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Open data
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Basic information
Entry | Database: PDB / ID: 2l9a | ||||||
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Title | Solution structure of LAK160-P12 | ||||||
![]() | LAK160-P12 | ||||||
![]() | DE NOVO PROTEIN / ANTIMICROBIAL PROTEIN / cationic / proline / ampiphatic | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 2 | ||||||
![]() | Vermeer, L.S. / Bui, T.T. / Lan, Y. / Jumagulova, E. / Kozlowska, J. / McIntyre, C. / Drake, A.F. / Mason, J.A. | ||||||
![]() | ![]() Title: The role of proline induced conformational flexibility in determining the antibacterial potency of linear cationic alpha-helical peptides Authors: Vermeer, L.S. / Bui, T.T. / Lan, Y. / Jumagulova, E. / Kozlowska, J. / McIntyre, C. / Drake, A.F. / Mason, J.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.8 KB | Display | ![]() |
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PDB format | ![]() | 70.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 346.9 KB | Display | ![]() |
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Full document | ![]() | 387.6 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 8.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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: 2666.508 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthesized by solid phase synthesis / Source: (synth.) synthetic construct (others) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: synthetic cationic antimicrobial peptide LAK160-P12 | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1mM LAK160-P12; 100mM SDS; 5mM TRIS; 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100mM / pH: 7 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
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Processing
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Refinement | Method: molecular dynamics / Software ordinal: 1 / Details: Default ARIA refinement in water | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 81 / NOE intraresidue total count: 23 / NOE long range total count: 0 / NOE medium range total count: 28 / NOE sequential total count: 30 | ||||||||||||||||||||||||||||||||||||||||||||
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 / Representative conformer: 2 |