1d1h

SOLUTION STRUCTURE OF HANATOXIN 1

Method: SOLUTION NMR Dmax: 36.1 Å Quality: REASONABLE

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

HANATOXIN TYPE 1

OrganismNot specified

UniProt P56852

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 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 3.4;300 K;Ionic strength (raw mmCIF value) 0;Pressure 1 NMR sample composition:2MM HANATOXIN1 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 TXHN1_GRASP
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

SAXS profile for 1d1h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d1h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d1h
Deposition date deposition_date1999-09-16
Structure title titleSOLUTION STRUCTURE OF HANATOXIN 1
Keywords keywordsCYSTINE KNOT, TOXIN; TOXIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier8.66
Radius of gyration Rg (electron density) rg_electron9.28
Forward intensity I(0) i0118517000.00
Molecular weight molecular_weight86578.0 kDa
Excluded volume excluded_volume106070 ų
Envelope volume envelope_volume13807 ų
Hydration-shell volume shell_volume9691 ų
Envelope diameter envelope_diameter39.7
Shell Rg shell_rg17.81
Envelope Rg envelope_rg12.81
Shape Rg shape_rg9.32
Total Rg total_rg9.50
Total atoms total_atoms11487
Residues n_residues735
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax36.1
Rg (real space) rg_real8.73
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.1850e+08
I(0) uncertainty (real space) i0_real_error1.3480e+06
Rg (reciprocal space) rg_reciprocal8.73
I(0) (reciprocal space) i0_reciprocal118500000.0000
Solution quality estimate total_estimate0.7150
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary10.1
Skewness Skewness skewness0.658
Kurtosis Kurtosis kurtosis0.474
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36810.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.312; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.383; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1d1ha_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.6 — omega toxin-like
Family Family familyg.3.6.2 — Spider toxins

8. Citations (2)

9. Files and Curves (10)