BMRB Entry 15485
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15485
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Title: Segmental isotope labeling of Npl3 PubMed: 17936301
Deposition date: 2007-09-24 Original release date: 2008-06-26
Authors: Skrisovska, Lenka; Allain, Frederic
Citation: Skrisovska, Lenka; Allain, Frederic. "Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: application to the RRMs of Npl3p and hnRNP L." J. Mol. Biol. 375, 151-164 (2008).
Assembly members:
Npl3_RRM1, polymer, 108 residues, 12239 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Npl3_RRM1: MGSSHHHHHHSSGLVPRGSH
MHHRQEGELSNTRLFVRPFP
LDVQESELNEIFGPFGPMKE
VKILNGFAFVEFEEAESAAK
AIEEVHGKSFANQPLEVVYS
KLPAKRYR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 237 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 513 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM 1 | 1 |
Entities:
Entity 1, RRM 1 108 residues - 12239 Da.
Residues 1-20 represent a N-terminal sequence originated from pET28a+ vector which includes His tag
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | HIS | HIS | ARG | GLN | GLU | GLY | GLU | LEU | SER | ||||
| 4 | ASN | THR | ARG | LEU | PHE | VAL | ARG | PRO | PHE | PRO | ||||
| 5 | LEU | ASP | VAL | GLN | GLU | SER | GLU | LEU | ASN | GLU | ||||
| 6 | ILE | PHE | GLY | PRO | PHE | GLY | PRO | MET | LYS | GLU | ||||
| 7 | VAL | LYS | ILE | LEU | ASN | GLY | PHE | ALA | PHE | VAL | ||||
| 8 | GLU | PHE | GLU | GLU | ALA | GLU | SER | ALA | ALA | LYS | ||||
| 9 | ALA | ILE | GLU | GLU | VAL | HIS | GLY | LYS | SER | PHE | ||||
| 10 | ALA | ASN | GLN | PRO | LEU | GLU | VAL | VAL | TYR | SER | ||||
| 11 | LYS | LEU | PRO | ALA | LYS | ARG | TYR | ARG |
Samples:
sample_1: Npl3 RRM1, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%
sample_2: Npl3 RRM1, [U-13C; U-15N], 1 mM; D2O 100%
sample_3: Npl3 RRM1, [U-15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis
ATHNOS-CANDID, T. Herrmann - automated NOE assignment, automated peak picking, structure calculation
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 600 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| EMBL | CAA46817 CAA50291 CAY78932 |
| GB | AAA34818 AAB64865 AHY75384 AJP38110 AJU58232 |
| REF | NP_010720 |
| SP | Q01560 |
| TPG | DAA12270 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts