6soc

BamABCDE in MSP1D1 nanodisc ensemble 1-5

Method: ELECTRON MICROSCOPY Dmax: 135.9 Å Quality: EXCELLENT

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

Outer membrane protein assembly factor BamA

Escherichia coli

UniProt B7MBF8

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 24–806 Not recorded Outer membrane protein assembly factor BamB × 1 (A0A2S5ZNM3) Outer membrane protein assembly factor BamC × 1 (A0A4T5IPK3) Outer membrane protein assembly factor BamD × 1 (P0AC04) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

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

View Construct and Data Evidence
UniProt name BAMA_ECO45
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–783; UniProt 24–806

Outer membrane protein assembly factor BamB

Escherichia coli

UniProt A0A2S5ZNM3

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 22–392 Not recorded Outer membrane protein assembly factor BamA × 1 (B7MBF8) Outer membrane protein assembly factor BamC × 1 (A0A4T5IPK3) Outer membrane protein assembly factor BamD × 1 (P0AC04) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2S5ZNM3_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–371; UniProt 22–392

Outer membrane protein assembly factor BamC

Escherichia coli

UniProt A0A4T5IPK3

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 25–83 Not recorded Outer membrane protein assembly factor BamA × 1 (B7MBF8) Outer membrane protein assembly factor BamB × 1 (A0A2S5ZNM3) Outer membrane protein assembly factor BamD × 1 (P0AC04) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4T5IPK3_ECOLX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–59; UniProt 25–83

Outer membrane protein assembly factor BamD

Escherichia coli

UniProt P0AC04

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 26–243 Not recorded Outer membrane protein assembly factor BamA × 1 (B7MBF8) Outer membrane protein assembly factor BamB × 1 (A0A2S5ZNM3) Outer membrane protein assembly factor BamC × 1 (A0A4T5IPK3) Outer membrane protein assembly factor BamE × 1 (P0A938) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAMD_ECO57
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–218; UniProt 26–243

Outer membrane protein assembly factor BamE

Escherichia coli

UniProt P0A938

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 24–110 Not recorded Outer membrane protein assembly factor BamA × 1 (B7MBF8) Outer membrane protein assembly factor BamB × 1 (A0A2S5ZNM3) Outer membrane protein assembly factor BamC × 1 (A0A4T5IPK3) Outer membrane protein assembly factor BamD × 1 (P0AC04) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAME_ECOL6
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–87; UniProt 24–110

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 6soc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6soc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6soc
Deposition date deposition_date2019-08-29
Structure title titleBamABCDE in MSP1D1 nanodisc ensemble 1-5
Keywords keywordsOuter membrane, OMP, beta-barrel, folding, insertion, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.63
Radius of gyration Rg (electron density) rg_electron43.20
Forward intensity I(0) i0432541000.00
Molecular weight molecular_weight168110.0 kDa
Excluded volume excluded_volume208970 ų
Envelope volume envelope_volume279000 ų
Hydration-shell volume shell_volume55124 ų
Envelope diameter envelope_diameter131.6
Shell Rg shell_rg47.65
Envelope Rg envelope_rg41.15
Shape Rg shape_rg43.20
Total Rg total_rg43.42
Total atoms total_atoms11866
Residues n_residues1518
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 dmax135.9
Rg (real space) rg_real43.45
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real4.3250e+08
I(0) uncertainty (real space) i0_real_error7.0400e+06
Rg (reciprocal space) rg_reciprocal43.62
I(0) (reciprocal space) i0_reciprocal432600000.0000
Solution quality estimate total_estimate0.9050
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.028
Kurtosis Kurtosis kurtosis-0.735
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27010000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)