BMRB Entry 18621

Name: NMR Chemical Shift Assignments of N terminal La motif domain of La protein
Published: 2013-02-14

Click here to enlarge.

PDB ID: 2m5w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18621
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR Chemical Shift Assignments of N terminal La motif domain of La protein

Deposition date:

2012-07-27

Original release date:

2013-02-14

Authors:

Bouras, Georgios; Argyriou, Aikaterini; Apostolidi, Maria; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios

Citation:

Citation: Apostolidi, Maria; Vourtsis, Dionysios; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios. "H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum." Biomol. NMR Assignments 8, 47-51 (2014).
PubMed: 23239108

Assembly members:

Assembly members:
La_motif, polymer, 91 residues, 10534.9 Da.

Natural source:

Natural source: Common Name: Dictyostelium discoideum Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
La_motif: MSEETSTQILKQVEYYFSDS NFPRDKFLRSEAAKNVDNYI SIDVIASFNRMKTISTDLQL ITEALKKSTRLQVSEDGKMV RRLDPLPENID

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	383
15N chemical shifts	88
1H chemical shifts	514

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	La-type RNA-binding domain	1

Entities:

Entity 1, La-type RNA-binding domain 91 residues - 10534.9 Da.

1

MET

SER

GLU

THR

SER

THR

GLN

ILE

LEU

2

LYS

GLN

VAL

GLU

TYR

PHE

SER

ASP

SER

3

ASN

PHE

PRO

ARG

ASP

LYS

PHE

LEU

ARG

SER

4

GLU

ALA

LYS

ASN

VAL

ASP

ASN

TYR

ILE

5

SER

ILE

ASP

VAL

ILE

ALA

SER

PHE

ASN

ARG

6

MET

LYS

THR

ILE

SER

THR

ASP

LEU

GLN

LEU

7

ILE

THR

GLU

ALA

LEU

LYS

SER

THR

ARG

8

LEU

GLN

VAL

SER

GLU

ASP

GLY

LYS

MET

VAL

9

ARG

LEU

ASP

PRO

LEU

PRO

GLU

ASN

ILE

10

ASP

Samples:

sample_1: La-type RNA-binding domain, [U-98% 15N], 0.37 mM; buffer salts 50 mM

sample_2: La-type RNA-binding domain, [U-98% 13C; U-98% 15N], 0.37 mM; buffer salts 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz