← Back to search
2ns3

Solution structure of ribbon BuIA

Method: SOLUTION NMR Dmax: 14.8 Å Quality: REASONABLE
▼

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

Alpha-conotoxin BuIA

OrganismNot specified

UniProt P69657

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 44–56 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4；282 K；Pressure ambient NMR sample composition：1mM ribbon BuIA; 90% H2O, 10% D2O | 90% H2O/10% 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.

Other PDB Difference from Current Entry 2NS3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2I28 Solution Structure of alpha-Conotoxin BuIA Deposited 2006-08-16 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 44–56（13 aa） Fragment：Alpha-conotoxin BuIA
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.04；278 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR measurement conditions pH 3.04；288 K；Ionic strength (raw mmCIF value) 0；Pressure 1
NMR sample composition 5mM alpha-conotoxin BuIA; 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
4EZ1 Crystal structure of acetylcholine binding protein (AChBP) from Aplysia Californica in complex with alpha-conotoxin BuIA Deposited 2012-05-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain K 44–56（13 aa） Fragment：UNP residues 44-56
Chain L 44–56（13 aa） Fragment：UNP residues 44-56
Chain M 44–56（13 aa） Fragment：UNP residues 44-56
Chain N 44–56（13 aa） Fragment：UNP residues 44-56
Chain O 44–56（13 aa） Fragment：UNP residues 44-56
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M Tris-HCl, 0.25 M magnesium chloride, 20% w/v PEG4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.49 Å R-free 0.227

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXA1_CONBU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–13； UniProt 44–56

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 2ns3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ns3
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id2ns3
Deposition date deposition_date2006-11-03
Structure title titleSolution structure of ribbon BuIA
Keywords keywordsribbon disulfide connectivity, Toxin; TOXIN
Experimental Method methodSOLUTION NMR
▼

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

Radius of gyration Rg (Guinier) rg_guinier4.86 Å
Radius of gyration Rg (electron density) rg_electron5.94 Å
Forward intensity I(0) i012107400.00
Molecular weight molecular_weight26312.0 kDa
Excluded volume excluded_volume31827 ų
Envelope volume envelope_volume2174 ų
Hydration-shell volume shell_volume3306 ų
Envelope diameter envelope_diameter22.7 Å
Shell Rg shell_rg10.78 Å
Envelope Rg envelope_rg6.93 Å
Shape Rg shape_rg5.95 Å
Total Rg total_rg6.15 Å
Total atoms total_atoms3420
Residues n_residues260
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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 dmax14.8 Å
Rg (real space) rg_real5.03 Å
Rg uncertainty (real space) rg_real_error0.02 Å
I(0) (real space) i0_real1.2270e+07
I(0) uncertainty (real space) i0_real_error7.1840e+04
Rg (reciprocal space) rg_reciprocal4.82 Å
I(0) (reciprocal space) i0_reciprocal12110000.0000
Solution quality estimate total_estimate0.6858
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary— Å
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha2.1910
Highest regularization parameter α highest_alpha229.6000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 0.814; Sysdev: 0.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.508
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▶

8. Citations (1)

▶

9. Files and Curves (10)