BMRB Entry 51797

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51797

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Title:
Backbone assignment of the extended C-terminal domain of Tetrahymena telomerase protein p65
Deposition date:
2023-01-23
Original release date:
2023-06-19
Authors:
Yang, Yuan; Eichhorn, Catherine; Jiang, Yi Xiao; Wang, Yaqiang; Feigon, Juli
Citation:

Citation: Wang, Yaqiang; He, Yao; Wang, Yanjiao; Yang, Yuan; Singh, Mahavir; Eichhorn, Catherine; Cheng, Xinyi; Jiang, Yi Xiao; Zhou, Z. Hong; Feigon, Juli. "Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR"  J. Mol. Biol. 435, 168044-168044 (2023).
PubMed: 37330293

Assembly members:

Assembly members:
entity_1, polymer, 169 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Tetrahymena Thermophila   Taxonomy ID: 5911   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Tetrahymena Thermophila

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GQKNKNMNQSRKASDEFVSI DVEIKQNCLIKIINIPQGTL KAEVVLAVRHLGYEFYCDYI DENSNQINSNLIQQDQHPQL NDLLKEGQAMIRFQNSDEQR LAIQKLLNHNNNKLQIEIRG QICDVISTIPEDEEKNYWNY IKFKKNEFRKFFFMKKQQKK QNITQNYNK

Data sets:
Data typeCount
13C chemical shifts212
15N chemical shifts124
1H chemical shifts124

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1p65-aL-xRRM21

Entities:

Entity 1, p65-aL-xRRM2 169 residues - Formula weight is not available

The first amino acid, 352 Glycine, is a non-native residue resulted from TEV protease cleavage site. There is a loop truncation between amino acids 420 and 443.

1   GLYGLNLYSASNLYSASNMETASNGLNSER
2   ARGLYSALASERASPGLUPHEVALSERILE
3   ASPVALGLUILELYSGLNASNCYSLEUILE
4   LYSILEILEASNILEPROGLNGLYTHRLEU
5   LYSALAGLUVALVALLEUALAVALARGHIS
6   LEUGLYTYRGLUPHETYRCYSASPTYRILE
7   ASPGLUASNSERASNGLNILEASNSERASN
8   LEUILEGLNGLNASPGLNHISPROGLNLEU
9   ASNASPLEULEULYSGLUGLYGLNALAMET
10   ILEARGPHEGLNASNSERASPGLUGLNARG
11   LEUALAILEGLNLYSLEULEUASNHISASN
12   ASNASNLYSLEUGLNILEGLUILEARGGLY
13   GLNILECYSASPVALILESERTHRILEPRO
14   GLUASPGLUGLULYSASNTYRTRPASNTYR
15   ILELYSPHELYSLYSASNGLUPHEARGLYS
16   PHEPHEPHEMETLYSLYSGLNGLNLYSLYS
17   GLNASNILETHRGLNASNTYRASNLYS

Samples:

sample_1: extended C-terminal domain of Tetrahymena telomerase protein p65, [U-98% 13C; U-98% 15N], 0.8 mM; H2O 95%; D2O, [U-100% 2H], 5%; sodium phosphate 20 mM; potassium chloride 50 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 80 mM; pH: 6.1; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN vv3.5pl7 - collection

NMRPipe - processing

NMRFAM-SPARKY vv1.470 - data analysis

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz

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