SEQUENCE The sequence of this protein was published in a journal (Zamudio, F. Z., et al. 1997, FEBS ...SEQUENCE The sequence of this protein was published in a journal (Zamudio, F. Z., et al. 1997, FEBS Lett. 405, 385-389).
Mass: 3776.495 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. This sequence occurs naturally in the venom of scorpion Pandinus imperator. References: UniProt: P59868
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2D NOESY
1
2
1
DQF-COSY
1
3
1
E-COSY
NMR details
Text: This structure was determined using standard 2D homonuclear techniques.
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz
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Processing
NMR software
Name
Version
Developer
Classification
XwinNMR
3
Bruker
collection
XwinNMR
3
Bruker
processing
X-PLOR
3.851
Brunger
structuresolution
X-PLOR
3.851
Brunger
refinement
Refinement
Method: distance geometry simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 519 restraints, 473 are NOE-derived distance constraints, 25 dihedral angle restraints, 12 distance restraints from hydrogen bonds, and 9 distance ...Details: The structures are based on a total of 519 restraints, 473 are NOE-derived distance constraints, 25 dihedral angle restraints, 12 distance restraints from hydrogen bonds, and 9 distance restraints form disulfide bonds.
NMR representative
Selection criteria: closest to the average
NMR ensemble
Conformer selection criteria: The submitted conformer models are those with the lowest energy and the least restraint violations. Conformers calculated total number: 100 / Conformers submitted total number: 20
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