+Open data
-Basic information
Entry | Database: PDB / ID: 2dx3 | ||||||
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Title | NMR structure of DP5_conformation1: monomeric alpha-helix | ||||||
Components | DP5_conformation1 | ||||||
Keywords | DE NOVO PROTEIN / alpha-helix | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Tamura, A. / Araki, M. | ||||||
Citation | Journal: Proteins / Year: 2006 Title: Transformation of an alpha-helix peptide into a beta-hairpin induced by addition of a fragment results in creation of a coexisting state. Authors: Araki, M. / Tamura, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2dx3.cif.gz | 56.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dx3.ent.gz | 38.8 KB | Display | PDB format |
PDBx/mmJSON format | 2dx3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2dx3_validation.pdf.gz | 340.3 KB | Display | wwPDB validaton report |
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Full document | 2dx3_full_validation.pdf.gz | 384.8 KB | Display | |
Data in XML | 2dx3_validation.xml.gz | 6.7 KB | Display | |
Data in CIF | 2dx3_validation.cif.gz | 9.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dx/2dx3 ftp://data.pdbj.org/pub/pdb/validation_reports/dx/2dx3 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2117.430 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized and does not appear to occur in nature. This sequence was designed based on a strategy. |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: This structures were determined using standard 2D homonuclear techniques |
-Sample preparation
Details | Contents: 1mM TP; 10mM acetic acid-3mM NAOH buffer, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 6.5mM / pH: 4.5 / Pressure: ambient / Temperature: 283 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 750 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: fewest violations | |||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 10 |