BMRB Entry 18620

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

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18620

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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:

NMR Chemical Shift Assignments of N terminal RRM 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:
RRM, polymer, 99 residues, 11412.86 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):
RRM: GKTLYSKGWPEDTTIEKVQE FFNANGGYKVVSVRLRKKSD KSFKGSFLADFETEEIVNKI ITEAPKLGEKELIYQTFKQF SDEKKDEKEKFFASTNGDK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	430
15N chemical shifts	102
1H chemical shifts	536

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM domain	1

Entities:

Entity 1, RRM domain 99 residues - 11412.86 Da.

1

GLY

LYS

THR

LEU

TYR

SER

LYS

GLY

TRP

PRO

2

GLU

ASP

THR

ILE

GLU

LYS

VAL

GLN

GLU

3

PHE

ASN

ALA

ASN

GLY

TYR

LYS

VAL

4

VAL

SER

VAL

ARG

LEU

ARG

LYS

SER

ASP

5

LYS

SER

PHE

LYS

GLY

SER

PHE

LEU

ALA

ASP

6

PHE

GLU

THR

GLU

ILE

VAL

ASN

LYS

ILE

7

ILE

THR

GLU

ALA

PRO

LYS

LEU

GLY

GLU

LYS

8

GLU

LEU

ILE

TYR

GLN

THR

PHE

LYS

GLN

PHE

9

SER

ASP

GLU

LYS

ASP

GLU

LYS

GLU

LYS

10

PHE

ALA

SER

THR

ASN

GLY

ASP

LYS

Samples:

sample_1: RRM, [U-98% 15N], 0.35 mM; buffer salts 50 mM

sample_2: RRM, [U-98% 13C; U-98% 15N], 0.35 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