BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18592

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

Data sets:
Data typeCount
13C chemical shifts361
15N chemical shifts96
1H chemical shifts623

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MRH domain1

Entities:

Entity 1, MRH domain 94 residues - 10544.053 Da.

1   TYRARGALAILELYSGLYMETGLUTHRLYS
2   ARGGLUILEGLYGLYTYRTHRTYRLYSVAL
3   VALPHETYRGLUASNVALPHEGLNASPSER
4   ILELEULEUGLYASNPHEALASERGLNGLU
5   GLYASNVALLEULYSTYRGLUASNGLYGLN
6   SERCYSTRPASNGLYPROHISARGSERALA
7   ILEVALTHRVALGLUCYSGLYVALGLUASN
8   GLUILEVALSERVALLEUGLUALAGLNLYS
9   CYSGLUTYRLEUILELYSMETLYSSERPRO
10   ALAALACYSSER

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:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_1isotropicsample_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

Related Database Links:

PDB
DBJ BAA13906
EMBL CAB58410
REF NP_588052
SP Q9USH8

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts