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Open data
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Basic information
Entry | Database: PDB / ID: 2nd3 | ||||||
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Title | Solution structure of the de novo mini protein gEEH_04 | ||||||
![]() | De novo mini protein EEH_04 | ||||||
![]() | ![]() ![]() | ||||||
Biological species | artificial gene (others) | ||||||
Method | ![]() ![]() | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Pulavarti, S.V. / Bahl, C.D. / Gilmore, J.M. / Eletsky, A. / Buchko, G.W. / Baker, D. / Szyperski, T. | ||||||
![]() | ![]() Title: Accurate de novo design of hyperstable constrained peptides. Authors: Bhardwaj, G. / Mulligan, V.K. / Bahl, C.D. / Gilmore, J.M. / Harvey, P.J. / Cheneval, O. / Buchko, G.W. / Pulavarti, S.V. / Kaas, Q. / Eletsky, A. / Huang, P.S. / Johnsen, W.A. / Greisen, P. ...Authors: Bhardwaj, G. / Mulligan, V.K. / Bahl, C.D. / Gilmore, J.M. / Harvey, P.J. / Cheneval, O. / Buchko, G.W. / Pulavarti, S.V. / Kaas, Q. / Eletsky, A. / Huang, P.S. / Johnsen, W.A. / Greisen, P.J. / Rocklin, G.J. / Song, Y. / Linsky, T.W. / Watkins, A. / Rettie, S.A. / Xu, X. / Carter, L.P. / Bonneau, R. / Olson, J.M. / Coutsias, E. / Correnti, C.E. / Szyperski, T. / Craik, D.J. / Baker, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 282.1 KB | Display | ![]() |
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PDB format | ![]() | 241.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2nd2C ![]() 5jg9C ![]() 5jhiC ![]() 5ji4C ![]() 5kvnC ![]() 5kwoC ![]() 5kwpC ![]() 5kwxC ![]() 5kwzC ![]() 5kx0C ![]() 5kx1C ![]() 5kx2C C: citing same article ( |
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Similar structure data | |
Other databases |
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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: 4664.215 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) artificial gene (others) / Production host: ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1 mM [U-10% 13C; U-100% 15N] EEH_04, 50 mM sodium phosphate, 4 uM DSS, 0.02 % sodium azide, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 50 / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: distance geometry, ![]() | |||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 614 / NOE intraresidue total count: 135 / NOE long range total count: 157 / NOE medium range total count: 156 / NOE sequential total count: 166 | |||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |