BMRB Entry 18592

Name: MRH domain of the Glucosidase II beta subunit from S. pombe
Published: 2013-04-29

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PDB ID: 2lvx
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

MRH domain of the Glucosidase II beta subunit from S. pombe

Deposition date:

2012-07-12

Original release date:

2013-04-29

Authors:

Dahms, N.; Olson, L.; Peterson, F.

Citation:

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).
PubMed: 23609449

Assembly members:

Assembly members:
MRH_domain, polymer, 94 residues, 10544.053 Da.

Natural source:

Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Schizosaccharomyces pombe

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE30-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MRH_domain: YRAIKGMETKREIGGYTYKV VFYENVFQDSILLGNFASQE GNVLKYENGQSCWNGPHRSA IVTVECGVENEIVSVLEAQK CEYLIKMKSPAACS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	361
15N chemical shifts	96
1H chemical shifts	623

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

TYR

THR

TYR

LYS

VAL

3

VAL

PHE

TYR

GLU

ASN

VAL

PHE

GLN

ASP

SER

4

ILE

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

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

PDB	2LVX 4XQM
DBJ	BAA13906
EMBL	CAB58410
REF	NP_588052
SP	Q9USH8
AlphaFold	Q9USH8