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- PDB-2lkt: Solution structure of N-terminal domain of human TIG3 in 2 M UREA -
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Open data
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Basic information
Entry | Database: PDB / ID: 2lkt | ||||||
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Title | Solution structure of N-terminal domain of human TIG3 in 2 M UREA | ||||||
![]() | Retinoic acid receptor responder protein 3 | ||||||
![]() | HYDROLASE / TIG3 / human tumor suppressor II family / NlpC/P60 | ||||||
Function / homology | ![]() positive regulation of protein-glutamine gamma-glutamyltransferase activity / phosphatidylethanolamine acyl-chain remodeling / N-acylphosphatidylethanolamine metabolic process / phospholipase A1 / : / phospholipase A1 activity / Acyl chain remodelling of PE / N-acyltransferase activity / phospholipase A2 activity / positive regulation of keratinocyte differentiation ...positive regulation of protein-glutamine gamma-glutamyltransferase activity / phosphatidylethanolamine acyl-chain remodeling / N-acylphosphatidylethanolamine metabolic process / phospholipase A1 / : / phospholipase A1 activity / Acyl chain remodelling of PE / N-acyltransferase activity / phospholipase A2 activity / positive regulation of keratinocyte differentiation / phospholipase A2 / calcium-independent phospholipase A2 activity / calcium-dependent phospholipase A2 activity / acyltransferase activity / lipid catabolic process / phospholipid metabolic process / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / negative regulation of cell population proliferation / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Wang, L. / Yu, W. / Xia, B. | ||||||
![]() | ![]() Title: (1)H, (13)C, and (15)N resonance assignments of the N-terminal domain of human TIG3 Authors: Wang, L. / Yu, W. / Ren, X. / Lin, J. / Jin, C. / Xia, B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 762.9 KB | Display | ![]() |
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PDB format | ![]() | 640.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 409.3 KB | Display | ![]() |
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Full document | ![]() | 508.2 KB | Display | |
Data in XML | ![]() | 36.2 KB | Display | |
Data in CIF | ![]() | 63.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 14050.886 Da / Num. of mol.: 1 / Fragment: NlpC/P60 structural domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9UL19, Hydrolases; Acting on ester bonds; Carboxylic-ester hydrolases |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Solution structure of N-terminal domain of human TIG3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 0.5 mM [U-13C; U-15N] TIG3N protein-1, 50 mM sodium phosphate-2, 50 mM sodium chloride-3, 20 mM DTT-4, 2 M urea-5, 95 % H2O-6, 5 % [U-2H] D2O-7, 0.01 % DSS-8, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 100 / pH: 7 / Pressure: 1 atm / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: using AMBER ff03 force filed refinement | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 3218 / NOE intraresidue total count: 1144 / NOE long range total count: 454 / NOE medium range total count: 233 / NOE sequential total count: 509 | ||||||||||||||||||||||||||||||||||||||||||||
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: 20 / Maximum lower distance constraint violation: 0.099 Å / Maximum upper distance constraint violation: 0.231 Å / Representative conformer: 1 |