BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27867

Title: chemical shifts assignments of TGIF1-RD2a   PubMed: 31388821

Deposition date: 2019-04-04 Original release date: 2019-05-06

Authors: Nie, Yao; Cai, Cong; Zhu, Jiang; Yang, Yunhuang

Citation: Cai, Cong; Nie, Yao; Yue, Xiali; Zhu, Jiang; Hu, Rui; Liu, Maili; Yang, Yunhuang. "Backbone and side chain resonance assignments of the C-terminal domain of human TGIF1"  Biomol. NMR Assignments 13, 357-360 (2019).

Assembly members:
TGIF1-TD2a, polymer, 122 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
TGIF1-TD2a: GSMGIKNFMPALEETPFHSC TAGPNPTLGRPLSPKPSSPG SVLARPSVICHTTVTALKDV PFSLCQSVGVGQNTDIQQIA AKNFTDTSLMYPEDTCKSGP STNTQSGLFNTPPPTPPDLN QD

Data sets:
Data typeCount
13C chemical shifts463
15N chemical shifts104
1H chemical shifts706

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TGIF2-RD2a monomer1

Entities:

Entity 1, TGIF2-RD2a monomer 122 residues - Formula weight is not available

1   GLYSERMETGLYILELYSASNPHEMETPRO
2   ALALEUGLUGLUTHRPROPHEHISSERCYS
3   THRALAGLYPROASNPROTHRLEUGLYARG
4   PROLEUSERPROLYSPROSERSERPROGLY
5   SERVALLEUALAARGPROSERVALILECYS
6   HISTHRTHRVALTHRALALEULYSASPVAL
7   PROPHESERLEUCYSGLNSERVALGLYVAL
8   GLYGLNASNTHRASPILEGLNGLNILEALA
9   ALALYSASNPHETHRASPTHRSERLEUMET
10   TYRPROGLUASPTHRCYSLYSSERGLYPRO
11   SERTHRASNTHRGLNSERGLYLEUPHEASN
12   THRPROPROPROTHRPROPROASPLEUASN
13   GLNASP

Samples:

sample_1: TGIF1-TD2a, [U-100% 13C; U-100% 15N], 0.5 mM; HEPES 20 mM; NaCl 80 mM; DTT 2 mM; PMSF 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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