BMRB Entry 34761

Name: Solution structure of tandem RRM1 and RRM2 domains of yeast NPL3
Published: 2025-07-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34761

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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 structure of tandem RRM1 and RRM2 domains of yeast NPL3

Deposition date:

2022-10-04

Original release date:

2025-07-07

Authors:

Kachariya, N.; Sattler, M.; Keil, P.; Strasser, K.

Citation:

Citation: Keil, P.; Wulf, A.; Kachariya, N.; Reuscher, S.; Huhn, K.; Silbern, I.; Altmuller, J.; Keller, M.; Stehle, R.; Zarnack, K.; Sattler, M.; Urlaub, H.; Strasser, K.. "Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA." Nucleic Acids Res. 51, 831-851 (2023).
PubMed: 36583366

Assembly members:

Assembly members:
entity_1, polymer, 161 residues, 18228.414 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET family vector

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GELSNTRLFVRPFPLDVQES ELNEIFGPFGPMKEVKILNG FAFVEFEEAESAAKAIEEVH GKSFANQPLEVVYSKLPAKR YRITMKNLPEGCSWQDLKDL ARENSLETTFSSVNTRDFDG TGALEFPSEEILVEALERLN NIEFRGSVITVERDDNPPPI R

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	452
15N chemical shifts	163
1H chemical shifts	995

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 161 residues - 18228.414 Da.

1

GLY

GLU

LEU

SER

ASN

THR

ARG

LEU

PHE

VAL

2

ARG

PRO

PHE

PRO

LEU

ASP

VAL

GLN

GLU

SER

3

GLU

LEU

ASN

GLU

ILE

PHE

GLY

PRO

PHE

GLY

4

PRO

MET

LYS

GLU

VAL

LYS

ILE

LEU

ASN

GLY

5

PHE

ALA

PHE

VAL

GLU

PHE

GLU

ALA

GLU

6

SER

ALA

LYS

ALA

ILE

GLU

VAL

HIS

7

GLY

LYS

SER

PHE

ALA

ASN

GLN

PRO

LEU

GLU

8

VAL

TYR

SER

LYS

LEU

PRO

ALA

LYS

ARG

9

TYR

ARG

ILE

THR

MET

LYS

ASN

LEU

PRO

GLU

10

GLY

CYS

SER

TRP

GLN

ASP

LEU

LYS

ASP

LEU

11

ALA

ARG

GLU

ASN

SER

LEU

GLU

THR

PHE

12

SER

VAL

ASN

THR

ARG

ASP

PHE

ASP

GLY

13

THR

GLY

ALA

LEU

GLU

PHE

PRO

SER

GLU

14

ILE

LEU

VAL

GLU

ALA

LEU

GLU

ARG

LEU

ASN

15

ASN

ILE

GLU

PHE

ARG

GLY

SER

VAL

ILE

THR

16

VAL

GLU

ARG

ASP

ASN

PRO

ILE

17

ARG

Samples:

sample_1: RRM1,2 of NPL3, [U-100% 15N], 150 uM

sample_2: RRM1,2 of NPL3, [U-100% 13C; U-100% 15N], 1000 uM

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

TopSpin v3.5pl6, Bruker Biospin - collection

TopSpin, Bruker Biospin - processing

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

CcpNmr Analysis v2.5.0, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AVANCE III 950 MHz
Bruker AVANCE III 900 MHz
Bruker AVANCE III 800 MHz

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