BMRB Entry 50522

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50522

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Title:
NMR assignment of Fc fragment of mouse immunoglobulin G2b glycoprotein galactosylated (G2) glycoform
Deposition date:
2020-10-19
Original release date:
2021-06-30
Authors:
Yanaka, Saeko; Yamaguchi, Yoshiki; Takizawa, Takeshi; Miyanoiri, Yohie; Yogo, Rina; Shimada, Ichio; Kato, Koichi
Citation:

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).
PubMed: 33423189

Assembly members:

Assembly members:
entity_1, polymer, 219 residues, Formula weight is not available
entity_2, polymer, 10 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: purified from the natural source

Entity Sequences (FASTA):

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 shifts64
15N chemical shifts202
1H chemical shifts260

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fc fragment of mouse immunoglobulin G2b glycoprotein galactosylated, 11
2Fc fragment of mouse immunoglobulin G2b glycoprotein galactosylated, 21
3(G2) glycoform, 12
4(G2) glycoform, 22

Entities:

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

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, (G2) glycoform, 1 10 residues - Formula weight is not available

The structure is illustrated in the manuscript

1   NAGNAGMANMANNAGGMANNAGFUCG

Samples:

sample_1: Fc fragment of mouse immunoglobulin G2b glycoprotein non-galactosylated, [U-13C; U-15N], 10 mg/mL; (G2) 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; 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 HCCH COSYsample_1isotropicsample_conditions_1
2D HCA(CO)sample_1isotropicsample_conditions_1
2D H(CA)COsample_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 peaks
SPARKY: Backbone or all simulated peaks