BMRB Entry 36185

Name: Solution structure of RRM domian of La protein from Trypanosoma brucei
Published: 2019-05-13

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PDB ID: 5zuh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36185
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of RRM domian of La protein from Trypanosoma brucei

Deposition date:

2018-05-07

Original release date:

2019-05-13

Authors:

Shan, F.

Citation:

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" FEBS J. 286, 3129-3147 (2019).
PubMed: 30993866

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	195
15N chemical shifts	91
1H chemical shifts	611

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 99 residues - 11282.726 Da.

1

THR

ASP

HIS

GLN

THR

VAL

TYR

VAL

LYS

PRO

2

VAL

PRO

THR

ALA

THR

LEU

GLU

GLN

LEU

3

THR

GLU

PHE

SER

LYS

HIS

GLY

THR

VAL

4

GLN

ALA

VAL

TRP

ARG

TYR

PHE

ALA

GLY

5

LYS

ASP

ALA

PRO

GLU

SER

ARG

THR

6

LYS

PRO

SER

VAL

PHE

VAL

PHE

ASN

SER

7

SER

GLU

ALA

GLU

ALA

PHE

GLN

LYS

ALA

8

PRO

MET

TYR

ASP

VAL

GLN

LEU

THR

9

ALA

GLU

MET

LYS

THR

TYR

LEU

GLU

ARG

10

LYS

ALA

GLU

ILE

ALA

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D NOESY	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks