BMRB Entry 27399

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27399

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Title:
A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding
Deposition date:
2018-02-08
Original release date:
2018-04-24
Authors:
Stowell, James; Wagstaff, Jane; Hill, Chris; Yu, Minmin; McLaughlin, Stephen; Freund, Stefan; Passmore, Lori
Citation:

Citation: Stowell, James; Wagstaff, Jane; Hill, Chris; Yu, Minmin; McLaughlin, Stephen; Freund, Stefan; Passmore, Lori. "A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding."  J. Biol. Chem. 293, 9210-9222 (2018).
PubMed: 29695507

Assembly members:

Assembly members:
USR+YTH_domain, polymer, 207 residues, Formula weight is not available
19mer_DSR_RNA, polymer, 19 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
USR+YTH_domain: GAYPEKSSYLLSNSSNDSAS RKEKPKARASTPPPLNFSRA SEHRNEKGERISMINPRVVL DENGISHRSRYFIMLCDNET AIAHAKKTSIWAVKKDSSKR ISDAYKKASVYFIFVAQQTY NALGYAQVVSDLNSTELPFW SDSSHAGGVRIKWIKTCNLF SAEISEIVSHMDHGSEARDG MEMMYDEGSRLCTLINYAIM KRIGRDR
19mer_DSR_RNA: CUCUUUAAACCUAAAAAGC

Data sets:
Data typeCount
13C chemical shifts440
15N chemical shifts138
1H chemical shifts138

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USR+YTH domain1
2RNA2

Entities:

Entity 1, USR+YTH domain 207 residues - Formula weight is not available

1   GLYALATYRPROGLULYSSERSERTYRLEU
2   LEUSERASNSERSERASNASPSERALASER
3   ARGLYSGLULYSPROLYSALAARGALASER
4   THRPROPROPROLEUASNPHESERARGALA
5   SERGLUHISARGASNGLULYSGLYGLUARG
6   ILESERMETILEASNPROARGVALVALLEU
7   ASPGLUASNGLYILESERHISARGSERARG
8   TYRPHEILEMETLEUCYSASPASNGLUTHR
9   ALAILEALAHISALALYSLYSTHRSERILE
10   TRPALAVALLYSLYSASPSERSERLYSARG
11   ILESERASPALATYRLYSLYSALASERVAL
12   TYRPHEILEPHEVALALAGLNGLNTHRTYR
13   ASNALALEUGLYTYRALAGLNVALVALSER
14   ASPLEUASNSERTHRGLULEUPROPHETRP
15   SERASPSERSERHISALAGLYGLYVALARG
16   ILELYSTRPILELYSTHRCYSASNLEUPHE
17   SERALAGLUILESERGLUILEVALSERHIS
18   METASPHISGLYSERGLUALAARGASPGLY
19   METGLUMETMETTYRASPGLUGLYSERARG
20   LEUCYSTHRLEUILEASNTYRALAILEMET
21   LYSARGILEGLYARGASPARG

Entity 2, RNA 19 residues - Formula weight is not available

1   CUCUUUAAAC
2   CUAAAAAGC

Samples:

sample_1: USR+YTH domain with RNA, [U-100% 13C; U-100% 15N; U-80% 2H], 200 uM; 19mer DSR RNA 200 uM; D2O, [U-100% 2H], 5%; sodium chloride 150 mM; PIPES 20 mM

sample_conditions_1: ionic strength: 170 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N-1H BEST_TROSYsample_1isotropicsample_conditions_1
3D trHNCOsample_1isotropicsample_conditions_1
3D trHNCACOsample_1isotropicsample_conditions_1
3D trHNCAsample_1isotropicsample_conditions_1
3D trHNCOCAsample_1isotropicsample_conditions_1
3D trHNCOCACBsample_1isotropicsample_conditions_1
3D trHNCACBsample_1isotropicsample_conditions_1
3D trHNCANNHsample_1isotropicsample_conditions_1
3D trHNCOCANNHsample_1isotropicsample_conditions_1

Software:

Topspin_3.1, Bruker Biospin - collection

qMDD, Kazimierczuk and Orekhov - processing

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

Sparky, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

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