SAXSdb — 1cw5

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

TYPE IIA BACTERIOCIN CARNOBACTERIOCIN B2

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 19–66	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 2.8；298 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT NMR sample composition：5.0 MG CARNOBACTERIOCIN B2 IS DISOLVED IN 700 UL OF TFE-D3/H2O, 90%:10% V/V, PH 2.8.	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 1CW5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1RY3 NMR Solution Structure of the Precursor for Carnobacteriocin B2, an Antimicrobial Peptide from Carnobacterium piscicola Deposited 2003-12-19	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–64（64 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 2；308 K；Pressure ambient NMR sample composition 1 mM precarnobacteriocin B2 U-15N \| 70% TFE-d3, 30% H2O NMR sample composition 1 mM precarnobacteriocin B2 U-15N,U-13C \| 70% TFE-d3, 30% D2O	Resolution not provided

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

View Construct and Data Evidence

UniProt name	CBB2_CARPI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–48； UniProt 19–66

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	1cw5
Deposition date deposition_date	1999-08-25
Structure title title	SOLUTION STRUCTURE OF CARNOBACTERIOCIN B2
Keywords keywords	ANTIMICROBIAL PEPTIDE, HELIX, BACTERIOCIN, TOXIN; TOXIN
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	18.28 Å
Radius of gyration Rg (electron density) rg_electron	17.87 Å
Forward intensity I(0) i0	171152000.00
Molecular weight molecular_weight	99471.0 kDa
Excluded volume excluded_volume	121210 Å³
Envelope volume envelope_volume	54596 Å³
Hydration-shell volume shell_volume	20518 Å³
Envelope diameter envelope_diameter	78.3 Å
Shell Rg shell_rg	29.06 Å
Envelope Rg envelope_rg	22.78 Å
Shape Rg shape_rg	17.79 Å
Total Rg total_rg	18.70 Å
Total atoms total_atoms	13620
Residues n_residues	960
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	71.0 Å
Rg (real space) rg_real	18.51 Å
Rg uncertainty (real space) rg_real_error	0.85 Å
I(0) (real space) i0_real	1.7120e+08
I(0) uncertainty (real space) i0_real_error	2.3090e+06
Rg (reciprocal space) rg_reciprocal	18.48 Å
I(0) (reciprocal space) i0_reciprocal	171100000.0000
Solution quality estimate total_estimate	0.7007
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	18.2 Å
Skewness Skewness skewness	0.478
Kurtosis Kurtosis kurtosis	-0.269
Angular range angular_range	— – 0.4350 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	55550.0000
Real-space data points n_real_points	75
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: 0.339; 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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1cw5a_
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

CATH v4.4 (1 domains)

Domain ID domain_id	1cw5A00
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	130 —

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8. Citations (1)

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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	TYPE IIA BACTERIOCIN CARNOBACTERIOCIN B2
Molecular weight formula_weight	4974.5 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	13620

fit	/app/data/saxs_computation/cw/1cw5/1cw5.fit
pddf	/app/data/pr_computation/cw/1cw5/1cw5.pr.out
profile	/app/data/saxs_computation/cw/1cw5/1cw5.dat

SOLUTION STRUCTURE OF CARNOBACTERIOCIN B2

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

TYPE IIA BACTERIOCIN CARNOBACTERIOCIN B2

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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)