BMRB Entry 18292

Name: NMR structure of the RNA binding motif 39 (RBM39) from Mus musculus
Published: 2012-03-22

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PDB ID: 2lq5
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/BMR18292
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the RNA binding motif 39 (RBM39) from Mus musculus

Deposition date:

2012-02-23

Original release date:

2012-03-22

Authors:

Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the RNA binding motif 39 (RBM39) from Mus musculus" .

Assembly members:

Assembly members:
entity, polymer, 113 residues, 12516.306 Da.

Natural source:

Natural source: Common Name: House mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: VQPLATQCFQLSNMFNPQTE EEVGWDTEIKDDVIEECNKH GGVIHIYVDKNSAQGNVYVK CPSIAAAIAAVNALHGRWFA GKMITAAYVPLPTYHNLFPD SMTATQLLVPSRR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	476
15N chemical shifts	120
1H chemical shifts	756

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RBM39	1

Entities:

Entity 1, RBM39 113 residues - 12516.306 Da.

1

VAL

GLN

PRO

LEU

ALA

THR

GLN

CYS

PHE

GLN

2

LEU

SER

ASN

MET

PHE

ASN

PRO

GLN

THR

GLU

3

GLU

VAL

GLY

TRP

ASP

THR

GLU

ILE

LYS

4

ASP

VAL

ILE

GLU

CYS

ASN

LYS

HIS

5

GLY

VAL

ILE

HIS

ILE

TYR

VAL

ASP

LYS

6

ASN

SER

ALA

GLN

GLY

ASN

VAL

TYR

VAL

LYS

7

CYS

PRO

SER

ILE

ALA

ILE

ALA

8

VAL

ASN

ALA

LEU

HIS

GLY

ARG

TRP

PHE

ALA

9

GLY

LYS

MET

ILE

THR

ALA

TYR

VAL

PRO

10

LEU

PRO

THR

TYR

HIS

ASN

LEU

PHE

PRO

ASP

11

SER

MET

THR

ALA

THR

GLN

LEU

VAL

PRO

12

SER

ARG

Samples:

sample_1: RBM39, [U-95% 13C; U-95% 15N], 1.2 mM; sodium azide 4.5 mM; sodium chloride 50 mM; sodium phosphate 25 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.083 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
4D APSY HACANH	sample_1	isotropic	sample_conditions_1
5D APSY CBCACONH	sample_1	isotropic	sample_conditions_1
5D APSY HACACONH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

UNIO, Unio Herrmann Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LQ5 3S6E 4J5O 4OZ0 4OZ1 4RU2 5CXT
DBJ	BAE22009 BAE22477 BAE27657 BAE32977 BAG54289
EMBL	CAD97833 CAE45833 CAE45890 CAH18281 CAH90627
GB	AAA16346 AAA16347 AAH04000 AAH30493 AAH82607
REF	NP_001013225 NP_001125339 NP_001162566 NP_001164806 NP_001193433
SP	Q14498 Q5RC80 Q8VH51
TPG	DAA23046
AlphaFold	Q14498 Q5RC80 Q8VH51