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 50515

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50515

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Title: NMR assignments of the Fc fragment of mouse immunoglobulin G2b glycoprotein non-galactosylated (G0) glycoform   PubMed: 33423189

Deposition date: 2020-10-19 Original release date: 2021-06-30

Authors: Yanaka, Saeko; Yamaguchi, Yoshiki; Takizawa, Takeshi; Miyanoiri, Yohei; Yogo, Rina; Shimada, Ichio; Kato, Koichi

Citation: Yanaka, Saeko; Yamaguchi, Yoshiki; Takizawa, Takeshi; Miyanoiri, Yohei; Yogo, Rina; Shimada, Ichio; Kato, Koichi. "NMR assignments of the N-glycans of the Fc fragment of mouse immunoglobulin G2b glycoprotein."  Biomol. NMR Assign. 15, 187-192 (2021).

Assembly members:
entity_1, polymer, 219 residues, Formula weight is not available
entity_2, polymer, 8 residues, Formula weight is not available

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

Experimental source:   Production method: purified from the natural source

Entity Sequences (FASTA):
entity_1: CPAPNLEGGPSVFIFPPNIK DVLMISLTPKVTCVVVDVSE DDPDVQISWFVNNVEVHTAQ TQTHREDYNSTIRVVSTLPI QHQDWMSGKEFKCKVNNKDL PSPIERTISKIKGLVRAPQV YILPPPAEQLSRKDVSLTCL VVGFNPGDISVEWTSNGHTE ENYKDTAPVLDSDGSYFIYS KLNMKTSKWEKTDSFSCNVR HEGLKNYYLKKTISRSPGK
entity_2: XXXXXXXX

Data sets:
Data typeCount
13C chemical shifts53
15N chemical shifts202
1H chemical shifts250

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fc fragment of mouse immunoglobulin G2b glycoprotein non-galactosylated, 11
2Fc fragment of mouse immunoglobulin G2b glycoprotein non-galactosylated, 21
3(G0) glycoform, 12
4(G0) glycoform, 22

Entities:

Entity 1, Fc fragment of mouse immunoglobulin G2b glycoprotein non-galactosylated, 1 219 residues - Formula weight is not available

The structure is illustrated in the manuscript

1   CYSPROALAPROASNLEUGLUGLYGLYPRO
2   SERVALPHEILEPHEPROPROASNILELYS
3   ASPVALLEUMETILESERLEUTHRPROLYS
4   VALTHRCYSVALVALVALASPVALSERGLU
5   ASPASPPROASPVALGLNILESERTRPPHE
6   VALASNASNVALGLUVALHISTHRALAGLN
7   THRGLNTHRHISARGGLUASPTYRASNSER
8   THRILEARGVALVALSERTHRLEUPROILE
9   GLNHISGLNASPTRPMETSERGLYLYSGLU
10   PHELYSCYSLYSVALASNASNLYSASPLEU
11   PROSERPROILEGLUARGTHRILESERLYS
12   ILELYSGLYLEUVALARGALAPROGLNVAL
13   TYRILELEUPROPROPROALAGLUGLNLEU
14   SERARGLYSASPVALSERLEUTHRCYSLEU
15   VALVALGLYPHEASNPROGLYASPILESER
16   VALGLUTRPTHRSERASNGLYHISTHRGLU
17   GLUASNTYRLYSASPTHRALAPROVALLEU
18   ASPSERASPGLYSERTYRPHEILETYRSER
19   LYSLEUASNMETLYSTHRSERLYSTRPGLU
20   LYSTHRASPSERPHESERCYSASNVALARG
21   HISGLUGLYLEULYSASNTYRTYRLEULYS
22   LYSTHRILESERARGSERPROGLYLYS

Entity 2, (G0) glycoform, 1 8 residues - Formula weight is not available

The structure is illustrated in the manuscript

1   NAGNAGMANMANNAGMANNAGFUC

Samples:

sample_1: Fc fragment of mouse immunoglobulin G2b glycoprotein non-galactosylated, [U-13C; U-15N], 10 mg/mL; (G0) glycoform, [U-13C; U-15N], 10 mg/mL; sodium phosphate buffer 5 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 325 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D HSQC-TOCSYsample_1isotropicsample_conditions_1
2D HCCH-COSYsample_1isotropicsample_conditions_1
2D H(CA)COsample_1isotropicsample_conditions_1
2D HCA(CO)sample_1isotropicsample_conditions_1

Software:

TOPSPIN, SPARKY - chemical shift assignment, collection

NMR spectrometers:

  • Bruker DRX 400 MHz
  • Bruker DRX 600 MHz
  • Bruker AVANCE 800 MHz
  • Bruker AVANCEIII 950 MHz

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