+Open data
-Basic information
Entry | Database: PDB / ID: 2ltb | ||||||
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Title | Wild-type FAS1-4 | ||||||
Components | Transforming growth factor-beta-induced protein ig-h3 | ||||||
Keywords | UNKNOWN FUNCTION | ||||||
Function / homology | Function and homology information negative regulation of cell adhesion / extracellular matrix binding / response to stimulus / extracellular matrix structural constituent / basement membrane / localization / chondrocyte differentiation / collagen binding / extracellular matrix / visual perception ...negative regulation of cell adhesion / extracellular matrix binding / response to stimulus / extracellular matrix structural constituent / basement membrane / localization / chondrocyte differentiation / collagen binding / extracellular matrix / visual perception / cell adhesion molecule binding / extracellular matrix organization / trans-Golgi network / integrin binding / collagen-containing extracellular matrix / angiogenesis / cell population proliferation / cell adhesion / Amyloid fiber formation / extracellular space / extracellular exosome / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Authors | Underhaug, J. / Nielsen, N. / Runager, K. | ||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2013 Title: Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization. Authors: Underhaug, J. / Kolds, H. / Runager, K. / Nielsen, J.T. / Srensen, C.S. / Kristensen, T. / Otzen, D.E. / Karring, H. / Malmendal, A. / Schitt, B. / Enghild, J.J. / Nielsen, N.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ltb.cif.gz | 404.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ltb.ent.gz | 348.6 KB | Display | PDB format |
PDBx/mmJSON format | 2ltb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lt/2ltb ftp://data.pdbj.org/pub/pdb/validation_reports/lt/2ltb | 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: 14481.680 Da / Num. of mol.: 1 / Fragment: FAS1 4 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TGFBI, BIGH3 / Plasmid: pET SUMO / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q15582 |
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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 | pH: 7.4 / Pressure: ambient / Temperature: 300 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | |||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1802 / NOE intraresidue total count: 764 / NOE long range total count: 501 / NOE medium range total count: 161 / NOE sequential total count: 376 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 117 / Protein psi angle constraints total count: 117 | |||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |