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- PDB-1wpd: Evidence for domain-specific recognition of SK and Kv channels by... -

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Basic information

Entry
Database: PDB / ID: 1wpd
TitleEvidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins
ComponentsPotassium channel toxin alpha-KTx 6.2,Potassium channel toxin alpha-KTx 6.3
KeywordsTOXIN / Neurotoxin / chimera
Function / homology
Function and homology information


ion channel inhibitor activity / potassium channel regulator activity / toxin activity / extracellular region
Similarity search - Function
Scorpion short toxins signature. / Scorpion short chain toxin, potassium channel inhibitor / Scorpion short toxin, BmKK2 / Knottin, scorpion toxin-like superfamily
Similarity search - Domain/homology
Potassium channel toxin alpha-KTx 6.3 / Potassium channel toxin alpha-KTx 6.2
Similarity search - Component
Biological speciesScorpio palmatus (scorpion)
Heterometrus spinifer (Asian forest scorpion)
MethodSOLUTION NMR / distance geometry, molecular dynamics
AuthorsRegaya, I. / Beeton, C. / Ferrat, G. / Andreotti, N. / Chandy, G.K. / Darbon, H. / De Waard, M. / Sabatier, J.M.
CitationJournal: J.Biol.Chem. / Year: 2004
Title: Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins
Authors: Regaya, I. / Beeton, C. / Ferrat, G. / Andreotti, N. / Darbon, H. / De Waard, M. / Sabatier, J.M.
History
DepositionSep 1, 2004Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 19, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 18, 2019Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: diffrn_radiation_wavelength / entity ...diffrn_radiation_wavelength / entity / entity_name_com / entity_src_gen / entity_src_nat / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref / struct_ref_seq
Item: _diffrn_radiation_wavelength.wavelength / _entity.pdbx_description ..._diffrn_radiation_wavelength.wavelength / _entity.pdbx_description / _entity.src_method / _pdbx_nmr_software.name / _struct_ref.db_code / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.db_align_end / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.seq_align_beg / _struct_ref_seq.seq_align_end

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Potassium channel toxin alpha-KTx 6.2,Potassium channel toxin alpha-KTx 6.3


Theoretical massNumber of molelcules
Total (without water)3,8021
Polymers3,8021
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20structures with the least restraint violations
Representative

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Components

#1: Protein/peptide Potassium channel toxin alpha-KTx 6.2,Potassium channel toxin alpha-KTx 6.3 / Maurotoxin / MTX / Neurotoxin HsTX1


Mass: 3801.560 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Scorpio palmatus (scorpion), (gene. exp.) Heterometrus spinifer (Asian forest scorpion)
Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P80719, UniProt: P59867

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
1212D TOCSY
1312D NOESY

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz

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Processing

NMR software
NameVersionClassification
XwinNMR2processing
XEASY1.3.13data analysis
DIANA2.8structure solution
CNS1.1refinement
RefinementMethod: distance geometry, molecular dynamics / Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 20 / Conformers submitted total number: 20

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