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- PDB-1c49: STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE SCOR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c49 | ||||||
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Title | STRUCTURAL AND FUNCTIONAL DIFFERENCES OF TWO TOXINS FROM THE SCORPION PANDINUS IMPERATOR | ||||||
![]() | TOXIN K-BETA | ||||||
![]() | TOXIN / SCORPION TOXIN / POTASSIUM CHANNELS BLOCKERS / ALPHA-K TOXIN FAMILY / NEUROTOXIN / NMR SOLUTION STRUCTURE | ||||||
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 7.2![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING | ||||||
![]() | Klenk, K.C. / Tenenholz, T.C. / Matteson, D.R. / Rogowski, R.S. / Blaustein, M.P. / Weber, D.J. | ||||||
![]() | ![]() Title: Structural and functional differences of two toxins from the scorpion Pandinus imperator. Authors: Klenk, K.C. / Tenenholz, T.C. / Matteson, D.R. / Rogowski, R.S. / 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 | ![]() | 196.4 KB | Display | ![]() |
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PDB format | ![]() | 162.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 341.8 KB | Display | ![]() |
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Full document | ![]() | 463.7 KB | Display | |
Data in XML | ![]() | 14.4 KB | Display | |
Data in CIF | ![]() | 22.2 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: 4080.824 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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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TWO-DIMENSIONAL NMR ON AN UNLABELED SAMPLE OF RECOMBINANT PITX-KB (M). |
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Sample preparation
Details | Contents: 10% D2O AND 100%D2O |
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Sample conditions | Ionic strength: 1.44 mM / pH: 3.50 / Pressure: 1 atm / Temperature: 310.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY SIMULATED ANNEALING / Software ordinal: 1 Details: 425 NOE DISTANCE CONSTRAINTS, 22 H-BOND CONSTRAINTS, 11 CHI ANGLE CONSTRAINTS, 26 PHI ANGLE CONSTRAINTS | ||||||||||||
NMR ensemble | Conformers calculated total number: 500 / Conformers submitted total number: 18 |