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- PDB-1p0g: Structure of Antimicrobial Peptide, HP (2-20) and its Analogues D... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1p0g | ||||||
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Title | Structure of Antimicrobial Peptide, HP (2-20) and its Analogues Derived from Helicobacter pylori, as Determined by 1H NMR Spectroscopy | ||||||
![]() | 19-mer peptide from 50S ribosomal protein L1 | ||||||
![]() | RIBOSOME / coil-helix-coil | ||||||
Function / homology | ![]() regulation of translation / cytosolic large ribosomal subunit / tRNA binding / rRNA binding / structural constituent of ribosome / defense response to bacterium / translation Similarity search - Function | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING | ||||||
![]() | Lee, K.H. / Lee, D.G. / Park, Y.K. / Harm, K.S. / Kim, Y.M. | ||||||
![]() | ![]() Title: Interactions between antimicrobial peptide, HP(2-20) derived from helicobacter pylori, and membrain studied by nmr spectroscopy Authors: Lee, K.H. / Lee, D.G. / Park, Y.K. / Harm, K.S. / Kim, Y.M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 124.9 KB | Display | ![]() |
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PDB format | ![]() | 98.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 338.7 KB | Display | ![]() |
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Full document | ![]() | 433.2 KB | Display | |
Data in XML | ![]() | 6.9 KB | Display | |
Data in CIF | ![]() | 10.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1p0jC ![]() 1p0lC ![]() 1p0oC ![]() 1p5kC ![]() 1p5lC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 2325.836 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of peptide is naturally found in Helicobacter pylori References: UniProt: Q9ZK21, UniProt: P56029*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR TECHNIQUES |
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Sample preparation
Details | Contents: 1.5MM PEPTIDE; 150MM SDS-D25 / Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6 / Pressure: 1 atm / Temperature: 318 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 400 MHz |
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Processing
NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |