BMRB Entry 19967

Name: Solution NMR assignment of C-terminal RRM domain of La protein from D. discoideum.
Published: 2018-02-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19967

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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 NMR assignment of C-terminal RRM domain of La protein from D. discoideum.

Deposition date:

2014-05-12

Original release date:

2018-02-27

Authors:

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

Citation:

Citation: Argyriou, Aikaterini; Chasapis, Christos; Apostolidi, Maria; Konstantinidou, Parthena; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios. "Backbone and side chain NMR assignment, along with the secondary structure prediction of RRM2 domain of La protein from a lower eukaryote exhibiting identical structural organization with its human homolog" Biomol NMR Assign. 9, 219-222 (2015).
PubMed: 25281001

Assembly members:

Assembly members:
CRRM, polymer, 105 residues, 12027.6 Da.

Natural source:

Natural source: Common Name: cellular slime mold 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):
CRRM: KDVKKEVEEEEVMIPGVILC FKGVGKGLHRGDIKEIFSQY GEVQFVGYNSDEENGSVRYK TAESCKRAIESLTETKKEIG GQIPTYNLLEGEEEKKEWEK IIERK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	460
15N chemical shifts	108
1H chemical shifts	743

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CRRM domain	1

Entities:

Entity 1, CRRM domain 105 residues - 12027.6 Da.

1

LYS

ASP

VAL

LYS

GLU

VAL

GLU

2

GLU

VAL

MET

ILE

PRO

GLY

VAL

ILE

LEU

CYS

3

PHE

LYS

GLY

VAL

GLY

LYS

GLY

LEU

HIS

ARG

4

GLY

ASP

ILE

LYS

GLU

ILE

PHE

SER

GLN

TYR

5

GLY

GLU

VAL

GLN

PHE

VAL

GLY

TYR

ASN

SER

6

ASP

GLU

ASN

GLY

SER

VAL

ARG

TYR

LYS

7

THR

ALA

GLU

SER

CYS

LYS

ARG

ALA

ILE

GLU

8

SER

LEU

THR

GLU

THR

LYS

GLU

ILE

GLY

9

GLY

GLN

ILE

PRO

THR

TYR

ASN

LEU

GLU

10

GLY

GLU

LYS

GLU

TRP

GLU

LYS

11

ILE

GLU

ARG

LYS

Samples:

sample_1: CRRM, [U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: CRRM, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_3: CRRM 0.8 mM; H2O 90%; D2O 10%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance III 700 MHz

UNP	Q54TG6
AlphaFold	Q54TG6