BMRB Entry 27238

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for S-nitrosylated mouse galectin-2
Deposition date:
2017-08-29
Original release date:
2018-02-08
Authors:
Sakakura, Masayoshi; Tamura, Mayumi; Takeuchi, Tomoharu; Hatanaka, Tomomi; Arata, Yoichiro; Takahashi, Hideo
Citation:

Citation: Sakakura, Masayoshi; Tamura, Mayumi; Fujii, Norihiko; Takeuchi, Tomoharu; Hatanaka, Tomomi; Kishimoto, Seishi; Arata, Yoichiro; Takahashi, Hideo. "Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR"  FEBS J. 285, 1129-1145 (2018).
PubMed: 29392834

Assembly members:

Assembly members:
NO-mGal-2, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts122
1H chemical shifts122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protomer, NO-mGal-2 chain 11
2protomer, NO-mGal-2 chain 21

Entities:

Entity 1, protomer, NO-mGal-2 chain 1 130 residues - Formula weight is not available

1   METSERGLULYSPHEGLUVALLYSASPLEU
2   ASNMETLYSPROGLYMETSERLEULYSILE
3   LYSGLYLYSILEHISASNASPVALASPARG
4   PHELEUILEASNLEUGLYGLNGLYLYSGLU
5   THRLEUASNLEUHISPHEASNPROARGPHE
6   ASPGLUSERTHRILEVALCYSASNTHRSER
7   GLUGLYGLYARGTRPGLYGLNGLUGLNARG
8   GLUASNHISMETCYSPHESERPROGLYSER
9   GLUVALLYSILETHRILETHRPHEGLNASP
10   LYSASPPHELYSVALTHRLEUPROASPGLY
11   HISGLNLEUTHRPHEPROASNARGLEUGLY
12   HISASNGLNLEUHISTYRLEUSERMETGLY
13   GLYLEUGLNILESERSERPHELYSLEUGLU

Samples:

sample_1: NO-mGal-2, [U-99% 13C; U-98% 15N], 0.8 mM; MES 10 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

MddNMR, Orekhov - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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