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Yorodumi- PDB-2n1h: Solution structure of the GBII-beta MRH domain W409A point mutant -
+Open data
-Basic information
Entry | Database: PDB / ID: 2n1h | ||||||
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Title | Solution structure of the GBII-beta MRH domain W409A point mutant | ||||||
Components | Glucosidase 2 subunit beta | ||||||
Keywords | HYDROLASE / lectin / MRH | ||||||
Function / homology | Function and homology information mannan binding / glucosidase II complex / N-glycan processing / enzyme-substrate adaptor activity / protein N-linked glycosylation / D-mannose binding / enzyme regulator activity / endoplasmic reticulum lumen / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Olson, L.J. / Peterson, F.C. / Damhs, N.M. | ||||||
Citation | Journal: To be Published Title: Crystal structure and functional analyses of glucosdidase II's lectin domain: Insgihts into oligomannose recognition. Authors: Olson, L.J. / Orsi, R. / Peterson, F.C. / Parodi, A.J. / Kim, J.P. / D'Alessio, C. / Damhs, N.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n1h.cif.gz | 640.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n1h.ent.gz | 551.6 KB | Display | PDB format |
PDBx/mmJSON format | 2n1h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n1h_validation.pdf.gz | 461.8 KB | Display | wwPDB validaton report |
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Full document | 2n1h_full_validation.pdf.gz | 615 KB | Display | |
Data in XML | 2n1h_validation.xml.gz | 35.3 KB | Display | |
Data in CIF | 2n1h_validation.cif.gz | 58.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/2n1h ftp://data.pdbj.org/pub/pdb/validation_reports/n1/2n1h | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
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: 10428.844 Da / Num. of mol.: 1 / Fragment: MRH domain (UNP residues 380-473) / Mutation: W409A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast) Strain: 972 / ATCC 24843 / Gene: gtb1, gls2-beta, SPCC825.02 / Plasmid: pQE / Production host: Escherichia coli (E. coli) / Strain (production host): BL21[pREP4] / References: UniProt: Q9USH8 |
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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: 0.7 mM [U-99% 13C; U-99% 15N] MRH GIIb, 10 mM [U-99% 2H] imidazole, 150 mM sodium chloride, 0.02 % sodium azide, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 7.1 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software | Name: CYANA / Developer: Guntert, P. et al. / Classification: refinement |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 |
NMR constraints | NOE constraints total: 1454 / NOE intraresidue total count: 297 / NOE long range total count: 598 / NOE medium range total count: 194 / NOE sequential total count: 365 / Protein phi angle constraints total count: 52 / Protein psi angle constraints total count: 47 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |