BMRB Entry 7383

Name: NMR Structure of RRM-1 of Yeast NPL3 Protein
Published: 2008-05-06

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PDB ID: 2osq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7383
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of RRM-1 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, 74 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: ELSNTRLFVRPFPLDVQESE LNEIFGPFGPMKEVKILNGF AFVEFEEAESAAKAIEEVHG KSFANQPLEVVYSK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	258
15N chemical shifts	75
1H chemical shifts	476

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 74 residues - Formula weight is not available

1

GLU

LEU

SER

ASN

THR

ARG

LEU

PHE

VAL

ARG

2

PRO

PHE

PRO

LEU

ASP

VAL

GLN

GLU

SER

GLU

3

LEU

ASN

GLU

ILE

PHE

GLY

PRO

PHE

GLY

PRO

4

MET

LYS

GLU

VAL

LYS

ILE

LEU

ASN

GLY

PHE

5

ALA

PHE

VAL

GLU

PHE

GLU

ALA

GLU

SER

6

ALA

LYS

ALA

ILE

GLU

VAL

HIS

GLY

7

LYS

SER

PHE

ALA

ASN

GLN

PRO

LEU

GLU

VAL

8

VAL

TYR

SER

LYS

Samples:

sample_1: Nucleolar_protein_3, [U-99% 13C; U-99%15N], 1.0 ± 0.05 mM; Potassium phosphate 20 mM; potassium chloride 20 mM

sample_conditions_1: ionic strength: . .; 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
Varian INOVA 800 MHz
Bruker AVANCE 750 MHz

BMRB	15485
PDB	2JVO 2OSQ
DBJ	GAA22648
EMBL	CAA46817 CAA50291 CAY78932
GB	AAA34818 AAB64865 AHY75384 EDN60757 EDV07905
REF	NP_010720
SP	Q01560
TPG	DAA12270
AlphaFold	Q01560