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Yorodumi- PDB-1t9e: NMR solution structure of a disulfide analogue of the cyclic sunf... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1t9e | ||||||
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Title | NMR solution structure of a disulfide analogue of the cyclic sunflower trypsin inhibitor SFTI-1 | ||||||
Components | Trypsin inhibitor 1 | ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / sunflower trypsin inhibitor / Disulfide mutant / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | negative regulation of endopeptidase activity / endopeptidase inhibitor activity / serine-type endopeptidase inhibitor activity / protease binding / Trypsin inhibitor 1 Function and homology information | ||||||
Biological species | Helianthus annuus (common sunflower) | ||||||
Method | SOLUTION NMR / Structures were calculated using torsion angle dynamics, refined using cartesian dynamics, energy minimization in solvent using CNS. | ||||||
Authors | Korsinczky, M.L.J. / Clark, R.J. / Craik, D.J. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1 Authors: Korsinczky, M.L.J. / Clark, R.J. / Craik, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t9e.cif.gz | 76.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t9e.ent.gz | 57.1 KB | Display | PDB format |
PDBx/mmJSON format | 1t9e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1t9e_validation.pdf.gz | 344.2 KB | Display | wwPDB validaton report |
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Full document | 1t9e_full_validation.pdf.gz | 375.2 KB | Display | |
Data in XML | 1t9e_validation.xml.gz | 6.6 KB | Display | |
Data in CIF | 1t9e_validation.cif.gz | 9.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t9/1t9e ftp://data.pdbj.org/pub/pdb/validation_reports/t9/1t9e | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1499.753 Da / Num. of mol.: 1 / Mutation: C3(ABA), C11(ABA) / Source method: obtained synthetically Details: The peptide was synthesized using standard solid phase peptide synthesis methods using BOC chemistry. The peptide backbone was cyclicized in solution by addition of HBTU and DIEA which ...Details: The peptide was synthesized using standard solid phase peptide synthesis methods using BOC chemistry. The peptide backbone was cyclicized in solution by addition of HBTU and DIEA which resulted in the formation of a peptide bond between D14 and G1. The sequence of the peptide is naturally found in Helianthus Annus (sunflower) Source: (synth.) Helianthus annuus (common sunflower) / References: UniProt: Q4GWU5 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-Sample preparation
Details |
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Sample conditions | pH: 4.5 / Pressure: ambient / Temperature: 290 K |
-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 DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 MHz |
-Processing
NMR software |
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Refinement | Method: Structures were calculated using torsion angle dynamics, refined using cartesian dynamics, energy minimization in solvent using CNS. 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: 20 |