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1bsn

SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX

Method: SOLUTION NMR Dmax: 58.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (EPSILON SUBUNIT)

Escherichia coli

UniProt P0A6E6

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–138 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7.4；295 K；Ionic strength (raw mmCIF value) 0.03；Pressure 10000 Resolution not provided

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 1BSN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AQT EPSILON SUBUNIT OF F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI Deposited 1997-07-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 3–138（136 aa） Fragment：EPSILON CHAIN
Mutation：A1G, M2S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；PROTEIN (4 MG/ML)IN 50 MM HEPES BUFFER, PH 7.5, 200 MM (NH2)2SO4, 2 M (NA/K)PO4
Resolution 2.30 Å R-free 0.288
1BSH SOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX Deposited 1998-08-27 Parsed fields agree Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–138（138 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；295 K；Ionic strength (raw mmCIF value) 0.03；Pressure 10000
Resolution not provided
1FS0 COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI Deposited 2000-09-07 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 1–138（138 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；0.5M tartrate, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.269
1FS0 COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI Deposited 2000-09-07 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 1–138（138 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；0.5M tartrate, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.10 Å R-free 0.269

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPE_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–138； UniProt 1–138

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 1bsn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bsn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bsn
Deposition date deposition_date1998-08-28
Structure title titleSOLUTION STRUCTURE OF THE EPSILON SUBUNIT OF THE F1-ATPSYNTHASE FROM ESCHERICHIA COLI AND ORIENTATION OF THE SUBUNIT RELATIVE TO THE BETA SUBUNITS OF THE COMPLEX
Keywords keywordsATPSYNTHASE, F1-ATPASE, EPSILON SUBUNIT, NMR SPECTROSCOPY, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.51 Å
Radius of gyration Rg (electron density) rg_electron16.30 Å
Forward intensity I(0) i04522170.00
Molecular weight molecular_weight14931.0 kDa
Excluded volume excluded_volume18679 ų
Envelope volume envelope_volume23397 ų
Hydration-shell volume shell_volume12799 ų
Envelope diameter envelope_diameter59.6 Å
Shell Rg shell_rg21.20 Å
Envelope Rg envelope_rg16.72 Å
Shape Rg shape_rg16.31 Å
Total Rg total_rg17.27 Å
Total atoms total_atoms2106
Residues n_residues138
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax58.0 Å
Rg (real space) rg_real17.52 Å
Rg uncertainty (real space) rg_real_error0.46 Å
I(0) (real space) i0_real4.5220e+06
I(0) uncertainty (real space) i0_real_error6.1570e+04
Rg (reciprocal space) rg_reciprocal17.52 Å
I(0) (reciprocal space) i0_reciprocal4522000.0000
Solution quality estimate total_estimate0.8019
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.9 Å
Skewness Skewness skewness0.386
Kurtosis Kurtosis kurtosis-0.220
Angular range angular_range— – 0.4550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha896000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bsna1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.10 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Family Family familya.2.10.1 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Domain ID domain_idd1bsna2
Class classb — All beta proteins
Fold Fold foldb.93 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Superfamily Superfamily superfamilyb.93.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Family Family familyb.93.1.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id1bsnA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal
Domain ID domain_id1bsnA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
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8. Citations (2)

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9. Files and Curves (10)