+Open data
-Basic information
Entry | Database: PDB / ID: 2nas | ||||||
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Title | Solution structure of a PWWP doamin from Trypanosoma brucei | ||||||
Components | Uncharacterized protein | ||||||
Keywords | DNA BINDING PROTEIN / PWWP | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Trypanosoma brucei brucei TREU927 (eukaryote) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Wang, R. / Liao, S. / Dai, K. / Zhang, J. / Tu, X. | ||||||
Citation | Journal: To be Published Title: Soluion Structure of a PWWP domain from Trypanosoma brucei Authors: Wang, R. / Liao, S. / Dai, K. / Zhang, J. / Tu, X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nas.cif.gz | 756 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nas.ent.gz | 643.6 KB | Display | PDB format |
PDBx/mmJSON format | 2nas.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2nas_validation.pdf.gz | 539.5 KB | Display | wwPDB validaton report |
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Full document | 2nas_full_validation.pdf.gz | 862.3 KB | Display | |
Data in XML | 2nas_validation.xml.gz | 89.4 KB | Display | |
Data in CIF | 2nas_validation.cif.gz | 76.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/na/2nas ftp://data.pdbj.org/pub/pdb/validation_reports/na/2nas | HTTPS FTP |
-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: 12346.772 Da / Num. of mol.: 1 / Fragment: PWWP DOMAIN (UNP RESIDUES 1-110) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei TREU927 (eukaryote) Strain: TREU927 / Gene: Tb927.2.3480 / Production host: Escherichia coli (E. coli) / References: UniProt: Q586Y0 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 25 mM [U-99% 13C; U-99% 15N] sodium phosphate-1, 150 mM [U-99% 13C; U-99% 15N] sodium chloride-2, 2 mM [U-99% 13C; U-99% 15N] DTT-3, 100% D2O Solvent system: 100% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 150 / pH: 6.8 / Pressure: ambient atm / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry 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: 500 / Conformers submitted total number: 20 / Representative conformer: 1 |