SAXSdb — 3leu

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

LEUCOCIN A

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 25–61	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 2.8；308 K	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 3LEU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CW6 REFINED SOLUTION STRUCTURE OF LEUCOCIN A Deposited 1999-08-25	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 25–61（37 aa） Fragment：LEUCOCIN A-UAL 187	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 2.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT NMR sample composition 2MM LEUCOCIN A IN 90% TFE-D3,10% H2O	Resolution not provided
2LEU HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN 90% AQUEOUS TRIFLUOROETHANOL (TFE) (0.1% TFA), 18 STRUCTURES Deposited 1997-05-20	Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 25–61（37 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 2.8；299 K	Resolution not provided
2LJQ (C9S, C14S)-leucocin A Deposited 2011-09-22	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 25–61（37 aa）	Mutation：C9S, C14S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] peptide, 100 uM DSS, trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2LJT C9L,C14L-LeuA Deposited 2011-09-23	Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 25–61（37 aa）	Mutation：C9L, C14L	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 90 % [U-2H] TFE, 10 % H2O, 0.1 % TFA, 2.6 mM DSS, trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided

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

View Construct and Data Evidence

UniProt name	LCCA_LEUGE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–37； UniProt 25–61

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	3leu
Deposition date deposition_date	1997-05-20
Structure title title	HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN DODECYLPHOSPHOCHOLINE MICELLES, 19 STRUCTURES (1:40 RATIO OF LEUCOCIN A:DPC) (0.1% TFA)
Keywords keywords	ANTIBACTERIAL PEPTIDE, BACTERIOCIN; ANTIBACTERIAL PEPTIDE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	15.13 Å
Radius of gyration Rg (electron density) rg_electron	14.79 Å
Forward intensity I(0) i0	97325600.00
Molecular weight molecular_weight	74753.0 kDa
Excluded volume excluded_volume	90782 Å³
Envelope volume envelope_volume	40921 Å³
Hydration-shell volume shell_volume	18303 Å³
Envelope diameter envelope_diameter	65.2 Å
Shell Rg shell_rg	25.11 Å
Envelope Rg envelope_rg	19.47 Å
Shape Rg shape_rg	14.83 Å
Total Rg total_rg	15.35 Å
Total atoms total_atoms	10070
Residues n_residues	703
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	60.3 Å
Rg (real space) rg_real	15.27 Å
Rg uncertainty (real space) rg_real_error	0.72 Å
I(0) (real space) i0_real	9.7330e+07
I(0) uncertainty (real space) i0_real_error	1.3660e+06
Rg (reciprocal space) rg_reciprocal	15.26 Å
I(0) (reciprocal space) i0_reciprocal	97330000.0000
Solution quality estimate total_estimate	0.6982
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	15.3 Å
Skewness Skewness skewness	0.459
Kurtosis Kurtosis kurtosis	-0.177
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	111800.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.589; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.307; 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) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3leua_
Class class	j — Peptides
Fold Fold fold	j.106 — Leucocin-like bacteriocin
Superfamily Superfamily superfamily	j.106.1 — Leucocin-like bacteriocin
Family Family family	j.106.1.1 — Leucocin-like bacteriocin

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8. Citations (5)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	LEUCOCIN A
Molecular weight formula_weight	3937.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	10070

fit	/app/data/saxs_computation/le/3leu/3leu.fit
pddf	/app/data/pr_computation/le/3leu/3leu.pr.out
profile	/app/data/saxs_computation/le/3leu/3leu.dat

HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN DODECYLPHOSPHOCHOLINE MICELLES, 19 STRUCTURES (1:40 RATIO OF LEUCOCIN A:DPC) (0.1% TFA)

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

LEUCOCIN A

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (5)

9. Files and Curves (10)

Files (7)

Curves (3)