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Yorodumi- PDB-2l6r: High resolution NMR structure of gpW (W protein of bacteriophage ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l6r | ||||||
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Title | High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH | ||||||
Components | Head-to-tail joining protein W (GpW) from bacteriophage origin | ||||||
Keywords | VIRAL PROTEIN / gpW / atom by atom analysis / fast protein folding / downhill protein folding / folding simulations | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Enterobacteria phage lambda (virus) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing, distance geometry | ||||||
Authors | Sborgi, L. / Verma, A. / Munoz, V. / de Alba, E. | ||||||
Citation | Journal: To be Published Title: High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH Authors: Sborgi, L. / Verma, A. / Munoz, V. / 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 | 2l6r.cif.gz | 365.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l6r.ent.gz | 317.4 KB | Display | PDB format |
PDBx/mmJSON format | 2l6r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l6/2l6r ftp://data.pdbj.org/pub/pdb/validation_reports/l6/2l6r | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6989.052 Da / Num. of mol.: 1 / Fragment: UNP residues 1-62 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage lambda (virus) / Gene: W / Production host: Escherichia coli (E. coli) / References: UniProt: P68660*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: NMR model structure for atom by atom analysis of gpW unfolding | ||||||||||||||||||||||||||||||||||||||||
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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: 0.02 / pH: 3.5 / Pressure: ambient / Temperature: 293.1 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, distance geometry 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: 19 |