BMRB Entry 18592
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18592
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Title: MRH domain of the Glucosidase II beta subunit from S. pombe PubMed: 23609449
Deposition date: 2012-07-12 Original release date: 2013-04-29
Authors: Dahms, N.; Olson, L.; Peterson, F.
Citation: Olson, Linda; Orsi, Ramiro; Alculumbre, Solana; Peterson, Francis; Stigliano, Ivan; Parodi, Armando; Dahms, Cecilia. "Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum." J. Biol. Chem. 288, 16460-16475 (2013).
Assembly members:
MRH_domain, polymer, 94 residues, 10544.053 Da.
Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MRH_domain: YRAIKGMETKREIGGYTYKV
VFYENVFQDSILLGNFASQE
GNVLKYENGQSCWNGPHRSA
IVTVECGVENEIVSVLEAQK
CEYLIKMKSPAACS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 361 |
15N chemical shifts | 96 |
1H chemical shifts | 623 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MRH domain | 1 |
Entities:
Entity 1, MRH domain 94 residues - 10544.053 Da.
1 | TYR | ARG | ALA | ILE | LYS | GLY | MET | GLU | THR | LYS | ||||
2 | ARG | GLU | ILE | GLY | GLY | TYR | THR | TYR | LYS | VAL | ||||
3 | VAL | PHE | TYR | GLU | ASN | VAL | PHE | GLN | ASP | SER | ||||
4 | ILE | LEU | LEU | GLY | ASN | PHE | ALA | SER | GLN | GLU | ||||
5 | GLY | ASN | VAL | LEU | LYS | TYR | GLU | ASN | GLY | GLN | ||||
6 | SER | CYS | TRP | ASN | GLY | PRO | HIS | ARG | SER | ALA | ||||
7 | ILE | VAL | THR | VAL | GLU | CYS | GLY | VAL | GLU | ASN | ||||
8 | GLU | ILE | VAL | SER | VAL | LEU | GLU | ALA | GLN | LYS | ||||
9 | CYS | GLU | TYR | LEU | ILE | LYS | MET | LYS | SER | PRO | ||||
10 | ALA | ALA | CYS | SER |
Samples:
sample_1: imidazole, [U-100% 2H], 10 mM; sodium chloride 150 mM; H2O 95%; D2O, [U-99% 2H], 5%
sample_conditions_1: ionic strength: 150 mM; pH: 7.1; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
3D_13C-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
3D_13C-separated_NOESY (AROMATIC) | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
TOPSPIN v2.1, Bruker - collection
NMRPipe v2009, Delagio,F. et al. - processing
XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis
GARANT v2.1, C. Bartels - data analysis
CYANA v2.1, Guntert, P. - structural calculation
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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