8wkk

Cryo-EM structure of the whole rod with export apparatus and hook within the flagellar motor-hook complex in the CW state.

Method: ELECTRON MICROSCOPY Dmax: 334.2 Å Quality: GOOD

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

Flagellar biosynthetic protein FliQ

OrganismNot specified

UniProt P0A1L5

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain A; UniProt 1–89 Chain B; UniProt 1–89 Chain C; UniProt 1–89 Chain D; UniProt 1–89 Not recorded Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIQ_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–89; UniProt 1–89 Author chain B; PDBConstruct 1–89; UniProt 1–89 Author chain C; PDBConstruct 1–89; UniProt 1–89 Author chain D; PDBConstruct 1–89; UniProt 1–89

Flagellar biosynthetic protein FliR

OrganismNot specified

UniProt P54702

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain E; UniProt 1–264 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name FLIR_SALTY
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–264; UniProt 1–264

Flagellar biosynthetic protein FliP

OrganismNot specified

UniProt P54700

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain F; UniProt 1–245 Chain G; UniProt 1–245 Chain H; UniProt 1–245 Chain I; UniProt 1–245 Chain J; UniProt 1–245 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIP_SALTY
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–245; UniProt 1–245 Author chain G; PDBConstruct 1–245; UniProt 1–245 Author chain H; PDBConstruct 1–245; UniProt 1–245 Author chain I; PDBConstruct 1–245; UniProt 1–245 Author chain J; PDBConstruct 1–245; UniProt 1–245

Flagellar hook-basal body complex protein FliE

OrganismNot specified

UniProt P26462

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain K; UniProt 1–104 Chain L; UniProt 1–104 Chain M; UniProt 1–104 Chain N; UniProt 1–104 Chain O; UniProt 1–104 Chain P; UniProt 1–104 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIE_SALTY
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–104; UniProt 1–104 Author chain L; PDBConstruct 1–104; UniProt 1–104 Author chain M; PDBConstruct 1–104; UniProt 1–104 Author chain N; PDBConstruct 1–104; UniProt 1–104 Author chain O; PDBConstruct 1–104; UniProt 1–104 Author chain P; PDBConstruct 1–104; UniProt 1–104

Flagellar basal body rod protein FlgB

OrganismNot specified

UniProt P16437

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain Q; UniProt 1–138 Chain R; UniProt 1–138 Chain S; UniProt 1–138 Chain T; UniProt 1–138 Chain U; UniProt 1–138 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGB_SALTY
Isoform
PDB entities 5
Chains and sequence ranges Author chain Q; PDBConstruct 1–138; UniProt 1–138 Author chain R; PDBConstruct 1–138; UniProt 1–138 Author chain S; PDBConstruct 1–138; UniProt 1–138 Author chain T; PDBConstruct 1–138; UniProt 1–138 Author chain U; PDBConstruct 1–138; UniProt 1–138

Flagellar basal-body rod protein FlgC

OrganismNot specified

UniProt P0A1I7

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain V; UniProt 1–134 Chain W; UniProt 1–134 Chain X; UniProt 1–134 Chain Y; UniProt 1–134 Chain Z; UniProt 1–134 Chain a; UniProt 1–134 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name FLGC_SALTY
Isoform
PDB entities 6
Chains and sequence ranges Author chain V; PDBConstruct 1–134; UniProt 1–134 Author chain W; PDBConstruct 1–134; UniProt 1–134 Author chain X; PDBConstruct 1–134; UniProt 1–134 Author chain Y; PDBConstruct 1–134; UniProt 1–134 Author chain Z; PDBConstruct 1–134; UniProt 1–134 Author chain a; PDBConstruct 1–134; UniProt 1–134

Flagellar M-ring protein

OrganismNot specified

UniProt P15928

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain b; UniProt 1–560 Chain c; UniProt 1–560 Chain d; UniProt 1–560 Chain e; UniProt 1–560 Chain f; UniProt 1–560 Chain g; UniProt 1–560 Chain h; UniProt 1–560 Chain i; UniProt 1–560 Chain j; UniProt 1–560 Chain k; UniProt 1–560 Chain l; UniProt 1–560 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIF_SALTY
Isoform
PDB entities 7
Chains and sequence ranges Author chain b; PDBConstruct 1–560; UniProt 1–560 Author chain c; PDBConstruct 1–560; UniProt 1–560 Author chain d; PDBConstruct 1–560; UniProt 1–560 Author chain e; PDBConstruct 1–560; UniProt 1–560 Author chain f; PDBConstruct 1–560; UniProt 1–560 Author chain g; PDBConstruct 1–560; UniProt 1–560 Author chain h; PDBConstruct 1–560; UniProt 1–560 Author chain i; PDBConstruct 1–560; UniProt 1–560 Author chain j; PDBConstruct 1–560; UniProt 1–560 Author chain k; PDBConstruct 1–560; UniProt 1–560 Author chain l; PDBConstruct 1–560; UniProt 1–560

Flagellar basal-body rod protein FlgF

OrganismNot specified

UniProt P16323

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain m; UniProt 1–251 Chain n; UniProt 1–251 Chain o; UniProt 1–251 Chain p; UniProt 1–251 Chain q; UniProt 1–251 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGF_SALTY
Isoform
PDB entities 8
Chains and sequence ranges Author chain m; PDBConstruct 1–251; UniProt 1–251 Author chain n; PDBConstruct 1–251; UniProt 1–251 Author chain o; PDBConstruct 1–251; UniProt 1–251 Author chain p; PDBConstruct 1–251; UniProt 1–251 Author chain q; PDBConstruct 1–251; UniProt 1–251

Flagellar basal-body rod protein FlgG

OrganismNot specified

UniProt P0A1J3

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain 0; UniProt 1–260 Chain 1; UniProt 1–260 Chain 2; UniProt 1–260 Chain 3; UniProt 1–260 Chain 4; UniProt 1–260 Chain 5; UniProt 1–260 Chain 6; UniProt 1–260 Chain 7; UniProt 1–260 Chain 8; UniProt 1–260 Chain 9; UniProt 1–260 Chain ZA; UniProt 1–260 Chain ZB; UniProt 1–260 Chain ZC; UniProt 1–260 Chain ZD; UniProt 1–260 Chain ZE; UniProt 1–260 Chain r; UniProt 1–260 Chain s; UniProt 1–260 Chain t; UniProt 1–260 Chain u; UniProt 1–260 Chain v; UniProt 1–260 Chain w; UniProt 1–260 Chain x; UniProt 1–260 Chain y; UniProt 1–260 Chain z; UniProt 1–260 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar hook protein FlgE × 29 (P0A1J1) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGG_SALTY
Isoform
PDB entities 9
Chains and sequence ranges Author chain 0; PDBConstruct 1–260; UniProt 1–260 Author chain 1; PDBConstruct 1–260; UniProt 1–260 Author chain 2; PDBConstruct 1–260; UniProt 1–260 Author chain 3; PDBConstruct 1–260; UniProt 1–260 Author chain 4; PDBConstruct 1–260; UniProt 1–260 Author chain 5; PDBConstruct 1–260; UniProt 1–260 Author chain 6; PDBConstruct 1–260; UniProt 1–260 Author chain 7; PDBConstruct 1–260; UniProt 1–260 Author chain 8; PDBConstruct 1–260; UniProt 1–260 Author chain 9; PDBConstruct 1–260; UniProt 1–260 Author chain ZA; PDBConstruct 1–260; UniProt 1–260 Author chain ZB; PDBConstruct 1–260; UniProt 1–260 Author chain ZC; PDBConstruct 1–260; UniProt 1–260 Author chain ZD; PDBConstruct 1–260; UniProt 1–260 Author chain ZE; PDBConstruct 1–260; UniProt 1–260 Author chain r; PDBConstruct 1–260; UniProt 1–260 Author chain s; PDBConstruct 1–260; UniProt 1–260 Author chain t; PDBConstruct 1–260; UniProt 1–260 Author chain u; PDBConstruct 1–260; UniProt 1–260 Author chain v; PDBConstruct 1–260; UniProt 1–260 Author chain w; PDBConstruct 1–260; UniProt 1–260 Author chain x; PDBConstruct 1–260; UniProt 1–260 Author chain y; PDBConstruct 1–260; UniProt 1–260 Author chain z; PDBConstruct 1–260; UniProt 1–260

