BMRB Entry 7382

Name: NMR Structure of RRM-2 of Yeast NPL3 Protein
Published: 2008-05-06

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PDB ID: 2osr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7382
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of RRM-2 of Yeast NPL3 Protein

Deposition date:

2007-03-21

Original release date:

2008-05-06

Authors:

Deka, P.; Bucheli, M.; Skrisovska, L.; Allain, F.; Moore, C.; Buratowski, S.; Varani, G.

Citation:

Citation: Deka, P.; Bucheli, M.; Moore, C.; Buratowski, S.; Varani, G.. "Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals" J. Mol. Biol. 375, 136-150 (2008).
PubMed: 18022637

Assembly members:

Assembly members:
Nucleolar_protein_3, polymer, 87 residues, Formula weight is not available

Natural source:

Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: not available Kingdom: Eukaryota Genus/species: Fungi Saccharomyces

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nucleolar_protein_3: KLPAKRYRITMKNLPEGCSW QDLKDLARENSLETTFSSVN TRDFDGTGALEFPSEEILVE ALERLNNIEFRGSVITVERD DNPPPIR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	317
15N chemical shifts	88
1H chemical shifts	583

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Nucleolar_protein_3	1

Entities:

Entity 1, Nucleolar_protein_3 87 residues - Formula weight is not available

1

LYS

LEU

PRO

ALA

LYS

ARG

TYR

ARG

ILE

THR

2

MET

LYS

ASN

LEU

PRO

GLU

GLY

CYS

SER

TRP

3

GLN

ASP

LEU

LYS

ASP

LEU

ALA

ARG

GLU

ASN

4

SER

LEU

GLU

THR

PHE

SER

VAL

ASN

5

THR

ARG

ASP

PHE

ASP

GLY

THR

GLY

ALA

LEU

6

GLU

PHE

PRO

SER

GLU

ILE

LEU

VAL

GLU

7

ALA

LEU

GLU

ARG

LEU

ASN

ILE

GLU

PHE

8

ARG

GLY

SER

VAL

ILE

THR

VAL

GLU

ARG

ASP

9

ASP

ASN

PRO

ILE

ARG

Samples:

sample_1: Nucleolar_protein_3 mM; Potassium phosphate 20 mM; potassium chloride 20 mM

sample_conditions_1: ionic strength: . mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, GUNTERT, P. ET AL. - refinement

CYANA v2.1, GUNTERT, P. ET AL. - structure solution

NMR spectrometers:

Bruker DMX 500 MHz
Bruker AVANCE 750 MHz
Varian INOVA 800 MHz

BMRB	15487
PDB	2JVR 2OSR
DBJ	GAA22648
EMBL	CAA46817 CAA50291 CAY78932
GB	AAA34818 AAB64865 AHY75384 EDN60757 EDV07905
REF	NP_010720 XP_011105020
SP	Q01560
TPG	DAA12270
AlphaFold	Q01560