+Open data
-Basic information
Entry | Database: PDB / ID: 2go0 | ||||||
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Title | NMR solution structure of human pancreatitis-associated protein | ||||||
Components | Regenerating islet-derived protein 3 alpha | ||||||
Keywords | PROTEIN BINDING / C-type lectin / fibril | ||||||
Function / homology | Function and homology information disruption of cell wall in another organism / positive regulation of detection of glucose / response to symbiotic bacterium / positive regulation of keratinocyte proliferation / negative regulation of keratinocyte differentiation / negative regulation of inflammatory response to wounding / oligosaccharide binding / peptidoglycan binding / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / Antimicrobial peptides ...disruption of cell wall in another organism / positive regulation of detection of glucose / response to symbiotic bacterium / positive regulation of keratinocyte proliferation / negative regulation of keratinocyte differentiation / negative regulation of inflammatory response to wounding / oligosaccharide binding / peptidoglycan binding / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / Antimicrobial peptides / positive regulation of wound healing / acute-phase response / hormone activity / response to peptide hormone / response to wounding / negative regulation of inflammatory response / antimicrobial humoral immune response mediated by antimicrobial peptide / signaling receptor activity / carbohydrate binding / positive regulation of cell population proliferation / extracellular space / extracellular region / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, torsion angle dynamics | ||||||
Authors | Chen, C.P. / Ho, M.R. / Lou, Y.C. | ||||||
Citation | Journal: To be Published Title: Human pancreatitis-associated protein forms fibrillar aggregate with native-like conformation. Authors: Ho, M.R. / Lou, Y.C. / Lin, W.C. / Lyu, P.C. / Chen, C.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2go0.cif.gz | 800.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2go0.ent.gz | 691.8 KB | Display | PDB format |
PDBx/mmJSON format | 2go0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/go/2go0 ftp://data.pdbj.org/pub/pdb/validation_reports/go/2go0 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 15175.892 Da / Num. of mol.: 1 / Fragment: residues 1-137 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q06141 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | pH: 4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry, simulated annealing, torsion angle dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |