BMRB Entry 25718

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25718
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Regnase-1 N-terminal domain
Deposition date:
2015-07-18
Original release date:
2016-03-14
Authors:
Yokogawa, Mariko; Tsushima, Takashi; Noda, Nobuo; Kumeta, Hiroyuki; Adachi, Wakana; Enokizono, Yoshiaki; Yamashita, Kazuo; Standley, Daron; Takeuchi, Osamu; Akira, Shizuo; Inagaki, Fuyuhiko
Citation:

Citation: Yokogawa, Mariko; Tsushima, Takashi; Noda, Nobuo; Kumeta, Hiroyuki; Adachi, Wakana; Enokizono, Yoshiaki; Yamashita, Kazuo; Standley, Daron; Takeuchi, Osamu; Akira, Shizuo; Inagaki, Fuyuhiko. "Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions"  Sci. Rep. 6, 22324-22324 (2016).
PubMed: 26927947

Assembly members:

Assembly members:
Reg1_NTD, polymer, 49 residues, 5422.245 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6p

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Reg1_NTD: GPHMTSELQMKVDFFRKLGY SSSEIHSVLQKLGVQADTNT VLGELVKHG

Data sets:
Data typeCount
13C chemical shifts214
15N chemical shifts50
1H chemical shifts336

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 49 residues - 5422.245 Da.

1   GLYPROHISMETTHRSERGLULEUGLNMET
2   LYSVALASPPHEPHEARGLYSLEUGLYTYR
3   SERSERSERGLUILEHISSERVALLEUGLN
4   LYSLEUGLYVALGLNALAASPTHRASNTHR
5   VALLEUGLYGLULEUVALLYSHISGLY

Samples:

sample_1: Reg1_NTD, [U-99% 13C; U-99% 15N], 1.1 mM; DSS 5 ug; D2O, [U-2H], 10 % v/v; HEPES 20 mM; sodium chloride 150 mM; H2O 90 % v/v

sample_conditions_1: ionic strength: 170 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)HAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Olivia, Masashi Yokochi - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

rnmrtk vv.3, JC Hoch and AS Sterm - processing

NMR spectrometers:

  • Agilent INOVA 800 MHz
  • Agilent INOVA 600 MHz
  • Agilent INOVA 600 MHz

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