coiling protein B (FcpB) × 32 （B0SR03）	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 163	Flagellin B1 (FlaB1) × 84 （B0SSZ5） Flagellar coiling protein A (FcpA) × 47 （B0STJ8）	Consistent with protein count

Other States of the Same Protein in the Database

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. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6pwb__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6pwb__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6pwb__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	0.00 Å
Rg (electron density)	139.30 Å
Total Rg	139.20 Å
Atom count	157148
Residues	39287
Excluded volume	2167000 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6pwb__assembly_1__model_1`	163-meric （163）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. 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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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Method resolution_method	—
颗粒数 num_particles	10581

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

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6pwb__assembly_1__model_1

6pwb__assembly_1__model_1 | I(q)

6pwb__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. 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

7. Citations (4)

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Flagellar coiling protein A (FcpA)

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Flagellar coiling protein B (FcpB)

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6pwb__assembly_1__model_1

6pwb__assembly_1__model_1 | I(q)

6pwb__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

5. 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

7. Citations (4)