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- PDB-1hp2: SOLUTION STRUCTURE OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS... -

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Basic information

Entry
Database: PDB / ID: 1hp2
TitleSOLUTION STRUCTURE OF A TOXIN FROM THE SCORPION TITYUS SERRULATUS (TSTX-K ALPHA) DETERMINED BY NMR.
ComponentsTITYUSTOXIN K ALPHA
KeywordsTOXIN / K+ channel / scorpion toxin / alpha-K toxin
Function / homologyScorpion 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 4.1
Function and homology information
Biological speciesTityus serrulatus (Brazilian scorpion)
MethodSOLUTION NMR / distance geometry simulated annealing
AuthorsEllis, K.C. / Tenenholz, T.C. / Gilly, W.F. / Blaustein, M.P. / Weber, D.J.
Citation
Journal: Biochemistry / Year: 2001
Title: Interaction of a toxin from the scorpion Tityus serrulatus with a cloned K+ channel from squid (sqKv1A).
Authors: Ellis, K.C. / Tenenholz, T.C. / Jerng, H. / Hayhurst, M. / Dudlak, C.S. / Gilly, W.F. / Blaustein, M.P. / Weber, D.J.
#1: Journal: MOL.PHARMACOL. / Year: 1991
Title: Polypeptide Toxins from the Venoms of Old World and New World Scorpions Preferentially Block Different Potassium Channels
Authors: Blaustein, M.P. / Rogowski, R.S. / Schneider, M.J. / Krueger, B.K.
History
DepositionDec 12, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 13, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Nov 13, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: TITYUSTOXIN K ALPHA


Theoretical massNumber of molelcules
Total (without water)3,9561
Polymers3,9561
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 100structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #25closest to the average

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Components

#1: Protein/peptide TITYUSTOXIN K ALPHA / TSTX-K ALPHA / TSK4


Mass: 3955.845 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Tityus serrulatus (Brazilian scorpion) / Production host: Escherichia coli (E. coli) / References: UniProt: P46114
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
121DQF-COSY
131TOCSY
141ROESY
152E-COSY
261TOCSY
371TOCSY
481TOCSY
591TOCSY
51012D NOESY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques.

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Sample preparation

Details
Solution-IDContentsSolvent system
14.53 mM TsTx-Ka 2.2 mM d11-Tris 0.1 mM EDTA 0.35 mM NaN390% H2O/10% D2O
24.53 mM TsTx-Ka 2.2 mM d11-Tris 0.1 mM EDTA 0.35 mM NaN3100% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
11.443.51 atm310 K
21.443.51 atm305 K
31.443.51 atm300 K
41.443.51 atm295 K
51.443.51 atm290 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851Brungerrefinement
X-PLOR3.851Brungerstructure solution
XwinNMRcollection
NMRPipe1.7Delagilioprocessing
Felixprocessing
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
Details: These structures are based on a total of 569 NOE distance contraints, 13 dihedral angle restraints, and 16 phi angle restraints.
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 30

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