+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ie6 | ||||||
---|---|---|---|---|---|---|---|
Title | SOLUTION STRUCTURE OF IMPERATOXIN A | ||||||
![]() | IMPERATOXIN A | ||||||
![]() | TOXIN / Triple stranded antiparellel beta-sheet / inhibitory cystine knot | ||||||
Function / homology | Scorpion calcine / Scorpion calcine family / Scorpion calcine family signature. / calcium channel inhibitor activity / toxin activity / extracellular region / Imperacalcin![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
![]() | Lee, C.W. / Takeuchi, K. / Takahashi, H. / Sato, K. / Shimada, I. / Kim, D.H. / Kim, J.I. | ||||||
![]() | ![]() Title: Molecular basis of the high-affinity activation of type 1 ryanodine receptors by imperatoxin A. Authors: Lee, C.W. / Lee, E.H. / Takeuchi, K. / Takahashi, H. / Shimada, I. / Sato, K. / Shin, S.Y. / Kim, D.H. / Kim, J.I. | ||||||
History |
| ||||||
Remark 999 | 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). |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 203.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 176 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 485.6 KB | Display | |
Data in XML | ![]() | 21 KB | Display | |
Data in CIF | ![]() | 32 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | 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 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||
NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-
Sample preparation
Details | Contents: 5mM Imperatoxin A; 90% H2O, 10% D2O / Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 0 / pH: 3.4 / Pressure: ambient / Temperature: 300 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | 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 |
-
Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |