BMRB Entry 36324

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36324

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Title:
Solution structure of disulfide bond mutaion of the core domain of Fibroblast growth factor 21 (FGF21)
Deposition date:
2020-03-14
Original release date:
2025-10-13
Authors:
Zhu, L.; Zhao, H.; Wang, J.
Citation:

Citation: Zhu, Lei; Zhao, Hongxin; Liu, Juanjuan; Cai, Hao; Wu, Bo; Liu, Zhijun; Zhou, Shu; Liu, Qingsong; Li, Xiaokun; Bao, Bin; Liu, Jian; Dai, Han; Wang, Junfeng. "Dynamic folding modulation generates FGF21 variant against diabetes."  EMBO Rep. 22, e51352-e51352 (2021).
PubMed: 33295692

Assembly members:

Assembly members:
Fibroblast growth factor 21, polymer, 129 residues, 14103.977 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Fibroblast growth factor 21: GQVRQRYLYTSGPHGLSSCH LEIREDGTVGCAADQSPESL LQLKALKPGVIQILGVKTSR FLCQRPDGALYGSLHFDPEA CSFRELLLEDGYNVYQSEAH GLPLHLPGNKSPHRDPAPRG PARFLPLPG

Data sets:
Data typeCount
13C chemical shifts442
15N chemical shifts114
1H chemical shifts753

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 129 residues - 14103.977 Da.

1   GLYGLNVALARGGLNARGTYRLEUTYRTHR
2   SERGLYPROHISGLYLEUSERSERCYSHIS
3   LEUGLUILEARGGLUASPGLYTHRVALGLY
4   CYSALAALAASPGLNSERPROGLUSERLEU
5   LEUGLNLEULYSALALEULYSPROGLYVAL
6   ILEGLNILELEUGLYVALLYSTHRSERARG
7   PHELEUCYSGLNARGPROASPGLYALALEU
8   TYRGLYSERLEUHISPHEASPPROGLUALA
9   CYSSERPHEARGGLULEULEULEUGLUASP
10   GLYTYRASNVALTYRGLNSERGLUALAHIS
11   GLYLEUPROLEUHISLEUPROGLYASNLYS
12   SERPROHISARGASPPROALAPROARGGLY
13   PROALAARGPHELEUPROLEUPROGLY

Samples:

sample_1: FGF21SS, [U-99% 15N], 0.5 mM; sodium azide 0.2 % w/v; sodium chloride 100 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: FGF21SS, [U-99% 13C; U-99% 15N], 0.5 mM; sodium azide 0.2 % w/v; sodium chloride 100 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: FGF21SS, [U-99% 13C; U-99% 15N], 0.5 mM; sodium azide 0.2 % w/v; sodium chloride 100 mM; sodium phosphate 20 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 160 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

CcpNmr Analysis, CCPN - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 850 MHz

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