BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 50002

Title: Pof8 RNA recognition motif 2   PubMed: 33131423

Deposition date: 2019-08-18 Original release date: 2021-08-13

Authors: Eichhorn, Catherine; Feigon, Juli

Citation: Basu, Ritwika; Eichhorn, Catherine; Cheng, Ryan; Peterson, Robert; Feigon, Juli. "Structure of S. pombe telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins"  RNA Biol. 18, 1181-1192 (2021).

Assembly members:
entity_1, polymer, 121 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
entity_1: KDEDNLDFTKNLLTRIKNLH PLTNKSTIHSLLSYVFSRQT QNIACEPMYIDYRKDETEAI IRWKTPLHAETCINAFRTQE RKQNSHDDIRAHRKKGSSRP FLIAELITGEEEKNYWRMLK K

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts106
1H chemical shifts131

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Pof8 C-terminal xRRM1

Entities:

Entity 1, Pof8 C-terminal xRRM 121 residues - Formula weight is not available

1   LYSASPGLUASPASNLEUASPPHETHRLYS
2   ASNLEULEUTHRARGILELYSASNLEUHIS
3   PROLEUTHRASNLYSSERTHRILEHISSER
4   LEULEUSERTYRVALPHESERARGGLNTHR
5   GLNASNILEALACYSGLUPROMETTYRILE
6   ASPTYRARGLYSASPGLUTHRGLUALAILE
7   ILEARGTRPLYSTHRPROLEUHISALAGLU
8   THRCYSILEASNALAPHEARGTHRGLNGLU
9   ARGLYSGLNASNSERHISASPASPILEARG
10   ALAHISARGLYSLYSGLYSERSERARGPRO
11   PHELEUILEALAGLULEUILETHRGLYGLU
12   GLUGLULYSASNTYRTRPARGMETLEULYS
13   LYS

Samples:

sample_1: Pof8 C-terminal xRRM, [U-13C; U-15N], 0.8 mM; sodium phosphate 20 mM; potassium chloride 50 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
15N-(1H) NOEsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - collection

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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 800 MHz

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