BMRB Entry 26725
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26725
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Title: MtRpsA_S4 PubMed: 27412769
Deposition date: 2016-01-08 Original release date: 2016-02-16
Authors: Biling, Huang
Citation: Huang, Biling; Fu, Jinglin; Guo, Chenyun; Wu, Xueji; Lin, Donghai; Liao, Xinli. "(1)H, (15)N, (13)C resonance assignments for pyrazinoic acid binding domain of ribosomal protein S1 from Mycobacterium tuberculosis" Biomol. NMR Assign. 10, 321-324 (2016).
Assembly members:
entity, polymer, 89 residues, Formula weight is not available
Natural source: Common Name: high GC Gram+ Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: QEDPWRHFARTHAIGQIVPG
KVTKLVPFGAFVRVEEGIEG
LVHISELAERHVEVPDQVVA
VGDDAMVKVIDIDLERRRIS
LSLKQANED
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 355 |
15N chemical shifts | 87 |
1H chemical shifts | 691 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MtRpsA_S4 | 1 |
Entities:
Entity 1, MtRpsA_S4 89 residues - Formula weight is not available
1 | GLN | GLU | ASP | PRO | TRP | ARG | HIS | PHE | ALA | ARG | ||||
2 | THR | HIS | ALA | ILE | GLY | GLN | ILE | VAL | PRO | GLY | ||||
3 | LYS | VAL | THR | LYS | LEU | VAL | PRO | PHE | GLY | ALA | ||||
4 | PHE | VAL | ARG | VAL | GLU | GLU | GLY | ILE | GLU | GLY | ||||
5 | LEU | VAL | HIS | ILE | SER | GLU | LEU | ALA | GLU | ARG | ||||
6 | HIS | VAL | GLU | VAL | PRO | ASP | GLN | VAL | VAL | ALA | ||||
7 | VAL | GLY | ASP | ASP | ALA | MET | VAL | LYS | VAL | ILE | ||||
8 | ASP | ILE | ASP | LEU | GLU | ARG | ARG | ARG | ILE | SER | ||||
9 | LEU | SER | LEU | LYS | GLN | ALA | ASN | GLU | ASP |
Samples:
sample_1: MtRpsA_S4, [U-100% 13C; U-100% 15N], 0.6 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts