+Open data
-Basic information
Entry | Database: PDB / ID: 2l96 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of LAK160-P7 | ||||||
Components | LAK160-P7 | ||||||
Keywords | DE NOVO PROTEIN / ANTIMICROBIAL PROTEIN / cationic / proline / ampiphatic | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Vermeer, L.S. / Bui, T.T. / Lan, Y. / Jumagulova, E. / Kozlowska, J. / McIntyre, C. / Drake, A.F. / Mason, J.A. | ||||||
Citation | Journal: To be Published 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2l96.cif.gz | 86.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2l96.ent.gz | 71.4 KB | Display | PDB format |
PDBx/mmJSON format | 2l96.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2l96_validation.pdf.gz | 354.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2l96_full_validation.pdf.gz | 396.8 KB | Display | |
Data in XML | 2l96_validation.xml.gz | 6.1 KB | Display | |
Data in CIF | 2l96_validation.cif.gz | 8.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l9/2l96 ftp://data.pdbj.org/pub/pdb/validation_reports/l9/2l96 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-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) |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Synthetic cationic anti-microbial peptide LAK160-P7 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1mM LAK160-P7; 100mM SDS; 5mM TRIS; 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||
Sample conditions | Ionic strength: 105mM / pH: 7 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: molecular dynamics / Software ordinal: 1 / Details: Standard ARIA refinement in water | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 82 / NOE intraresidue total count: 23 / NOE long range total count: 0 / NOE medium range total count: 24 / NOE sequential total count: 35 | ||||||||||||||||||||||||||||||||||||||||||||
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: 8 |