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- PDB-6ats: Exploring Cystine Dense Peptide Space to Open a Unique Molecular ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6ats | ||||||
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Title | Exploring Cystine Dense Peptide Space to Open a Unique Molecular Toolbox | ||||||
![]() | Potassium channel toxin kappa-KTx 1.2 | ||||||
![]() | TOXIN / Knottins / Cystine knot / Toxins | ||||||
Function / homology | Hefutoxin / Hefutoxin family / potassium channel regulator activity / defense response to fungus / toxin activity / killing of cells of another organism / extracellular region / Potassium channel toxin kappa-KTx 1.2![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Gewe, M.M. / Rupert, P. / Strong, R.K. | ||||||
![]() | ![]() Title: Screening, large-scale production and structure-based classification of cystine-dense peptides. Authors: Correnti, C.E. / Gewe, M.M. / Mehlin, C. / Bandaranayake, A.D. / Johnsen, W.A. / Rupert, P.B. / Brusniak, M.Y. / Clarke, M. / Burke, S.E. / De Van Der Schueren, W. / Pilat, K. / Turnbaugh, S. ...Authors: Correnti, C.E. / Gewe, M.M. / Mehlin, C. / Bandaranayake, A.D. / Johnsen, W.A. / Rupert, P.B. / Brusniak, M.Y. / Clarke, M. / Burke, S.E. / De Van Der Schueren, W. / Pilat, K. / Turnbaugh, S.M. / May, D. / Watson, A. / Chan, M.K. / Bahl, C.D. / Olson, J.M. / Strong, R.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 14.5 KB | Display | ![]() |
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PDB format | ![]() | 9.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 402.4 KB | Display | ![]() |
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Full document | ![]() | 402.4 KB | Display | |
Data in XML | ![]() | 3.7 KB | Display | |
Data in CIF | ![]() | 4.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6atlC ![]() 6atnC ![]() 6atuC ![]() 6atwC ![]() 6au7C ![]() 6aupC ![]() 6av8C ![]() 6avaC ![]() 6avcC ![]() 6avdC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein/peptide | Mass: 2866.093 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Cell line (production host): HEK-293F / Production host: ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.78 Å3/Da / Density % sol: 30.9 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.5 / Details: 0.1M Tris pH 8.5, 20% Ethanol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944+ / Detector: CCD / Date: Mar 8, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 2535 / % possible obs: 89.6 % / Redundancy: 2.7 % / CC1/2: 0.994 / Rmerge(I) obs: 0.032 / Rpim(I) all: 0.022 / Χ2: 1.506 / Net I/σ(I): 14.45 |
Reflection shell | Resolution: 1.9→1.98 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.035 / Num. unique obs: 63 / CC1/2: 0.994 / Rpim(I) all: 0.028 / % possible all: 45 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.29 Å2
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Refinement step | Cycle: 1 / Resolution: 1.9→23.03 Å
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Refine LS restraints |
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