+Open data
-Basic information
Entry | Database: PDB / ID: 2l24 | ||||||
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Title | Antimicrobial peptide | ||||||
Components | Hemagglutinin | ||||||
Keywords | ANTIMICROBIAL PROTEIN / antimicrobial peptide / design / hemagglutinin | ||||||
Function / homology | Function and homology information clathrin-dependent endocytosis of virus by host cell / membrane => GO:0016020 / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane Similarity search - Function | ||||||
Biological species | Influenza A virus | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | fewest violations, model 1 | ||||||
Authors | Zhu, S. / Aumelas, A. / Gao, B. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2011 Title: Convergent evolution-guided design of antimicrobial peptides derived from influenza A virus hemagglutinin. Authors: Zhu, S. / Aumelas, A. / Gao, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l24.cif.gz | 40.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l24.ent.gz | 29.2 KB | Display | PDB format |
PDBx/mmJSON format | 2l24.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l2/2l24 ftp://data.pdbj.org/pub/pdb/validation_reports/l2/2l24 | HTTPS FTP |
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-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: 1448.753 Da / Num. of mol.: 1 / Fragment: UNP residues 331-343 / Source method: obtained synthetically / Details: The peptide was chemically synthesized. / Source: (synth.) Influenza A virus / References: UniProt: Q6PP25 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.5-2.0 mM HA-FD-13aG12I-1, 60% trifluoroethanol/40% water Solvent system: 60% trifluoroethanol/40% water |
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Sample | Units: mM / Component: HA-FD-13aG12I-1 / Conc. range: 1.5-2.0 |
Sample conditions | Pressure: ambient / Temperature: 295 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||||||||||||||||||||
NMR constraints | Protein phi angle constraints total count: 8 | |||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | |||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10 / Maximum lower distance constraint violation: 14 Å / Maximum upper distance constraint violation: 83 Å / Representative conformer: 1 |