1cz6

SOLUTION STRUCTURE OF ANDROCTONIN

Method: SOLUTION NMR D_max: 81.0 Å Quality: REASONABLE

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

PROTEIN (ANDROCTONIN)

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 1–25	Not recorded	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4；285 K；Pressure AMBIENT NMR sample composition：3.25 MM	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	ANDT_ANDAU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–25； UniProt 1–25

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	1cz6
Deposition date deposition_date	1999-09-01
Structure title title	SOLUTION STRUCTURE OF ANDROCTONIN
Keywords keywords	BETA SHEET, 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	20.56 Å
Radius of gyration Rg (electron density) rg_electron	19.50 Å
Forward intensity I(0) i0	73883100.00
Molecular weight molecular_weight	61775.0 kDa
Excluded volume excluded_volume	75284 Å³
Envelope volume envelope_volume	64946 Å³
Hydration-shell volume shell_volume	24265 Å³
Envelope diameter envelope_diameter	79.7 Å
Shell Rg shell_rg	29.16 Å
Envelope Rg envelope_rg	22.98 Å
Shape Rg shape_rg	19.47 Å
Total Rg total_rg	20.51 Å
Total atoms total_atoms	8640
Residues n_residues	500
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	81.0 Å
Rg (real space) rg_real	20.61 Å
Rg uncertainty (real space) rg_real_error	0.76 Å
I(0) (real space) i0_real	7.3880e+07
I(0) uncertainty (real space) i0_real_error	1.1600e+06
Rg (reciprocal space) rg_reciprocal	20.60 Å
I(0) (reciprocal space) i0_reciprocal	73880000.0000
Solution quality estimate total_estimate	0.7203
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	23.5 Å
Skewness Skewness skewness	0.437
Kurtosis Kurtosis kurtosis	-0.090
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	2748000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.562; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.673; 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	d1cz6a_
Class class	j — Peptides
Fold Fold fold	j.3 — Antimicrobial beta-hairpin
Superfamily Superfamily superfamily	j.3.1 — Antimicrobial beta-hairpin
Family Family family	j.3.1.3 — Androctonin

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8. Citations (2)

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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	PROTEIN (ANDROCTONIN)
Molecular weight formula_weight	3088.7 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	8640

fit	/app/data/saxs_computation/cz/1cz6/1cz6.fit
pddf	/app/data/pr_computation/cz/1cz6/1cz6.pr.out
profile	/app/data/saxs_computation/cz/1cz6/1cz6.dat

SOLUTION STRUCTURE OF ANDROCTONIN

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

PROTEIN (ANDROCTONIN)

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 (2)

9. Files and Curves (10)

Files (7)

Curves (3)