BMRB Entry 25160

Name: NMR structure of the RRM1 of human LARP6
Published: 2014-12-22

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PDB ID: 2mtg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25160
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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 structure of the RRM1 of human LARP6

Deposition date:

2014-08-18

Original release date:

2014-12-22

Authors:

Martino, Luigi; Atkinson, Andrew; Kelly, Geoff; Conte, Maria

Citation:

Citation: Martino, Luigi; Pennell, Simon; Kelly, Geoff; Busi, Baptiste; Brown, Paul; Atkinson, Andrew; Salisbury, Nicholas; Ooi, Zi; See, Kang; Smerdon, Stephen; Alfano, Caterina; Bui, Tam; Conte, Maria. "Synergic interplay of the La motif, RRM1, and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module" Nucleic Acids Res. ., .-. (2014).
PubMed: 25488812

Assembly members:

Assembly members:
LARP6_RRM1, polymer, 116 residues, 13132.548 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-duet1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LARP6_RRM1: NLPSKMLLVYDLYLSPKLWA LATPQKNGRVQEKVMEHLLK LFGTFGVISSVRILKPGREL PPDIRRISSRYSQVGTQECA IVEFEEVEAAIKAHEFMITE SQGKENMKAVLIGMKP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	689
13C chemical shifts	461
15N chemical shifts	104

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 116 residues - 13132.548 Da.

1

ASN

LEU

PRO

SER

LYS

MET

LEU

VAL

TYR

2

ASP

LEU

TYR

LEU

SER

PRO

LYS

LEU

TRP

ALA

3

LEU

ALA

THR

PRO

GLN

LYS

ASN

GLY

ARG

VAL

4

GLN

GLU

LYS

VAL

MET

GLU

HIS

LEU

LYS

5

LEU

PHE

GLY

THR

PHE

GLY

VAL

ILE

SER

6

VAL

ARG

ILE

LEU

LYS

PRO

GLY

ARG

GLU

LEU

7

PRO

ASP

ILE

ARG

ILE

SER

ARG

8

TYR

SER

GLN

VAL

GLY

THR

GLN

GLU

CYS

ALA

9

ILE

VAL

GLU

PHE

GLU

VAL

GLU

ALA

10

ILE

LYS

ALA

HIS

GLU

PHE

MET

ILE

THR

GLU

11

SER

GLN

GLY

LYS

GLU

ASN

MET

LYS

ALA

VAL

12

LEU

ILE

GLY

MET

LYS

PRO

Samples:

sample_1: LARP6 RRM1, [U-95% 13C; U-95% 15N], 0.5 mM; TRIS 50 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 7.25; pressure: 1 atm; ionic strength: 0.1 M

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	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

Software:

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Varian INOVA 800 MHz
Bruker Avance 700 MHz
Bruker Avance 500 MHz

DBJ	BAA92061 BAK62255
EMBL	CAD38733
GB	AAH06082 AAH09446 AAH14018 AAN76710 AAN76711
REF	NP_001233506 NP_001273608 NP_060827 XP_001088126 XP_002753339
SP	Q9BRS8
AlphaFold	Q9BRS8