Flagellar hook protein FlgE

OrganismNot specified

UniProt P0A1J1

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 × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain ZF; UniProt 1–403 Chain ZG; UniProt 1–403 Chain ZH; UniProt 1–403 Chain ZI; UniProt 1–403 Chain ZJ; UniProt 1–403 Chain ZK; UniProt 1–403 Chain ZL; UniProt 1–403 Chain ZM; UniProt 1–403 Chain ZN; UniProt 1–403 Chain ZO; UniProt 1–403 Chain ZP; UniProt 1–403 Chain ZQ; UniProt 1–403 Chain ZR; UniProt 1–403 Chain ZS; UniProt 1–403 Chain ZT; UniProt 1–403 Chain ZU; UniProt 1–403 Chain ZV; UniProt 1–403 Chain ZW; UniProt 1–403 Chain ZX; UniProt 1–403 Chain ZY; UniProt 1–403 Chain ZZ; UniProt 1–403 Chain Za; UniProt 1–403 Chain Zb; UniProt 1–403 Chain Zc; UniProt 1–403 Chain Zd; UniProt 1–403 Chain Ze; UniProt 1–403 Chain Zf; UniProt 1–403 Chain Zg; UniProt 1–403 Chain Zh; UniProt 1–403 Not recorded Flagellar biosynthetic protein FliQ × 4 (P0A1L5) Flagellar biosynthetic protein FliR × 1 (P54702) Flagellar biosynthetic protein FliP × 5 (P54700) Flagellar hook-basal body complex protein FliE × 6 (P26462) Flagellar basal body rod protein FlgB × 5 (P16437) Flagellar basal-body rod protein FlgC × 6 (P0A1I7) Flagellar M-ring protein × 11 (P15928) Flagellar basal-body rod protein FlgF × 5 (P16323) Flagellar basal-body rod protein FlgG × 24 (P0A1J3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time: 4 Blot force: 10 Wait time: 30 Blot total: 1 Drain time: 2 Resolution 3.30 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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLGE_SALTY
Isoform
PDB entities 10
Chains and sequence ranges Author chain ZF; PDBConstruct 1–403; UniProt 1–403 Author chain ZG; PDBConstruct 1–403; UniProt 1–403 Author chain ZH; PDBConstruct 1–403; UniProt 1–403 Author chain ZI; PDBConstruct 1–403; UniProt 1–403 Author chain ZJ; PDBConstruct 1–403; UniProt 1–403 Author chain ZK; PDBConstruct 1–403; UniProt 1–403 Author chain ZL; PDBConstruct 1–403; UniProt 1–403 Author chain ZM; PDBConstruct 1–403; UniProt 1–403 Author chain ZN; PDBConstruct 1–403; UniProt 1–403 Author chain ZO; PDBConstruct 1–403; UniProt 1–403 Author chain ZP; PDBConstruct 1–403; UniProt 1–403 Author chain ZQ; PDBConstruct 1–403; UniProt 1–403 Author chain ZR; PDBConstruct 1–403; UniProt 1–403 Author chain ZS; PDBConstruct 1–403; UniProt 1–403 Author chain ZT; PDBConstruct 1–403; UniProt 1–403 Author chain ZU; PDBConstruct 1–403; UniProt 1–403 Author chain ZV; PDBConstruct 1–403; UniProt 1–403 Author chain ZW; PDBConstruct 1–403; UniProt 1–403 Author chain ZX; PDBConstruct 1–403; UniProt 1–403 Author chain ZY; PDBConstruct 1–403; UniProt 1–403 Author chain ZZ; PDBConstruct 1–403; UniProt 1–403 Author chain Za; PDBConstruct 1–403; UniProt 1–403 Author chain Zb; PDBConstruct 1–403; UniProt 1–403 Author chain Zc; PDBConstruct 1–403; UniProt 1–403 Author chain Zd; PDBConstruct 1–403; UniProt 1–403 Author chain Ze; PDBConstruct 1–403; UniProt 1–403 Author chain Zf; PDBConstruct 1–403; UniProt 1–403 Author chain Zg; PDBConstruct 1–403; UniProt 1–403 Author chain Zh; PDBConstruct 1–403; UniProt 1–403

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8wkk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wkk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wkk
Deposition date deposition_date2023-09-28
Structure title titleCryo-EM structure of the whole rod with export apparatus and hook within the flagellar motor-hook complex in the CW state.
Keywords keywordsFlagellum, Flagellar motor, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron122.30
Forward intensity I(0) i082652400000.00
Molecular weight molecular_weight2387700.0 kDa
Excluded volume excluded_volume2960400 ų
Envelope volume envelope_volume4543900 ų
Hydration-shell volume shell_volume337260 ų
Envelope diameter envelope_diameter492.7
Shell Rg shell_rg95.44
Envelope Rg envelope_rg125.60
Shape Rg shape_rg122.20
Total Rg total_rg122.60
Total atoms total_atoms167771
Residues n_residues22617
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax334.2
Rg (real space) rg_real108.20
Rg uncertainty (real space) rg_real_error2.23
I(0) (real space) i0_real7.9050e+10
I(0) uncertainty (real space) i0_real_error1.9310e+09
Rg (reciprocal space) rg_reciprocal101.30
I(0) (reciprocal space) i0_reciprocal78580000000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary102.8
Skewness Skewness skewness0.529
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha0.4530
Highest regularization parameter α highest_alpha4624000000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.028; Oscil: 0.899; Stabil: 0.991; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.013

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)