+Open data
-Basic information
Entry | Database: PDB / ID: 2mhw | ||||||
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Title | The solution NMR structure of maximin-4 in SDS micelles | ||||||
Components | Antimicrobial peptide | ||||||
Keywords | ANTIMICROBIAL PROTEIN / MEMBRANE PROTEIN / membrane peptides / lipid bilayers / bacterial resistance / antimicrobial peptides | ||||||
Function / homology | Bombinin / Bombinin / hemolysis in another organism / defense response to fungus / defense response to bacterium / extracellular region / Antimicrobial peptide / Maximins 4/H3 type 3 Function and homology information | ||||||
Biological species | Bombina maxima (large-webbed bell toad) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Toke, O. / Banoczi, Z. / Kiraly, P. / Heinzmann, R. / Burck, J. / Ulrich, A.S. / Hudecz, F. | ||||||
Citation | Journal: Eur.Biophys.J. / Year: 2011 Title: A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments. Authors: Toke, O. / Banoczi, Z. / Kiraly, P. / Heinzmann, R. / Burck, J. / Ulrich, A.S. / Hudecz, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mhw.cif.gz | 88.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mhw.ent.gz | 52.2 KB | Display | PDB format |
PDBx/mmJSON format | 2mhw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mhw_validation.pdf.gz | 377 KB | Display | wwPDB validaton report |
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Full document | 2mhw_full_validation.pdf.gz | 435.7 KB | Display | |
Data in XML | 2mhw_validation.xml.gz | 9.5 KB | Display | |
Data in CIF | 2mhw_validation.cif.gz | 13.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/2mhw ftp://data.pdbj.org/pub/pdb/validation_reports/mh/2mhw | 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: 2617.137 Da / Num. of mol.: 1 / Fragment: UNP residues 44-70 / Source method: obtained synthetically / Source: (synth.) Bombina maxima (large-webbed bell toad) / References: UniProt: C3RSY7, UniProt: Q58T52*PLUS |
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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: 1-1.2 mM maximin, 10 mM sodium-phosphate, 200 mM [U-100% 2H] d25-sodium-dodecyl-sulfate, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 220 / pH: 5.0 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer | Type: Varian Varian NMR System / Manufacturer: Varian / Model: Varian NMR System / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | |||||||||||||||||||||
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: 10 |