SAXSdb — 1l2p

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

ATP Synthase B Chain

Escherichia coli

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 62–122	Fragment：Dimerization Domain (residues 62-122)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5；291 K；30% ISOPROPANOL, 45% 2-METHYL-2,4-PENTANEDIOL, pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 18.0K	Resolution 1.55 Å R-free 0.313

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 1L2P	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B9U MEMBRANE DOMAIN OF THE SUBUNIT B OF THE E.COLI ATP SYNTHASE Deposited 1999-02-15	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–34（34 aa） Fragment：MEMBRANE DOMAIN	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 50 mM NACL；Pressure 1 NMR sample composition CHLOROFORM/METHANOL/WATER=4/4/1	Resolution not provided
2KHK NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase Deposited 2009-04-08	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 30–82（53 aa） Fragment：residues in UNP 30-82	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.8；288 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT NMR sample composition 1mM [U-99% 13C; U-99% 15N] subunit b 30-82-1, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ATPF_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–61； UniProt 62–122

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	1l2p
Deposition date deposition_date	2002-02-22
Structure title title	ATP Synthase b Subunit Dimerization Domain
Keywords keywords	alpha helix, 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	25.35 Å
Radius of gyration Rg (electron density) rg_electron	27.00 Å
Forward intensity I(0) i0	1135890.00
Molecular weight molecular_weight	7046.0 kDa
Excluded volume excluded_volume	8698 Å³
Envelope volume envelope_volume	13550 Å³
Hydration-shell volume shell_volume	6062 Å³
Envelope diameter envelope_diameter	95.6 Å
Shell Rg shell_rg	24.75 Å
Envelope Rg envelope_rg	27.86 Å
Shape Rg shape_rg	26.94 Å
Total Rg total_rg	26.77 Å
Total atoms total_atoms	494
Residues n_residues	61
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	100.4 Å
Rg (real space) rg_real	26.19 Å
Rg uncertainty (real space) rg_real_error	1.67 Å
I(0) (real space) i0_real	1.1360e+06
I(0) uncertainty (real space) i0_real_error	2.1040e+04
Rg (reciprocal space) rg_reciprocal	25.93 Å
I(0) (reciprocal space) i0_reciprocal	1136000.0000
Solution quality estimate total_estimate	0.5425
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	11.2 Å
Skewness Skewness skewness	0.692
Kurtosis Kurtosis kurtosis	-0.310
Angular range angular_range	— – 0.3150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	36300.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.015; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.002; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1l2pa_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.21 — F1F0 ATP synthase subunit B, membrane domain
Family Family family	f.23.21.1 — F1F0 ATP synthase subunit B, membrane domain

CATH v4.4 (1 domains)

Domain ID domain_id	1l2pA00
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	620 — F1F0 ATP synthase subunit B, membrane domain

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8. Citations (1)

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Unit-cell length a length_a	35.700 Å
Unit-cell length b length_b	40.760 Å
Unit-cell length c length_c	42.350 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	4

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.550 Å
Low-resolution limit resolution_low	29.370 Å
R factor r_factor	0.2850
R_work r_work	0.2820
R_free r_free	0.3130

Description description	ATP Synthase B Chain
Molecular weight formula_weight	7059.0 kDa
EC 编号 ec_number	3.6.3.34
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	548

ATP Synthase b Subunit Dimerization Domain

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

ATP Synthase B Chain

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	54

fit	/app/data/saxs_computation/l2/1l2p/1l2p.fit
pddf	/app/data/pr_computation/l2/1l2p/1l2p.pr.out
profile	/app/data/saxs_computation/l2/1l2p/1l2p.dat