SAXSdb — 1fs0

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

ATP SYNTHASE EPSILON SUBUNIT

OrganismNot specified

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 1–138	Not recorded	ATP SYNTHASE GAMMA SUBUNIT × 1 （P0ABA6）	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
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain E； UniProt 1–138	Not recorded	ATP SYNTHASE GAMMA SUBUNIT × 2 （P0ABA6）	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

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 1FS0	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 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	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	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
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 Deposited 1998-08-28	Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	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

3 other PDB entries and 3 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 E； PDBConstruct 1–138； UniProt 1–138

ATP SYNTHASE GAMMA SUBUNIT

OrganismNot specified

UniProt P0ABA6

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 19–248	Not recorded	ATP SYNTHASE EPSILON SUBUNIT × 1 （P0A6E6）	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
2	Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain G； UniProt 19–248	Not recorded	ATP SYNTHASE EPSILON SUBUNIT × 2 （P0A6E6）	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

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	ATPG_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 1–230； UniProt 19–248

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	1fs0
Deposition date deposition_date	2000-09-07
Structure title title	COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI
Keywords keywords	ATP Synthase, Coiled coil, Gamma, epsilon, HYDROLASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	22.95 Å
Radius of gyration Rg (electron density) rg_electron	22.22 Å
Forward intensity I(0) i0	24984000.00
Molecular weight molecular_weight	38398.0 kDa
Excluded volume excluded_volume	48299 Å³
Envelope volume envelope_volume	57997 Å³
Hydration-shell volume shell_volume	22313 Å³
Envelope diameter envelope_diameter	75.0 Å
Shell Rg shell_rg	28.65 Å
Envelope Rg envelope_rg	22.59 Å
Shape Rg shape_rg	22.20 Å
Total Rg total_rg	23.11 Å
Total atoms total_atoms	2691
Residues n_residues	347
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	73.4 Å
Rg (real space) rg_real	22.95 Å
Rg uncertainty (real space) rg_real_error	0.51 Å
I(0) (real space) i0_real	2.4980e+07
I(0) uncertainty (real space) i0_real_error	3.4690e+05
Rg (reciprocal space) rg_reciprocal	22.95 Å
I(0) (reciprocal space) i0_reciprocal	24980000.0000
Solution quality estimate total_estimate	0.8985
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.0 Å
Skewness Skewness skewness	0.356
Kurtosis Kurtosis kurtosis	-0.333
Angular range angular_range	— – 0.3450 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	5108000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.944

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	ATP SYNTHASE EPSILON SUBUNIT
Molecular weight formula_weight	14956.0 kDa
EC 编号 ec_number	3.6.1.34
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E
Atom count atom_count	2945

AMTYHLDVVSAEQQMFSGLVEKIQVTGSEGELGIYPGHAPLLTAIKPGMIRIVKQHGHEEFIYLSGGILEVQPGNVTVLADTAIRGQDLDEARAMEAKRKAEEHISSSHGDVDYAQASAELAKAIAQLRVIELTKKAM

Entity 2 Entity 2 polymer

Description description	ATP SYNTHASE GAMMA SUBUNIT
Molecular weight formula_weight	25683.7 kDa
EC 编号 ec_number	3.6.1.34
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

KITKAMEMVAASKMRKSQDRMAASRPYAETMRKVIGHLAHGNLEYKHPYLEDRDVKRVGYLVVSTDRGLCGGLNINLFKKLLAEMKTWTDKGVQCDLAMIGSKGVSFFNSVGGNVVAQVTGMGDNPSLSELIGPVKVMLQAYDEGRLDKLYIVSNKFINTMSQVPTISQLLPLPASDDDDLKHKSWDYLYEPDPKALLDTLLRRYVESQVYQGVVENLASEQAARMVAMK

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	254

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1fs0e1
Class class	a — All alpha proteins
Fold Fold fold	a.2 — Long alpha-hairpin
Superfamily Superfamily superfamily	a.2.10 — Epsilon subunit of F1F0-ATP synthase C-terminal domain
Family Family family	a.2.10.1 — Epsilon subunit of F1F0-ATP synthase C-terminal domain

Domain ID domain_id	d1fs0e2
Class class	b — All beta proteins
Fold Fold fold	b.93 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Superfamily Superfamily superfamily	b.93.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain
Family Family family	b.93.1.1 — Epsilon subunit of F1F0-ATP synthase N-terminal domain

Domain ID domain_id	d1fs0g_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.49 — Pyruvate kinase C-terminal domain-like
Superfamily Superfamily superfamily	c.49.2 — ATP synthase (F1-ATPase), gamma subunit
Family Family family	c.49.2.1 — ATP synthase (F1-ATPase), gamma subunit

CATH v4.4 (4 domains)

Domain ID domain_id	1fs0E01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	15 — ATP Synthase; domain 1
Homologous superfamily homologous superfamily	10 — F0F1 ATP synthase delta/epsilon subunit, N-terminal

Domain ID domain_id	1fs0E02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	440 — ATP synthase delta/epsilon subunit, C-terminal domain

Domain ID domain_id	1fs0G01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1380 — Pyruvate Kinase; Chain: A, domain 1
Homologous superfamily homologous superfamily	10 — ATP synthase, F1 complex, gamma subunit

Domain ID domain_id	1fs0G02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	80 — ATP synthase, gamma subunit, helix hairpin domain

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8. Citations (1)

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Unit-cell length a length_a	76.720 Å
Unit-cell length b length_b	176.090 Å
Unit-cell length c length_c	67.070 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	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.2270
R_work r_work	0.2160
R_free r_free	0.2690

fit	/app/data/saxs_computation/fs/1fs0/1fs0.fit
pddf	/app/data/pr_computation/fs/1fs0/1fs0.pr.out
profile	/app/data/saxs_computation/fs/1fs0/1fs0.dat

COMPLEX OF GAMMA/EPSILON ATP SYNTHASE FROM E.COLI

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

ATP SYNTHASE EPSILON SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

ATP SYNTHASE GAMMA SUBUNIT

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

CATH v4.4 (4 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)