+Open data
-Basic information
Entry | Database: PDB / ID: 2n9n | ||||||
---|---|---|---|---|---|---|---|
Title | solution structure of VG16KRKP in C.neoformans (conformation 1) | ||||||
Components | antimicrobial peptide | ||||||
Keywords | ANTIMICROBIAL PROTEIN / antimicrobial peptide | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Bhunia, A. / Datta, A. | ||||||
Citation | Journal: To be Published Title: solution structure of VG16KRKP in C.neoformans (conformation 1) Authors: Datta, A. / Bhunia, A. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2n9n.cif.gz | 110.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2n9n.ent.gz | 83.7 KB | Display | PDB format |
PDBx/mmJSON format | 2n9n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n9n_validation.pdf.gz | 418.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2n9n_full_validation.pdf.gz | 522.7 KB | Display | |
Data in XML | 2n9n_validation.xml.gz | 8.4 KB | Display | |
Data in CIF | 2n9n_validation.cif.gz | 11.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n9/2n9n ftp://data.pdbj.org/pub/pdb/validation_reports/n9/2n9n | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein/peptide | Mass: 1765.157 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1 mM protein, 55.5 mM H2O, 10 mM sodium phosphate, 1 mM DSS, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| |||||||||||||||
Sample conditions | pH: 5.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
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: 20 |