+Open data
-Basic information
Entry | Database: PDB / ID: 1ma4 | ||||||
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Title | Solution Structure of Tachyplesin I Mutant TPY4 in water | ||||||
Components | Tachyplesin 1 | ||||||
Keywords | ANTIMICROBIAL PROTEIN / Tachyplesin I / Beta Hairpin / Tyrosine Mutant / TPY4 | ||||||
Function / homology | defense response to bacterium / extracellular region / Tachyplesin-1 Function and homology information | ||||||
Method | SOLUTION NMR / Simulated Annealing with complete cross-validation | ||||||
Model type details | minimized average | ||||||
Authors | Laederach, A. / Andreotti, A.H. / Fulton, D.B. | ||||||
Citation | Journal: Biochemistry / Year: 2002 Title: Solution and micelle-bound structures of Tachyplesin I and its active linear derivatives Authors: Laederach, A. / Andreotti, A.H. / Fulton, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ma4.cif.gz | 197.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ma4.ent.gz | 156.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ma4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ma/1ma4 ftp://data.pdbj.org/pub/pdb/validation_reports/ma/1ma4 | HTTPS FTP |
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-Related 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: 2514.931 Da / Num. of mol.: 1 / Mutation: C3Y C7Y C12Y C16Y / Source method: obtained synthetically Details: The peptide was chemically synthesized using Fmoc solid state synthesis. The sequence of the peptide is naturally found in Tachypleus Tridentatus (Japanese Horeshoe Crab). References: UniProt: P14213 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: For reasons of overlap, data was collected at both 298K and 277K. NOEs from spectra at both temperatures were used. |
-Sample preparation
Details | Contents: TPY4 17 residue peptide Solvent system: 90%/10% H2O/D2O and 99% D2O with 0.15% TFA, pH 3.0 | |||||||||||||||
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
-Processing
NMR software |
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Refinement | Method: Simulated Annealing with complete cross-validation / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 300 / Conformers submitted total number: 31 |