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 36185

Title: Solution structure of RRM domian of La protein from Trypanosoma brucei   PubMed: 30993866

Deposition date: 2018-05-07 Original release date: 2019-05-13

Authors: Shan, F.

Citation: Shan, Fangzhen; Mei, Song; Zhang, Jiahai; Zhang, Xuecheng; Xu, Chao; Liao, Shanhui; Tu, Xiaoming. "A telomerase subunit homolog La protein from Trypanosoma brucei plays an essential role in ribosomal biogenesis"  .

Assembly members:
RNA binding protein La-like protein, polymer, 99 residues, 11282.726 Da.

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

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

Entity Sequences (FASTA):
RNA binding protein La-like protein: TDHQTVYVKPVPPTATLEQL TEFFSKHGTVQAVWRRYFAG KKDAPPESRTKPSVFVVFNS SEEAEAFQKAPPMYDDVQLT AEMKTTYLERKAEEIAAKK

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts91
1H chemical shifts611

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 99 residues - 11282.726 Da.

1   THRASPHISGLNTHRVALTYRVALLYSPRO
2   VALPROPROTHRALATHRLEUGLUGLNLEU
3   THRGLUPHEPHESERLYSHISGLYTHRVAL
4   GLNALAVALTRPARGARGTYRPHEALAGLY
5   LYSLYSASPALAPROPROGLUSERARGTHR
6   LYSPROSERVALPHEVALVALPHEASNSER
7   SERGLUGLUALAGLUALAPHEGLNLYSALA
8   PROPROMETTYRASPASPVALGLNLEUTHR
9   ALAGLUMETLYSTHRTHRTYRLEUGLUARG
10   LYSALAGLUGLUILEALAALALYSLYS

Samples:

sample_1: RRM, [U-13C; U-15N], 0.5 mM; DTT 2 mM; EDTA 2 mM; sodium chloride 200 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DMX 600 MHz

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