+Open data
-Basic information
Entry | Database: PDB / ID: 2jre | ||||||
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Title | C60-1, a PDZ domain designed using statistical coupling analysis | ||||||
Components | C60-1 PDZ domain peptide | ||||||
Keywords | DE NOVO PROTEIN / C60-1 / PDZ | ||||||
Function / homology | PDZ domain / Pdz3 Domain / Roll / Mainly Beta Function and homology information | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Larson, C. / Stiffler, M. / Li, P. / Rosen, M. / MacBeath, G. / Ranganathan, R. | ||||||
Citation | Journal: To be Published Title: C60-1, a PDZ domain designed using statistical coupling analysis Authors: Larson, C. / Stiffler, M. / Li, P. / Rosen, M. / MacBeath, G. / Ranganathan, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jre.cif.gz | 872.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jre.ent.gz | 744 KB | Display | PDB format |
PDBx/mmJSON format | 2jre.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jr/2jre ftp://data.pdbj.org/pub/pdb/validation_reports/jr/2jre | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11589.026 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide is a synthetic construct designed using statistical coupling analysis and expressed in Escherichia coli BL21 cells using the pHis8.3 vector. |
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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 | pH: 6.5 / Temperature: 288 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1718 / NOE intraresidue total count: 675 / NOE long range total count: 430 / NOE medium range total count: 152 / NOE sequential total count: 378 / Hydrogen bond constraints total count: 64 / Protein phi angle constraints total count: 51 / Protein psi angle constraints total count: 51 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 25 |