BMRB Entry 26912

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26912

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Title:
Chemical shift assignments of the first and second RRMs of Nrd1, a fission yeast MAPK target RNA binding protein
Deposition date:
2016-09-29
Original release date:
2017-04-26
Authors:
Kobayashi, Ayaho; Kanaba, Teppei; Mishima, Masaki
Citation:

Citation: Kobayashi, Ayaho; Kanaba, Teppei; Satoh, Ryosuke; Ito, Yutaka; Sugiura, Reiko; Mishima, Masaki. "Chemical shift assignments of the first and second RRMs of Nrd1, a fission yeast MAPK-target RNA binding protein"  Biomol. NMR Assignments 11, 123-126 (2017).
PubMed: 28284018

Assembly members:

Assembly members:
Nrd1, polymer, 177 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: fission yeast   Taxonomy ID: 4896   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Schizosaccharomyces pombe

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSF-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nrd1: NNTTQPVKTVYVGNLPPNTP IDEILSCVRTGPIESAWILP EKNCAFISFLDPSHATAFFQ DAALKRLTIRGTEVKVGWGK NSASNSSVLLAVQQSGACRN VFLGNLPNGITEDEIREDLE PFGPIDQIKIVTERNIAFVH FLNIAAAIKAVQELPLNPKW SKRRIYYGRDRCAVGLK

Data sets:
Data typeCount
13C chemical shifts625
15N chemical shifts138
1H chemical shifts910

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nrd1, chain 11
2Nrd1, chain 21

Entities:

Entity 1, Nrd1, chain 1 177 residues - Formula weight is not available

1   ASNASNTHRTHRGLNPROVALLYSTHRVAL
2   TYRVALGLYASNLEUPROPROASNTHRPRO
3   ILEASPGLUILELEUSERCYSVALARGTHR
4   GLYPROILEGLUSERALATRPILELEUPRO
5   GLULYSASNCYSALAPHEILESERPHELEU
6   ASPPROSERHISALATHRALAPHEPHEGLN
7   ASPALAALALEULYSARGLEUTHRILEARG
8   GLYTHRGLUVALLYSVALGLYTRPGLYLYS
9   ASNSERALASERASNSERSERVALLEULEU
10   ALAVALGLNGLNSERGLYALACYSARGASN
11   VALPHELEUGLYASNLEUPROASNGLYILE
12   THRGLUASPGLUILEARGGLUASPLEUGLU
13   PROPHEGLYPROILEASPGLNILELYSILE
14   VALTHRGLUARGASNILEALAPHEVALHIS
15   PHELEUASNILEALAALAALAILELYSALA
16   VALGLNGLULEUPROLEUASNPROLYSTRP
17   SERLYSARGARGILETYRTYRGLYARGASP
18   ARGCYSALAVALGLYLEULYS

Samples:

sample_1: Nrd1, [U-98% 13C; U-98% 15N], 0.85 mM; potassium phosphate 50 mM; potassium chloride 100 mM; TCEP 1 mM; EDTA 0.1 mM

sample_2: Nrd1, [U-98% 13C; U-98% 15N], 0.9 mM; potassium phosphate 50 mM; potassium chloride 100 mM; TCEP 1 mM; EDTA 0.1 mM

sample_3: Nrd1, [U-98% 15N], 1.2 mM; potassium phosphate 50 mM; potassium chloride 100 mM; TCEP 1 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
4D HCCONHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

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