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Open data
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Basic information
Entry | Database: PDB / ID: 9oil | ||||||
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Title | Solution Structure of the Broadspectrum Bacteriocin Garvicin Q | ||||||
![]() | Prepeptide GarQ | ||||||
![]() | ANTIBIOTIC / Bacteriocin / Lactic Acid Bacteria / Alpha Helix / Mannose Phospho-transferase system | ||||||
Function / homology | Bacteriocin, class IId / Lactococcin-like family / Bacteriocin-type signal sequence / defense response to bacterium / extracellular region / Prepeptide GarQ![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
![]() | Mallett, T.M. / Lamer, T. / Aleksandrzak-Piekarczyk, T. / Mckay, R.T. / Sit, C.S. / Rainey, J.K. / Van Belkum, M. / Vederas, J.C. | ||||||
Funding support | 1items
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![]() | ![]() Title: Solution Structure of the Broad-Spectrum Bacteriocin Garvicin Q Authors: Mallett, T. / Lamer, T. / Aleksandrzak-Piekarczyk, T. / McKay, R.T. / Catenza, K. / Sit, C. / Rainey, J.K. / Towle-Straub, K.M. / Vederas, J.C. / van Belkum, M.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 292.8 KB | Display | ![]() |
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PDB format | ![]() | 245.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 536.6 KB | Display | ![]() |
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Full document | ![]() | 660.1 KB | Display | |
Data in XML | ![]() | 25.2 KB | Display | |
Data in CIF | ![]() | 37.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9oiuC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
Other databases |
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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: 5349.951 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: BCC 43578 / Gene: garQ / Plasmid: pSPIH6 / Production host: ![]() ![]() |
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Has protein modification | N |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 1.0 mM [U-99% 13C; U-99% 15N] Garvicin Q, trifluoroethanol/water Details: 50 percent TFE in water, 100 microlitres. / Label: 13C,15N_Garvicin Q / Solvent system: trifluoroethanol/water |
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Sample | Conc.: 1.0 mM / Component: Garvicin Q / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Details: 50 percent TFE in water, 100 microlitres. / Ionic strength: 0 Not defined / Ionic strength err: 0.1 / Label: GarQ_Conditions / pH: 7 / PH err: 0.1 / Pressure: 1 atm / Pressure err: 0.1 / Temperature: 300.5 K / Temperature err: 2 |
-NMR measurement
NMR spectrometer |
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Processing
Software | Name: THESEUS / Version: 3.3.0 / Classification: refinement | ||||||||||||||||||||
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NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 2 | ||||||||||||||||||||
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 |