BMRB Entry 15545

Title:
1H 13C and 15N chemical shift for the human FLN29
Deposition date:
2007-11-05
Original release date:
2008-01-17
Authors:
Sauve, Simon; Gingras, Genevieve; Aubin, Remy; Hodgson, Derek; Aubin, Yves
Citation:

Citation: Sauve, Simon; Gingras, Genevieve; Aubin, Remy; Hodgson, Derek; Aubin, Yves. "NMR assignment of the N-terminal TRAF-like RING zinc finger domain of human FLN29"  Biomol. NMR Assignments 2, 33-36 (2008).
PubMed: 19636918

Assembly members:

Assembly members:
FLN29, polymer, 141 residues, 16218.7 Da.
ZN, non-polymer, 65.409 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   Vector: pet15b10

Data sets:
Data typeCount
13C chemical shifts544
15N chemical shifts136
1H chemical shifts635

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FLN291
2Zinc ion, 12
3Zinc ion, 22
4Zinc ion, 32
5Zinc ion, 42

Entities:

Entity 1, FLN29 141 residues - 16218.7 Da.

The glycine residue in position 1 results from the TEV protease cleavage of the Histidine tag and is not part of the native N-terminal FLN29 sequence

1   GLYMETALAGLUPHELEUASPASPGLNGLU
2   THRARGLEUCYSASPASNCYSLYSLYSGLU
3   ILEPROVALPHEASNPHETHRILEHISGLU
4   ILEHISCYSGLNARGASNILEGLYMETCYS
5   PROTHRCYSLYSGLUPROPHEPROLYSSER
6   ASPMETGLUTHRHISMETALAALAGLUHIS
7   CYSGLNVALTHRCYSLYSCYSASNLYSLYS
8   LEUGLULYSARGLEULEULYSLYSHISGLU
9   GLUTHRGLUCYSPROLEUARGLEUALAVAL
10   CYSGLNHISCYSASPLEUGLULEUSERILE
11   LEULYSLEULYSGLUHISGLUASPTYRCYS
12   GLYALAARGTHRGLULEUCYSGLYASNCYS
13   GLYARGASNVALLEUVALLYSASPLEULYS
14   THRHISPROGLUVALCYSGLYARGGLUGLY
15   GLU

Entity 2, Zinc ion, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: FLN29, [U-99% 13C; U-99% 15N], 200 uM; sodium phosphate 20 mM; zinc chloride 50 uM; DTT 1 mM; D2O 5%

sample_2: FLN29, [U-100% 13C; U-100% 15N], 400 uM; sodium phosphate 20 mM; zinc chloride 50 uM; DTT 1 mM; D2O 5%

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D C(CO)NH-TOCSYsample_2isotropicsample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v7.0.16, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

Smartnotebook v5.0.6, Brian Sykes Laboratory - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance III 600 MHz

Related Database Links:

DBJ BAA22541 BAE00351 BAF84020 BAI46493
GB AAH03553 ABM83456 ABM86667 AIC50745 EAW97995
REF NP_001137378 NP_001253436 NP_001271978 NP_006691 XP_002753069
SP O14545 Q4R970
AlphaFold O14545 Q4R970

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