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Yorodumi- PDB-2lx2: 1H,13C,15N assignments for an isoform of the type III antifreeze ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lx2 | ||||||
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Title | 1H,13C,15N assignments for an isoform of the type III antifreeze protein from notched-fin eelpout | ||||||
Components | Type III antifreeze protein nfeAFP11 | ||||||
Keywords | ANTIFREEZE PROTEIN / ice-binding / thermal hysteresis / anchored clathrate waters | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Zoarces elongatus (fish) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Kumeta, H. / Ogura, K. / Nishimiya, Y. / Miura, A. / Inagaki, F. / Tsuda, S. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2013 Title: NMR structure note: a defective isoform and its activity-improved variant of a type III antifreeze protein from Zoarces elongates Kner Authors: Kumeta, H. / Ogura, K. / Nishimiya, Y. / Miura, A. / Inagaki, F. / Tsuda, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lx2.cif.gz | 450.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lx2.ent.gz | 387.9 KB | Display | PDB format |
PDBx/mmJSON format | 2lx2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lx/2lx2 ftp://data.pdbj.org/pub/pdb/validation_reports/lx/2lx2 | HTTPS FTP |
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-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 | Mass: 7071.388 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Zoarces elongatus (fish) / Production host: Escherichia coli (E. coli) / References: UniProt: Q53UI9 |
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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: 2mM [U-100% 13C; U-100% 15N] nfeAFP11-1, 20mM potassium chloride-2, 0.1mM DSS-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 20 / pH: 6.8 / Pressure: ambient / Temperature: 277 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, torsion angle dynamics Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 20 / Representative conformer: 1 |