+Open data
-Basic information
Entry | Database: PDB / ID: 2kmz | ||||||
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Title | NMR Structure of hFn14 | ||||||
Components | Tumor necrosis factor receptor superfamily member 12A | ||||||
Keywords | APOPTOSIS / Fn14 / TWEAK / TNF Receptor / CRD / TNFRSF12A / Angiogenesis / Cell adhesion / Developmental protein / Differentiation / Disulfide bond / Membrane / Receptor / Transmembrane | ||||||
Function / homology | Function and homology information TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / regulation of wound healing / positive regulation of extrinsic apoptotic signaling pathway / TNFR2 non-canonical NF-kB pathway / angiogenesis / cell differentiation / cell adhesion / positive regulation of apoptotic process / apoptotic process / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | fewest violations, model 1 | ||||||
Authors | Pellegrini, M. / Willen, L. / Perroud, M. / Krushinskie, D. / Strauch, K. / Cuervo, H. / Sun, Y. / Day, E.S. / Schneider, P. / Zheng, T.S. | ||||||
Citation | Journal: Febs J. / Year: 2013 Title: Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions. Authors: Pellegrini, M. / Willen, L. / Perroud, M. / Krushinskie, D. / Strauch, K. / Cuervo, H. / Day, E.S. / Schneider, P. / Zheng, T.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kmz.cif.gz | 293.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kmz.ent.gz | 252.9 KB | Display | PDB format |
PDBx/mmJSON format | 2kmz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/km/2kmz ftp://data.pdbj.org/pub/pdb/validation_reports/km/2kmz | 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: 5615.390 Da / Num. of mol.: 1 / Fragment: CRD, residues 28-80 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FN14, TNFRSF12A / Production host: Pichia pastoris (fungus) / References: UniProt: Q9NP84 |
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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: 140 / pH: 7.4 / Pressure: ambient / Temperature: 298 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: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||
NMR ensemble | Conformer selection criteria: 20 lowest energy structures / Conformers calculated total number: 100 / Conformers submitted total number: 20 |