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Yorodumi- PDB-1v28: Solution structure of paralytic peptide of the wild Silkmoth, Ant... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v28 | ||||||
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Title | Solution structure of paralytic peptide of the wild Silkmoth, Antheraea yamamai | ||||||
Components | Paralytic Peptide | ||||||
Keywords | TOXIN / Paralytic peptide / antheraea yamamai / single beta sheet / ENF family | ||||||
Function / homology | Paralytic/GBP/PSP peptide / Paralytic/GBP/PSP peptide / cytokine activity / extracellular space / Paralytic peptide 2 Function and homology information | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing | ||||||
Authors | Kawaguchi, K. / Ying, A. / Suzuki, K. / Kumaki, Y. / Demura, M. / Nitta, K. | ||||||
Citation | Journal: To be Published Title: Structural characterization of paralytic peptide of the wild Silkmoth Antheraea yamamai by NMR Authors: Kawaguchi, K. / Ying, A. / Suzuki, K. / Kumaki, Y. / Demura, M. / Nitta, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1v28.cif.gz | 143 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v28.ent.gz | 99.3 KB | Display | PDB format |
PDBx/mmJSON format | 1v28.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1v28_validation.pdf.gz | 340 KB | Display | wwPDB validaton report |
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Full document | 1v28_full_validation.pdf.gz | 494.5 KB | Display | |
Data in XML | 1v28_validation.xml.gz | 15.3 KB | Display | |
Data in CIF | 1v28_validation.cif.gz | 23.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v2/1v28 ftp://data.pdbj.org/pub/pdb/validation_reports/v2/1v28 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2440.757 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic construct / References: UniProt: P30254*PLUS |
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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: 4.4 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: X-PLOR / Version: 3.851 / Developer: Michael Nilges, John Kuszewski, Axel T. Brunger / Classification: refinement |
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Refinement | Method: distance geometry, simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 189 restraints, 165 are NOE-derived distance constraints, 12 dihedral angle restraints, 12 distance restraints from hydrogen bonds. |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 25 |