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Yorodumi- PDB-2muh: High-resolution NMR structure of the protegrin-2 docked to DPC Mi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2muh | ||||||
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Title | High-resolution NMR structure of the protegrin-2 docked to DPC Micelles | ||||||
Components | Protegrin-2 | ||||||
Keywords | ANTIMICROBIAL PROTEIN / Protegrin | ||||||
Function / homology | Function and homology information lipopolysaccharide binding / antimicrobial humoral immune response mediated by antimicrobial peptide / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / innate immune response / extracellular space Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Filippov, A.V. / Efimov, S.V. / Klochkov, V.V. / Antzutkin, O.N. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2015 Title: High-resolution NMR structure of the antimicrobial peptide protegrin-2 in the presence of DPC micelles. Authors: Usachev, K.S. / Efimov, S.V. / Kolosova, O.A. / Filippov, A.V. / Klochkov, V.V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2muh.cif.gz | 97 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2muh.ent.gz | 68.9 KB | Display | PDB format |
PDBx/mmJSON format | 2muh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2muh_validation.pdf.gz | 432.4 KB | Display | wwPDB validaton report |
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Full document | 2muh_full_validation.pdf.gz | 604.2 KB | Display | |
Data in XML | 2muh_validation.xml.gz | 21.3 KB | Display | |
Data in CIF | 2muh_validation.cif.gz | 21.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/2muh ftp://data.pdbj.org/pub/pdb/validation_reports/mu/2muh | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homologyF&H Search |
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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: 1952.426 Da / Num. of mol.: 1 / Fragment: UNP residues 131-146 / Source method: obtained synthetically Details: solid-phase peptide synthesis using amino acids protected by the 9-uorenylmethoxycarbonyl group and with reaction mixture conductivity control. Source: (synth.) Sus scrofa (pig) / References: UniProt: P32195 |
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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: 4 mg/mL PG-2, 20 mg/mL [U-99% 2H] DPC, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 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: structures with the lowest energy Conformers calculated total number: 1000 / Conformers submitted total number: 20 |