1bnb

SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS

Method: SOLUTION NMR D_max: 28.5 Å Quality: GOOD

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

BOVINE NEUTROPHIL BETA-DEFENSIN 12

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 2–38	Not recorded	No other associated polymer	SOLUTION NMR mmCIF provides none of the parsed experimental conditions	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.

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

View Construct and Data Evidence

UniProt name	BD12_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–38； UniProt 2–38

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bnb
Deposition date deposition_date	1995-03-08
Structure title title	SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS
Keywords keywords	BETA-DEFENSIN 12; BETA-DEFENSIN 12
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	8.30 Å
Radius of gyration Rg (electron density) rg_electron	9.04 Å
Forward intensity I(0) i0	109960000.00
Molecular weight molecular_weight	82521.0 kDa
Excluded volume excluded_volume	101540 Å³
Envelope volume envelope_volume	10449 Å³
Hydration-shell volume shell_volume	8230 Å³
Envelope diameter envelope_diameter	35.1 Å
Shell Rg shell_rg	16.46 Å
Envelope Rg envelope_rg	11.48 Å
Shape Rg shape_rg	9.10 Å
Total Rg total_rg	9.10 Å
Total atoms total_atoms	11440
Residues n_residues	760
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	28.5 Å
Rg (real space) rg_real	8.27 Å
Rg uncertainty (real space) rg_real_error	0.29 Å
I(0) (real space) i0_real	1.1000e+08
I(0) uncertainty (real space) i0_real_error	1.0590e+06
Rg (reciprocal space) rg_reciprocal	8.27 Å
I(0) (reciprocal space) i0_reciprocal	110000000.0000
Solution quality estimate total_estimate	0.8471
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	9.7 Å
Skewness Skewness skewness	0.198
Kurtosis Kurtosis kurtosis	-0.481
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	13080.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.528

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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	d1bnba_
Class class	g — Small proteins
Fold Fold fold	g.9 — Defensin-like
Superfamily Superfamily superfamily	g.9.1 — Defensin-like
Family Family family	g.9.1.1 — Defensin

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8. Citations (3)

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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	BOVINE NEUTROPHIL BETA-DEFENSIN 12
Molecular weight formula_weight	4126.0 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	11440

fit	/app/data/saxs_computation/bn/1bnb/1bnb.fit
pddf	/app/data/pr_computation/bn/1bnb/1bnb.pr.out
profile	/app/data/saxs_computation/bn/1bnb/1bnb.dat

SOLUTION STRUCTURE OF BOVINE NEUTROPHIL BETA-DEFENSIN 12: THE PEPTIDE FOLD OF THE BETA-DEFENSINS IS IDENTICAL TO THAT OF THE CLASSICAL DEFENSINS

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

BOVINE NEUTROPHIL BETA-DEFENSIN 12

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 (3)

9. Files and Curves (10)

Files (7)

Curves (3)