+Open data
-Basic information
Entry | Database: PDB / ID: 1y2p | ||||||
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Title | Solution structure of Hstx3P | ||||||
Components | Neurotoxin HsTX1 | ||||||
Keywords | TOXIN / HSTX3P / POTASSIUM CHANNEL | ||||||
Function / homology | Scorpion short toxins signature. / Scorpion short chain toxin, potassium channel inhibitor / Scorpion short toxin, BmKK2 / Knottin, scorpion toxin-like superfamily / ion channel inhibitor activity / potassium channel regulator activity / toxin activity / extracellular region / Potassium channel toxin alpha-KTx 6.3 Function and homology information | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics | ||||||
Authors | Mosbah, A. / Gariga, L. / Darbon, H. / Sabatier, J.M. | ||||||
Citation | Journal: Proteins / Year: 2005 Title: The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily Authors: Carrega, L. / Mosbah, A. / Ferrat, G. / Beeton, C. / Andreotti, N. / Mansuelle, P. / Darbon, H. / De Waard, M. / Sabatier, J.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1y2p.cif.gz | 219.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1y2p.ent.gz | 192.3 KB | Display | PDB format |
PDBx/mmJSON format | 1y2p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1y2p_validation.pdf.gz | 346 KB | Display | wwPDB validaton report |
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Full document | 1y2p_full_validation.pdf.gz | 460.2 KB | Display | |
Data in XML | 1y2p_validation.xml.gz | 13.5 KB | Display | |
Data in CIF | 1y2p_validation.cif.gz | 21.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y2/1y2p ftp://data.pdbj.org/pub/pdb/validation_reports/y2/1y2p | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3836.585 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. ABU19 ABU34 OF HSTX4P References: UniProt: P59867 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details | Contents: 2Mm hstx3P, 90% H2O, 10% D2O / Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics Software ordinal: 1 | |||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function,structures with the lowest energy,structures with the least restraint violations,structures with favorable non-bond energy,structures with acceptable ...Conformer selection criteria: target function,structures with the lowest energy,structures with the least restraint violations,structures with favorable non-bond energy,structures with acceptable covalent geometry,back calculated data agree with experimental NOESY spectrum Conformers calculated total number: 50 / Conformers submitted total number: 20 |