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Open data
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Basic information
Entry | Database: PDB / ID: 2kyq | ||||||
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Title | 1H, 15N, 13C chemical shifts and structure of CKR-brazzein | ||||||
![]() | Defensin-like protein | ||||||
![]() | PLANT PROTEIN / SWEET-TASTING PROTEIN | ||||||
Function / homology | ![]() defense response to fungus / killing of cells of another organism / defense response to bacterium / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | closest to the average, model 9 | ||||||
![]() | Dittli, S.M. / Assadi-Porter, F.M. / Rao, H. / Tonelli, M. | ||||||
![]() | ![]() Title: Structural role of the terminal disulfide bond in the sweetness of brazzein. Authors: Dittli, S.M. / Rao, H. / Tonelli, M. / Quijada, J. / Markley, J.L. / Max, M. / Assadi-Porter, F. #1: ![]() Title: Insights into the sweetness of brazzein from beta-hairpin peptides derived from the N- and C- termini of brazzein Authors: Dittli, S.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 377.5 KB | Display | ![]() |
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PDB format | ![]() | 329.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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 | Mass: 6408.243 Da / Num. of mol.: 1 / Mutation: K3C, C4K, K5R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR / Details: Triple brazzein mutant: K3C,C4K,K5R | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | pH: 5.2 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 741 / NOE intraresidue total count: 157 / NOE long range total count: 213 / NOE medium range total count: 134 / NOE sequential total count: 249 / Hydrogen bond constraints total count: 28 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 94 / Protein psi angle constraints total count: 94 | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |