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- PDB-2pta: PANDINUS TOXIN K-A (PITX-KA) FROM PANDINUS IMPERATOR, NMR, 20 STR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2pta | ||||||
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Title | PANDINUS TOXIN K-A (PITX-KA) FROM PANDINUS IMPERATOR, NMR, 20 STRUCTURES | ||||||
![]() | PANDINUS TOXIN K-ALPHA | ||||||
![]() | NEUROTOXIN / POTASSIUM CHANNEL BLOCKERS / NMR SOLUTION STRUCTURE / ALPHA-K TOXIN FAMILY / SCORPION TOXIN | ||||||
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 / : / toxin activity / extracellular region / Potassium channel toxin alpha-KTx 7.1![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING | ||||||
![]() | Tenenholz, T.C. / Rogowski, R.S. / Collins, J.H. / Blaustein, M.P. / Weber, D.J. | ||||||
![]() | ![]() Title: Solution structure for Pandinus toxin K-alpha (PiTX-K alpha), a selective blocker of A-type potassium channels. Authors: Tenenholz, T.C. / Rogowski, R.S. / Collins, J.H. / Blaustein, M.P. / Weber, D.J. #1: ![]() Title: Three New Toxins from the Scorpion Pandinus Imperator Selectively Block Certain Voltage-Gated K+ Channels Authors: Rogowski, R.S. / Collins, J.H. / O'Neill, T.J. / Gustafson, T.A. / Werkman, T.R. / Rogawski, M.A. / Tenenholz, T.C. / Weber, D.J. / Blaustein, M.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 214.4 KB | Display | ![]() |
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PDB format | ![]() | 186 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 346.8 KB | Display | ![]() |
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Full document | ![]() | 463 KB | Display | |
Data in XML | ![]() | 15.9 KB | Display | |
Data in CIF | ![]() | 24.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 4048.825 Da / Num. of mol.: 1 / Fragment: COMPLETE PEPTIDE Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 3.45 / Temperature: 310 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX 600 / Manufacturer: Bruker / Model: DMX 600 / Field strength: 600.13 MHz |
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Processing
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NMR software |
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Refinement | Method: DISTANCE GEOMETRY SIMULATED ANNEALING / Software ordinal: 1 Details: 295 NOE DISTANCE CONSTRAINTS, 9 H-BONDS, 9 CHI ANGLE CONSTRAINTS. | ||||||||||||
NMR ensemble | Conformer selection criteria: NO DISTANCE VIOLATIONS GREATER THAN 0.30 ANGSTROMS, NO ANGULAR VIOLATIONS > 5 DEG, TOTAL ENERGY < 120 KCAL/MOL Conformers calculated total number: 500 / Conformers submitted total number: 20 |