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- PDB-2it8: Solution structure of a linear analog of the cyclic squash trypsi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2it8 | ||||||
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Title | Solution structure of a linear analog of the cyclic squash trypsin inhibitor MCoTI-II | ||||||
![]() | Trypsin inhibitor 2 | ||||||
![]() | PLANT PROTEIN / PLANT PROTEIN ANALOG / KNOTTIN / CYSTINE-KNOT / 3-10 HELIX / TRIPLE-STRANDED ANTI-PARALLEL BETA-SHEET | ||||||
Function / homology | ![]() negative regulation of serine-type endopeptidase activity / serine-type endopeptidase inhibitor activity / defense response / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing, restrained molecular dynamics | ||||||
![]() | Avrutina, O. / Chiche, L. / Diederichsen, U. / Heitz, A. / Kolmar, H. | ||||||
![]() | ![]() Title: Knottin cyclization: Structure and stability of cyclic and linear squash inhibitors do not differ significantly Authors: Heitz, A. / Avrutina, O. / Le-Nguyen, D. / Diederichsen, U. / Hernandez, J.F. / Gracy, J. / Kolmar, H. / Chiche, L. #1: ![]() Title: Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor MCoTI-II Authors: Avrutina, O. / Schmoldt, H.U. / Gabrijelcic-Geiger, D. / Le-Nguyen, D. / Sommerhoff, C.P. / Diederichsen, U. / Kolmar, H. #2: ![]() Title: Fmoc-assisted synthesis of a 29-residue cystine-knot trypsin inhibitor containing a guanyl amino acid at the P1-position Authors: Avrutina, O. / Schmoldt, H.U. / Kolmar, H. / Diederichsen, U. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: AUTHOR-DETERMINED |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 242.5 KB | Display | ![]() |
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PDB format | ![]() | 211.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 335 KB | Display | ![]() |
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Full document | ![]() | 389.9 KB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 21.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 3077.700 Da / Num. of mol.: 1 / Source method: obtained synthetically Source: (synth.) ![]() References: UniProt: P82409 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing, restrained molecular dynamics Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 30 |