[English] 日本語
Yorodumi- PDB-2mix: Structure of a novel venom peptide toxin from sample limited tere... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2mix | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of a novel venom peptide toxin from sample limited terebrid marine snail | ||||||
Components | venom peptide toxin | ||||||
Keywords | TOXIN / teretoxin / peptide toxin | ||||||
Function / homology | host cell postsynaptic membrane / acetylcholine receptor inhibitor activity / toxin activity / extracellular region / Venom peptide Tv1 Function and homology information | ||||||
Biological species | Terebridae (auger shells) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Bhuiyan, M.H. / Anand, P. / Grigoryan, A. / Holford, M. / Poget, S.F. | ||||||
Citation | Journal: Plos One / Year: 2014 Title: Sample limited characterization of a novel disulfide-rich venom peptide toxin from terebrid marine snail Terebra variegata. Authors: Anand, P. / Grigoryan, A. / Bhuiyan, M.H. / Ueberheide, B. / Russell, V. / Quinonez, J. / Moy, P. / Chait, B.T. / Poget, S.F. / Holford, M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2mix.cif.gz | 55.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2mix.ent.gz | 38.9 KB | Display | PDB format |
PDBx/mmJSON format | 2mix.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mix_validation.pdf.gz | 499.1 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2mix_full_validation.pdf.gz | 609.2 KB | Display | |
Data in XML | 2mix_validation.xml.gz | 18.2 KB | Display | |
Data in CIF | 2mix_validation.cif.gz | 17.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mi/2mix ftp://data.pdbj.org/pub/pdb/validation_reports/mi/2mix | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein/peptide | Mass: 2318.678 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Terebridae (auger shells) / References: UniProt: A0A0B4J184*PLUS |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample |
| |||||||||
Sample conditions | Ionic strength: 1 / pH: 6 / Pressure: ambient / Temperature: 278 K |
-NMR measurement
NMR spectrometer | Type: Agilent Uniform NMR System / Manufacturer: Agilent / Model: Uniform NMR System / Field strength: 600 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |