+Open data
-Basic information
Entry | Database: PDB / ID: 5kx2 | ||||||
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Title | NMR Solution Structure of Designed Peptide NC_cEE_D1 | ||||||
Components | Designed peptide NC_cEE_D1 | ||||||
Keywords | DE NOVO PROTEIN / synthetic designed peptide | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Harvey, P.J. / Craik, D.J. | ||||||
Citation | Journal: Nature / Year: 2016 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5kx2.cif.gz | 105.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5kx2.ent.gz | 74 KB | Display | PDB format |
PDBx/mmJSON format | 5kx2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kx/5kx2 ftp://data.pdbj.org/pub/pdb/validation_reports/kx/5kx2 | HTTPS FTP |
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-Related structure data
Related structure data | 2nd2C 2nd3C 5jg9C 5jhiC 5ji4C 5kvnC 5kwoC 5kwpC 5kwxC 5kwzC 5kx0C 5kx1C C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2083.544 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength units: Not defined / Label: conditions_1 / pH: 3.0 / PH err: 0.1 / Pressure: ambient / Temperature: 298 K / Temperature err: 0.1 |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 4 | ||||||||||||||||||||
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 |