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Yorodumi- PDB-2l5b: Solution structure of the transmembrane domain of Bcl-2 member Ha... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l5b | ||||||
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Title | Solution structure of the transmembrane domain of Bcl-2 member Harakiri in micelles | ||||||
Components | Activator of apoptosis harakiri | ||||||
Keywords | APOPTOSIS / Bcl-2 / BH3-only / Harakiri / transmembrane domain | ||||||
Function / homology | Function and homology information positive regulation of release of cytochrome c from mitochondria / positive regulation of protein-containing complex assembly / positive regulation of apoptotic process / apoptotic process / mitochondrion / membrane Similarity search - Function | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Barrera-Vilarmau, S. / Obregon, P. / de Alba, E. | ||||||
Citation | Journal: Plos One / Year: 2011 Title: Intrinsic order and disorder in the bcl-2 member harakiri: insights into its proapoptotic activity. Authors: Barrera-Vilarmau, S. / Obregon, P. / de Alba, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l5b.cif.gz | 184.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l5b.ent.gz | 159.8 KB | Display | PDB format |
PDBx/mmJSON format | 2l5b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2l5b_validation.pdf.gz | 333.8 KB | Display | wwPDB validaton report |
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Full document | 2l5b_full_validation.pdf.gz | 416.4 KB | Display | |
Data in XML | 2l5b_validation.xml.gz | 11.8 KB | Display | |
Data in CIF | 2l5b_validation.cif.gz | 19.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l5/2l5b ftp://data.pdbj.org/pub/pdb/validation_reports/l5/2l5b | 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: 3321.918 Da / Num. of mol.: 1 / Fragment: UNP Residues 61-91 / Source method: obtained synthetically / Details: chemically synthesized / References: UniProt: O00198 |
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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 | Ionic strength: 0.2 / pH: 3.2 / Pressure: ambient / Temperature: 323 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / 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: 200 / Conformers submitted total number: 20 |