BMRB Entry 53299

Name: RBM39 N-Terminal tandem RRM1-2
Published: 2025-08-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53299

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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:

RBM39 N-Terminal tandem RRM1-2

Deposition date:

2025-07-31

Original release date:

2025-08-21

Authors:

Malard, Florian; Bouton, Lea; Campagne, Sebastien

Citation:

Citation: Malard, Florian; Bouton, Lea; Campagne, Sebastien. "1H, 13C and 15N backbone resonance assignment of the RNA binding motif 39 (RBM39) tandem RNA recognition motifs (RRM1-2)" Biomol. NMR Assign. 19, 293-298 (2025).
PubMed: 40944856

Assembly members:

Assembly members:
entity_1, polymer, 191 residues, Formula weight is not available

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: pET24bII(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IDNLTPEERDARTVFCMQLA ARIRPRDLEEFFSTVGKVRD VRMISDRNSRRSKGIAYVEF VDVSSVPLAIGLTGQRVLGV PIIVQASQAEKNRAAAMANN LQKGSAGPMRLYVGSLHFNI TEDMLRGIFEPFGRIESIQL MMDSETGRSKGYGFITFSDS ECAKKALEQLNGFELAGRPM KVGHVTERTDA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	549
15N chemical shifts	187
1H chemical shifts	197

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RBM39_RRM1-2	1

Entities:

Entity 1, RBM39_RRM1-2 191 residues - Formula weight is not available

Starts at I142 to follow the numbering of the full length protein

1

ILE

ASP

ASN

LEU

THR

PRO

GLU

ARG

ASP

2

ALA

ARG

THR

VAL

PHE

CYS

MET

GLN

LEU

ALA

3

ALA

ARG

ILE

ARG

PRO

ARG

ASP

LEU

GLU

4

PHE

SER

THR

VAL

GLY

LYS

VAL

ARG

ASP

5

VAL

ARG

MET

ILE

SER

ASP

ARG

ASN

SER

ARG

6

ARG

SER

LYS

GLY

ILE

ALA

TYR

VAL

GLU

PHE

7

VAL

ASP

VAL

SER

VAL

PRO

LEU

ALA

ILE

8

GLY

LEU

THR

GLY

GLN

ARG

VAL

LEU

GLY

VAL

9

PRO

ILE

VAL

GLN

ALA

SER

GLN

ALA

GLU

10

LYS

ASN

ARG

ALA

MET

ALA

ASN

11

LEU

GLN

LYS

GLY

SER

ALA

GLY

PRO

MET

ARG

12

LEU

TYR

VAL

GLY

SER

LEU

HIS

PHE

ASN

ILE

13

THR

GLU

ASP

MET

LEU

ARG

GLY

ILE

PHE

GLU

14

PRO

PHE

GLY

ARG

ILE

GLU

SER

ILE

GLN

LEU

15

MET

ASP

SER

GLU

THR

GLY

ARG

SER

LYS

16

GLY

TYR

GLY

PHE

ILE

THR

PHE

SER

ASP

SER

17

GLU

CYS

ALA

LYS

ALA

LEU

GLU

GLN

LEU

18

ASN

GLY

PHE

GLU

LEU

ALA

GLY

ARG

PRO

MET

19

LYS

VAL

GLY

HIS

VAL

THR

GLU

ARG

THR

ASP

20

ALA

Samples:

sample_1: RBM39 N-Terminal tandem RRM1-2, [U-13C; U-15N], 500 uM; sodium phosphate 10 mM; sodium chloride 50 mM; TCEP 1 mM; D2O 10%

sample_conditions_1: ionic strength: 0.045 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_1	isotropic	sample_conditions_1
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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5 - chemical shift assignment

TOPSPIN v3.5 - collection

NMR spectrometers:

Bruker AVANCE III 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks