7ojf

CRYO-EM STRUCTURE OF SLYB13-BAMA FROM ESCHERICHIA COLI.

Method: ELECTRON MICROSCOPY Dmax: 129.0 Å Quality: GOOD

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

Outer membrane lipoprotein slyB

Escherichia coli BW25113

UniProt D2AGE2

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 1–155 Chain B; UniProt 1–155 Chain C; UniProt 1–155 Chain D; UniProt 1–155 Chain E; UniProt 1–155 Chain F; UniProt 1–155 Chain G; UniProt 1–155 Chain H; UniProt 1–155 Chain I; UniProt 1–155 Chain J; UniProt 1–155 Chain K; UniProt 1–155 Chain L; UniProt 1–155 Chain M; UniProt 1–155 Not recorded Outer membrane protein assembly factor BamA × 1 (C3TPJ2) PLM PALMITIC ACID × 13 L8Z (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(~{E},3~{R})-3-dodecanoyloxytetradec-5-enoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(~{E},3~{R})-3-oxidanyltetradec-11-enoyl]amino]-4-[(~{E},3~{R})-3-oxidanyltetradec-5-enoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(~{E},3~{R})-3-tetradecanoyloxytetradec-7-enoyl]oxy-oxan-2-yl]methoxy]-4,5-bis(oxidanyl)oxane-2-carboxylic acid × 13 LPP 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE × 12 GOL GLYCEROL × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Back-blotting for 4 seconds before plunging Resolution 3.90 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D2AGE2_SHIF2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–155; UniProt 1–155 Author chain B; PDBConstruct 1–155; UniProt 1–155 Author chain C; PDBConstruct 1–155; UniProt 1–155 Author chain D; PDBConstruct 1–155; UniProt 1–155 Author chain E; PDBConstruct 1–155; UniProt 1–155 Author chain F; PDBConstruct 1–155; UniProt 1–155 Author chain G; PDBConstruct 1–155; UniProt 1–155 Author chain H; PDBConstruct 1–155; UniProt 1–155 Author chain I; PDBConstruct 1–155; UniProt 1–155 Author chain J; PDBConstruct 1–155; UniProt 1–155 Author chain K; PDBConstruct 1–155; UniProt 1–155 Author chain L; PDBConstruct 1–155; UniProt 1–155 Author chain M; PDBConstruct 1–155; UniProt 1–155

Outer membrane protein assembly factor BamA

Escherichia coli BW25113

UniProt C3TPJ2

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain N; UniProt 1–810 Not recorded Outer membrane lipoprotein slyB × 13 (D2AGE2) PLM PALMITIC ACID × 13 L8Z (2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(~{E},3~{R})-3-dodecanoyloxytetradec-5-enoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(~{E},3~{R})-3-oxidanyltetradec-11-enoyl]amino]-4-[(~{E},3~{R})-3-oxidanyltetradec-5-enoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(~{E},3~{R})-3-tetradecanoyloxytetradec-7-enoyl]oxy-oxan-2-yl]methoxy]-4,5-bis(oxidanyl)oxane-2-carboxylic acid × 13 LPP 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE × 12 GOL GLYCEROL × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Back-blotting for 4 seconds before plunging Resolution 3.90 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 C3TPJ2_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 1–810; UniProt 1–810

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 7ojf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ojf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ojf
Deposition date deposition_date2021-05-14
Structure title titleCRYO-EM STRUCTURE OF SLYB13-BAMA FROM ESCHERICHIA COLI.
Keywords keywordsOUTER MEMBRANE CHAPERON, 2TM GLYCINE ZIPPER, OUTER MEMBRANE LIPOPROTEIN SLYB, LPS-LP BINDING PROTEIN, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.72
Radius of gyration Rg (electron density) rg_electron44.97
Forward intensity I(0) i01059610000.00
Molecular weight molecular_weight276010.0 kDa
Excluded volume excluded_volume349260 ų
Envelope volume envelope_volume545100 ų
Hydration-shell volume shell_volume97157 ų
Envelope diameter envelope_diameter126.8
Shell Rg shell_rg54.09
Envelope Rg envelope_rg42.64
Shape Rg shape_rg44.94
Total Rg total_rg45.51
Total atoms total_atoms19318
Residues n_residues2319
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 dmax129.0
Rg (real space) rg_real45.27
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.0600e+09
I(0) uncertainty (real space) i0_real_error1.8610e+07
Rg (reciprocal space) rg_reciprocal45.72
I(0) (reciprocal space) i0_reciprocal1060000000.0000
Solution quality estimate total_estimate0.8358
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.3
Skewness Skewness skewness-0.134
Kurtosis Kurtosis kurtosis-0.667
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118400000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)