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Biological Magnetic Resonance Data Bank


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BMRB Entry 25720

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25720
MolProbity Validation Chart

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Title: Regnase-1 C-terminal domain   PubMed: 26927947

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: 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).

Assembly members:
entity, polymer, 57 residues, 6383.458 Da.

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

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

Entity Sequences (FASTA):
entity: GPHMGDLAKERAGVYTKLCG VFPPHLVEAVMRRFPQLLDP QQLAAEILSYKSQHLSE

Data sets:
Data typeCount
13C chemical shifts268
15N chemical shifts58
1H chemical shifts418

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 57 residues - 6383.458 Da.

1   GLYPROHISMETGLYASPLEUALALYSGLU
2   ARGALAGLYVALTYRTHRLYSLEUCYSGLY
3   VALPHEPROPROHISLEUVALGLUALAVAL
4   METARGARGPHEPROGLNLEULEUASPPRO
5   GLNGLNLEUALAALAGLUILELEUSERTYR
6   LYSSERGLNHISLEUSERGLU

Samples:

sample_1: Reg1_CTD, [U-99% 13C; U-99% 15N], 2.3 mM; DSS 10 % v/v; D2O, [U-2H], 20 uL; 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
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (HCA)CO(CA)NHsample_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 HNCACBsample_1isotropicsample_conditions_1
2D HbCbCgCdHdsample_1isotropicsample_conditions_1
2D HbCbCgCdCeHesample_1isotropicsample_conditions_1
3D HCCH-TOCSY Aliphaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSY 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, JC Hoch and AS Sterm - processing

NMR spectrometers:

  • Agilent INOVA 600 MHz

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