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Yorodumi- PDB-7voz: Solution structure of cecropin P1(1-29) in dodecylphosphocholine ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7voz | ||||||
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Title | Solution structure of cecropin P1(1-29) in dodecylphosphocholine micelles | ||||||
Components | Cecropin-P1 | ||||||
Keywords | ANTIMICROBIAL PROTEIN / cecropin P1 / calmodulin-fusion / antimicrobial peptides | ||||||
Function / homology | antimicrobial peptide secretion / Cecropin family signature. / Cecropin / Cecropin family / antibacterial humoral response / defense response to bacterium / extracellular region / Cecropin-P1 Function and homology information | ||||||
Biological species | Ascaris suum (pig roundworm) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Gu, H. / Kumeta, H. / Aizawa, T. | ||||||
Funding support | 1items
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Citation | Journal: Acs Omega / Year: 2022 Title: Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues Authors: Gu, H. / Kato, T. / Kumeta, H. / Kumaki, Y. / Tsukamoto, T. / Kikukawa, T. / Demura, M. / Ishida, H. / Vogel, H.J. / Aizawa, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7voz.cif.gz | 203.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7voz.ent.gz | 173.5 KB | Display | PDB format |
PDBx/mmJSON format | 7voz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7voz_validation.pdf.gz | 392.6 KB | Display | wwPDB validaton report |
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Full document | 7voz_full_validation.pdf.gz | 515.6 KB | Display | |
Data in XML | 7voz_validation.xml.gz | 13.4 KB | Display | |
Data in CIF | 7voz_validation.cif.gz | 20.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vo/7voz ftp://data.pdbj.org/pub/pdb/validation_reports/vo/7voz | HTTPS FTP |
-Related structure data
Related structure data | 7dehC C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
Other databases |
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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: 3091.605 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Ascaris suum (pig roundworm) / Gene: ASCEC-1 / Production host: Escherichia coli (E. coli) / References: UniProt: P14661 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 1 mM [U-13C; U-15N] Cecropin P1 (1-29), 40 mM [U-2H] DPC, 90% H2O/10% D2O Label: 15N13C_sample / Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 42 mM / Label: conditions_1 / pH: 5.0 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Agilent Direct Drive / Manufacturer: Agilent / Model: Direct Drive / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |