BMRB Entry 15802
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15802
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Title: 1H, 13C, and 15N resonance assignments of a RNA binding protein GSP13 from Bacillus subtilis PubMed: 19636895
Deposition date: 2008-06-11 Original release date: 2008-07-29
Authors: Yu, Wenyu; Yu, Bingke; Hu, Jicheng; Jin, Changwen; Xia, Bin
Citation: Yu, Wenyu; Yu, Bingke; Hu, Jicheng; Xia, Wei; Jin, Changwen; Xia, Bin. "1H, 13C, and 15N resonance assignments of a general stress protein GSP13 from Bacillus subtilis" Biomol. NMR Assignments 2, 163-165 (2008).
Assembly members:
GSP13, polymer, 130 residues, Formula weight is not available
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a
Entity Sequences (FASTA):
GSP13: MAAKFEVGSVYTGKVTGLQA
YGAFVALDEETQGLVHISEV
THGFVKDINEHLSVGDEVQV
KVLAVDEEKGKISLSIRATQ
AAPEKKESKPRKPKAAQVSE
EASTPQGFNTLKDKLEEWIE
MSNRKDLIKK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 525 |
15N chemical shifts | 131 |
1H chemical shifts | 886 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | GSP13 | 1 |
Entities:
Entity 1, GSP13 130 residues - Formula weight is not available
1 | MET | ALA | ALA | LYS | PHE | GLU | VAL | GLY | SER | VAL | |
2 | TYR | THR | GLY | LYS | VAL | THR | GLY | LEU | GLN | ALA | |
3 | TYR | GLY | ALA | PHE | VAL | ALA | LEU | ASP | GLU | GLU | |
4 | THR | GLN | GLY | LEU | VAL | HIS | ILE | SER | GLU | VAL | |
5 | THR | HIS | GLY | PHE | VAL | LYS | ASP | ILE | ASN | GLU | |
6 | HIS | LEU | SER | VAL | GLY | ASP | GLU | VAL | GLN | VAL | |
7 | LYS | VAL | LEU | ALA | VAL | ASP | GLU | GLU | LYS | GLY | |
8 | LYS | ILE | SER | LEU | SER | ILE | ARG | ALA | THR | GLN | |
9 | ALA | ALA | PRO | GLU | LYS | LYS | GLU | SER | LYS | PRO | |
10 | ARG | LYS | PRO | LYS | ALA | ALA | GLN | VAL | SER | GLU | |
11 | GLU | ALA | SER | THR | PRO | GLN | GLY | PHE | ASN | THR | |
12 | LEU | LYS | ASP | LYS | LEU | GLU | GLU | TRP | ILE | GLU | |
13 | MET | SER | ASN | ARG | LYS | ASP | LEU | ILE | LYS | LYS |
Samples:
sample_1: GSP13, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 20 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_2: GSP13, [U-100% 15N], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.07 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | 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-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
PDB | |
DBJ | BAI86662 BAM55208 BAM59221 GAK80090 |
EMBL | CAB07921 CAB15128 CBI44065 CCU60178 CEI58372 |
GB | ADM39092 ADV93943 AEB25277 AEB64738 AEK90308 |
REF | NP_391017 WP_003220769 WP_003228864 WP_010331658 WP_013353366 |
SP | P80870 |
AlphaFold | P80870 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts