+Open data
-Basic information
Entry | Database: PDB / ID: 2n92 | ||||||
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Title | Solution structure of cecropin P1 with LPS | ||||||
Components | Cecropin-P1 | ||||||
Keywords | ANTIMICROBIAL PROTEIN / antimicrobial peptide / lipopolysaccharide | ||||||
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 / torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Baek, M. / Kamiya, M. / Kushibiki, T. / Nakazumi, T. / Tomisawa, S. / Abe, C. / Kumaki, Y. / Kikukawa, T. / Demura, M. / Kawano, K. / Aizawa, T. | ||||||
Citation | Journal: To be Published Title: Lipopolysaccharide bound structure of antimicrobial peptide cecropin P1 by NMR spectroscopy Authors: Baek, M. / Kamiya, M. / Kushibiki, T. / Nakazumi, T. / Tomisawa, S. / Abe, C. / Kumaki, Y. / Kikukawa, T. / Demura, M. / Kawano, K. / Aizawa, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n92.cif.gz | 224.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n92.ent.gz | 189.8 KB | Display | PDB format |
PDBx/mmJSON format | 2n92.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n92_validation.pdf.gz | 402.4 KB | Display | wwPDB validaton report |
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Full document | 2n92_full_validation.pdf.gz | 485.9 KB | Display | |
Data in XML | 2n92_validation.xml.gz | 11 KB | Display | |
Data in CIF | 2n92_validation.cif.gz | 16.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n9/2n92 ftp://data.pdbj.org/pub/pdb/validation_reports/n9/2n92 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3345.914 Da / Num. of mol.: 1 / Fragment: UNP residues 14-44 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 |
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |