BMRB Entry 34219

Title:
Solution structure of the MRH domain of Yos9 complexed with alpha3,alpha6-Man5
Deposition date:
2017-12-14
Original release date:
2019-01-28
Authors:
Kniss, A.; Kazemi, S.; Lohr, F.; Guntert, P.; Dotsch, V.
Citation:

Citation: Kniss, Andreas; Kazemi, Sina; Lohr, Frank; Berger, Maren; Rogov, Vladimir; Guntert, Peter; Sommer, Thomas; Jarosch, Ernst; Dotsch, Volker. "Structural investigation of glycan recognition by the ERAD quality control lectin Yos9"  J. Biomol. NMR 72, 1-10 (2018).
PubMed: 30066206

Assembly members:

Assembly members:
entity_1, polymer, 162 residues, 18328.627 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data typeCount
13C chemical shifts676
15N chemical shifts148
1H chemical shifts1067

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 162 residues - 18328.627 Da.

1   GLYALASERASNSERGLULYSTHRALALEU
2   LEUTHRLYSTHRLEUASNGLNGLYVALLYS
3   THRILEPHEASPLYSLEUASNGLUARGCYS
4   ILEPHETYRGLNALAGLYPHETRPILETYR
5   GLUTYRCYSPROGLYILEGLUPHEVALGLN
6   PHEHISGLYARGVALASNTHRLYSTHRGLY
7   GLUILEVALASNARGASPGLUSERLEUVAL
8   TYRARGLEUGLYLYSPROLYSALAASNVAL
9   GLUGLUARGGLUPHEGLULEULEUTYRASP
10   ASPVALGLYTYRTYRILESERGLUILEILE
11   GLYSERGLYASPILECYSASPVALTHRGLY
12   ALAGLUARGMETVALGLUILEGLNTYRVAL
13   CYSGLYGLYSERASNSERGLYPROSERTHR
14   ILEGLNTRPVALARGGLUTHRLYSILECYS
15   VALTYRGLUALAGLNVALTHRILEPROGLU
16   LEUCYSASNLEUGLULEULEUALALYSASN
17   GLUASP

Samples:

sample_1: MRH domain of Yos9, [U-98% 13C; U-98% 15N], 0.55 mM; alpha3,alpha6-Man5 8.25 mM

sample_2: MRH domain of Yos9, [U-98% 13C; U-98% 15N], 1 mM; alpha3,alpha6-Man5 15 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H TOCSYsample_1isotropicsample_conditions_1
3D 13C TOCSYsample_1isotropicsample_conditions_1
2D(HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (H)CB(CGCC)H TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.13, Goddard - chemical shift assignment

CYANA v3.9, Guntert, P. - structure calculation

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks