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Yorodumi- PDB-1x5j: The solution structure of the fifth fibronectin type III domain o... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1x5j | ||||||
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Title | The solution structure of the fifth fibronectin type III domain of human Neogenin | ||||||
Components | Neogenin | ||||||
Keywords | CELL ADHESION / RGM binding / fibronectin type III domain / structural genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information negative regulation of axon regeneration / Netrin-1 signaling / co-receptor binding / BMP receptor binding / plasma membrane protein complex / myoblast fusion / positive regulation of BMP signaling pathway / intracellular vesicle / Myogenesis / negative regulation of protein secretion ...negative regulation of axon regeneration / Netrin-1 signaling / co-receptor binding / BMP receptor binding / plasma membrane protein complex / myoblast fusion / positive regulation of BMP signaling pathway / intracellular vesicle / Myogenesis / negative regulation of protein secretion / protein secretion / axonal growth cone / axon guidance / neuron migration / cell-cell adhesion / multicellular organismal-level iron ion homeostasis / signaling receptor activity / intracellular iron ion homeostasis / cell adhesion / cadherin binding / regulation of DNA-templated transcription / Golgi apparatus / cell surface / nucleoplasm / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tochio, N. / Sasagawa, A. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: The solution structure of the fifth fibronectin type III domain of human Neogenin Authors: Tochio, N. / Sasagawa, A. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1x5j.cif.gz | 668.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1x5j.ent.gz | 558.9 KB | Display | PDB format |
PDBx/mmJSON format | 1x5j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1x5j_validation.pdf.gz | 341 KB | Display | wwPDB validaton report |
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Full document | 1x5j_full_validation.pdf.gz | 484.9 KB | Display | |
Data in XML | 1x5j_validation.xml.gz | 37.6 KB | Display | |
Data in CIF | 1x5j_validation.cif.gz | 58 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x5/1x5j ftp://data.pdbj.org/pub/pdb/validation_reports/x5/1x5j | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12342.897 Da / Num. of mol.: 1 / Fragment: fn3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: NEO1 / Plasmid: P041213-06 / References: UniProt: Q92859 |
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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: 1.3mM FN3 domain U-15N,13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |