1c49

STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE SCORPION PANDINUS IMPERATOR

Method: SOLUTION NMR D_max: 34.4 Å Quality: GOOD

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

TOXIN K-BETA

Pandinus imperator

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 1–35	Fragment：COMPLETE PEPTIDE	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 3.5；310 K；Ionic strength (raw mmCIF value) 1.44 mM；Pressure 1 NMR sample composition：10% D2O AND 100%D2O	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	SCKB_PANIM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–35； UniProt 1–35

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	1c49
Deposition date deposition_date	1999-08-17
Structure title title	STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE SCORPION PANDINUS IMPERATOR
Keywords keywords	SCORPION TOXIN, POTASSIUM CHANNELS BLOCKERS, ALPHA-K TOXIN FAMILY, NEUROTOXIN, NMR SOLUTION STRUCTURE, 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	8.79 Å
Radius of gyration Rg (electron density) rg_electron	9.07 Å
Forward intensity I(0) i0	94264200.00
Molecular weight molecular_weight	73401.0 kDa
Excluded volume excluded_volume	88891 Å³
Envelope volume envelope_volume	9727 Å³
Hydration-shell volume shell_volume	7907 Å³
Envelope diameter envelope_diameter	37.1 Å
Shell Rg shell_rg	16.21 Å
Envelope Rg envelope_rg	11.31 Å
Shape Rg shape_rg	9.07 Å
Total Rg total_rg	9.30 Å
Total atoms total_atoms	9936
Residues n_residues	630
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	34.4 Å
Rg (real space) rg_real	8.84 Å
Rg uncertainty (real space) rg_real_error	0.52 Å
I(0) (real space) i0_real	9.4260e+07
I(0) uncertainty (real space) i0_real_error	9.3400e+05
Rg (reciprocal space) rg_reciprocal	8.84 Å
I(0) (reciprocal space) i0_reciprocal	94260000.0000
Solution quality estimate total_estimate	0.7676
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	9.6 Å
Skewness Skewness skewness	0.527
Kurtosis Kurtosis kurtosis	0.035
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	21160.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.524; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.502; Smooth: 0.915

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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	d1c49a_
Class class	g — Small proteins
Fold Fold fold	g.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamily	g.3.7 — Scorpion toxin-like
Family Family family	g.3.7.2 — Short-chain scorpion toxins

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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	TOXIN K-BETA
Molecular weight formula_weight	4080.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	9936

来源生物 organism	Pandinus imperator
通用名 common_name	emperor scorpion
NCBI Class编号 ncbi_taxonomy_id	55084
宿主生物 host_organism	Escherichia coli BL21(DE3)

STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE SCORPION PANDINUS IMPERATOR

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

TOXIN K-BETA

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

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/c4/1c49/1c49.fit
pddf	/app/data/pr_computation/c4/1c49/1c49.pr.out
profile	/app/data/saxs_computation/c4/1c49/1c49.dat