+Open data
-Basic information
Entry | Database: PDB / ID: 2muz | ||||||
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Title | ssNMR structure of a designed rocker protein | ||||||
Components | designed rocker protein | ||||||
Keywords | DE NOVO PROTEIN / ssNMR / Rocker protein / DE NOVO desgin | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / Torsion angles ajustments using Chimera, Pymol, CODEX data fitting by Matlab. | ||||||
Authors | Wang, T. / Joh, N. / Wu, Y. / DeGrado, W.F. / Hong, M. | ||||||
Citation | Journal: Science / Year: 2014 Title: De novo design of a transmembrane Zn2+-transporting four-helix bundle. Authors: Joh, N.H. / Wang, T. / Bhate, M.P. / Acharya, R. / Wu, Y. / Grabe, M. / Hong, M. / Grigoryan, G. / DeGrado, W.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2muz.cif.gz | 18.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2muz.ent.gz | 13.1 KB | Display | PDB format |
PDBx/mmJSON format | 2muz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2muz_validation.pdf.gz | 342.6 KB | Display | wwPDB validaton report |
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Full document | 2muz_full_validation.pdf.gz | 343.2 KB | Display | |
Data in XML | 2muz_validation.xml.gz | 3.6 KB | Display | |
Data in CIF | 2muz_validation.cif.gz | 4.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mu/2muz ftp://data.pdbj.org/pub/pdb/validation_reports/mu/2muz | HTTPS FTP |
-Related structure data
Related structure data | 4p6jC 4p6kC 4p6lC 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: 2971.427 Da / Num. of mol.: 4 / 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 | Type: 19F CODEX |
-Sample preparation
Details | Contents: 1.5 mg/mL protein, 100% H2O / Solvent system: 100% H2O |
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Sample | Conc.: 1.5 mg/mL / Component: entity_1-1 / Isotopic labeling: F19 on Phe 14 |
Sample conditions | Ionic strength: 0.02 / pH: 7.0 / Pressure: ambient / Temperature: 220 K |
-NMR measurement
NMR spectrometer | Type: Bruker DSX / Manufacturer: Bruker / Model: DSX / Field strength: 400 MHz |
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-Processing
NMR software |
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Refinement | Method: Torsion angles ajustments using Chimera, Pymol, CODEX data fitting by Matlab. Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 1 / Conformers submitted total number: 1 |