BMRB Entry 7383
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PDB ID:
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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Title: NMR Structure of RRM-1 of Yeast NPL3 Protein PubMed: 18022637
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: 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).
Assembly members:
Nucleolar_protein_3, polymer, 74 residues, Formula weight is not available
Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: not available Kingdom: Eukaryota Genus/species: Fungi Saccharomyces
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Nucleolar_protein_3: ELSNTRLFVRPFPLDVQESE
LNEIFGPFGPMKEVKILNGF
AFVEFEEAESAAKAIEEVHG
KSFANQPLEVVYSK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 258 |
15N chemical shifts | 75 |
1H chemical shifts | 476 |
Additional metadata:
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 | GLU | ALA | GLU | SER | ||||
6 | ALA | ALA | LYS | ALA | ILE | GLU | 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
Related Database Links:
BMRB | 15485 |
PDB | |
DBJ | GAA22648 |
EMBL | CAA46817 CAA50291 CAY78932 |
GB | AAA34818 AAB64865 AHY75384 EDN60757 EDV07905 |
REF | NP_010720 |
SP | Q01560 |
TPG | DAA12270 |
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