BMRB Entry 18959

Name: NMR structure of Rsa1p238-259 from S. Cerevisiae
Published: 2013-11-26

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PDB ID: 2m3f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18959
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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 Rsa1p238-259 from S. Cerevisiae PubMed: 24234454

Deposition date: 2013-01-17 Original release date: 2013-11-26

Authors: Quinternet, Marc; Manival, Xavier

Citation: Rothe, Benjamin; Back, Regis; Quinternet, Marc; Bizarro, Jonathan; Robert, Marie-Cecile; Blaud, Magali; Romier, Christophe; Manival, Xavier; Charpentier, Bruno; Bertrand, Edouard; Branlant, Christiane. "Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly." Nucleic Acids Res. 42, 2015-2036 (2014).

Assembly members:
Rsa1p238-259, polymer, 22 residues, 2840.349 Da.

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

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
Rsa1p238-259: TDEDVKKWREERKKMWLLKI SN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	90
15N chemical shifts	26
1H chemical shifts	352

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rsa1p238-259	1

Entities:

Entity 1, Rsa1p238-259 22 residues - 2840.349 Da.

1

THR

ASP

GLU

ASP

VAL

LYS

TRP

ARG

GLU

2

GLU

ARG

LYS

MET

TRP

LEU

LYS

ILE

3

SER

ASN

Samples:

sample_1: Rsa1p238-259 2 mM; potassium phosphate 10 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 3.7; pressure: 1 atm; temperature: 293 K

sample_conditions_2: ionic strength: 150 mM; pH: 3.7; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC-TOCSY	sample_1	isotropic	sample_conditions_2

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CARA, Keller and Wuthrich - chemical shift assignment

PREDITOR, Wishart DS. - structure solution

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2M3F 4NUT
DBJ	GAA26783
EMBL	CAA97906 CAY86767
GB	AHY77988 AJP41956 AJU23400 AJU24088 AJU24761
REF	NP_015131
SP	Q08932
TPG	DAA11241

Biological Magnetic Resonance Data Bank