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Yorodumi- PDB-2jua: Assignment, structure, and dynamics of de novo designed protein S836 -
+Open data
-Basic information
Entry | Database: PDB / ID: 2jua | ||||||
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Title | Assignment, structure, and dynamics of de novo designed protein S836 | ||||||
Components | de novo protein S836 | ||||||
Keywords | DE NOVO PROTEIN | ||||||
Function / homology | Designed four-helix bundle protein / hypothetical protein mp506/mpn330, domain 1 / Up-down Bundle / Mainly Alpha Function and homology information | ||||||
Biological species | unidentified (others) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Go, A. / Kim, S. / Baum, J.S. / Hecht, M.H. | ||||||
Citation | Journal: Protein Sci. / Year: 2008 Title: Structure and dynamics of de novo proteins from a designed superfamily of 4-helix bundles. Authors: Go, A. / Kim, S. / Baum, J. / Hecht, M.H. #1: Journal: To be Published Title: NMR assignment of S836: a de novo Protein from a Designed Protein Superfamily Authors: Go, A. / Kim, S. / Hecht, M.H. / Baum, J.S. | ||||||
History |
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Remark 999 | Sequence This is a de novo Protein design sequence. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jua.cif.gz | 639.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jua.ent.gz | 533.2 KB | Display | PDB format |
PDBx/mmJSON format | 2jua.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jua_validation.pdf.gz | 339.2 KB | Display | wwPDB validaton report |
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Full document | 2jua_full_validation.pdf.gz | 532.4 KB | Display | |
Data in XML | 2jua_validation.xml.gz | 64.4 KB | Display | |
Data in CIF | 2jua_validation.cif.gz | 85.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ju/2jua ftp://data.pdbj.org/pub/pdb/validation_reports/ju/2jua | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11946.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Ambiguous conformational states: Y2, Q24, and N84 register possible alternate alpha carbon chemical shifts Source: (gene. exp.) unidentified (others) / Plasmid: pet3A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) |
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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: 4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||
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 |