BMRB Entry 15263
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15263
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Title: 1H, 13C, and 15N Chemical Shift Assignments for NAB2 N-terminal domain PubMed: 18190927
Deposition date: 2007-05-22 Original release date: 2008-02-21
Authors: Grant, Richard; Marshall, Neil; Yang, Ji-Chun; Fasken, Milo; Kelly, Seth; Harreman, Michelle; Neuhaus, David; Corbett, Anita; Stewart, Murray
Citation: Grant, Richard; Marshall, Neil; Yang, Ji-Chun; Fasken, Milo; Kelly, Seth; Harreman, Michelle; Neuhaus, David; Corbett, Anita; Stewart, Murray. "Structure of the N-Terminal Mlp1-Binding Domain of the Saccharomyces cerevisiae mRNA-Binding Protein, Nab2" J. Mol. Biol. 376, 1048-1059 (2008).
Assembly members:
NAB2_NTD, polymer, 105 residues, 11462.986 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):
NAB2_NTD: MSQEQYTENLKVIVAEKLAG
IPNFNEDIKYVAEYIVLLIV
NGGTVESVVDELASLFDSVS
RDTLANVVQTAFFALEALQQ
GESAENIVSKIRMMNAQSLG
QSDIA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 339 |
15N chemical shifts | 111 |
1H chemical shifts | 712 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NAB2 NTD polypeptide | 1 |
Entities:
Entity 1, NAB2 NTD polypeptide 105 residues - 11462.986 Da.
1 | MET | SER | GLN | GLU | GLN | TYR | THR | GLU | ASN | LEU | ||||
2 | LYS | VAL | ILE | VAL | ALA | GLU | LYS | LEU | ALA | GLY | ||||
3 | ILE | PRO | ASN | PHE | ASN | GLU | ASP | ILE | LYS | TYR | ||||
4 | VAL | ALA | GLU | TYR | ILE | VAL | LEU | LEU | ILE | VAL | ||||
5 | ASN | GLY | GLY | THR | VAL | GLU | SER | VAL | VAL | ASP | ||||
6 | GLU | LEU | ALA | SER | LEU | PHE | ASP | SER | VAL | SER | ||||
7 | ARG | ASP | THR | LEU | ALA | ASN | VAL | VAL | GLN | THR | ||||
8 | ALA | PHE | PHE | ALA | LEU | GLU | ALA | LEU | GLN | GLN | ||||
9 | GLY | GLU | SER | ALA | GLU | ASN | ILE | VAL | SER | LYS | ||||
10 | ILE | ARG | MET | MET | ASN | ALA | GLN | SER | LEU | GLY | ||||
11 | GLN | SER | ASP | ILE | ALA |
Samples:
sample_1: NAB2_NTD, [U-98% 13C; U-98% 15N], 2 mM; D2O, [U-2H], 10%; H2O 90%; sodium phosphate 25 mM; sodium chloride 10 mM
sample_conditions_1: ionic strength: 160 mM; pH: 6.0; pressure: 1 atm; temperature: 300 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC CT | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY 15N filtered in F2 | 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 HNHAHB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR, Brunger - structure solution
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DMX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
PDB | |
DBJ | GAA23273 |
EMBL | CAA96830 CAY79645 |
GB | AAA34819 AAA34820 AAU09727 AHY79261 AJP38679 |
REF | NP_011393 |
SP | P32505 |
TPG | DAA07987 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts