BMRB Entry 51440
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51440
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Title: Identification and characterization of an RRM-containing, RNA binding protein in Acinetobacter Baumannii PubMed: 35883478
Deposition date: 2022-05-13 Original release date: 2022-09-19
Authors: Ciani, Caterina; Perez-Rafols, Anna; Bonomo, Isabelle; Micaelli, Mariachiara; Esposito, Alfonso; Zucal, Chiara; Belli, Romina; D'Agostino, Vito Giuseppe; Bianconi, Irene; Calderone, Vito; Cerofolini, Linda; Fragai, Marco; Provenzani, Alessandro
Citation: Ciani, Caterina; Perez-Rafols, Anna; Bonomo, Isabelle; Micaelli, Mariachiara; Esposito, Alfonso; Zucal, Chiara; Belli, Romina; D'Agostino, Vito Giuseppe; Bianconi, Irene; Calderone, Vito; Cerofolini, Linda; Massidda, Orietta; Whalen, Michael Bernard; Fragai, Marco; Provenzani, Alessandro. "Identification and characterization of an RRM-containing, RNA binding protein in Acinetobacter Baumannii" Biomolecules 12, 922-922 (2022).
Assembly members:
entity_1, polymer, 107 residues, Formula weight is not available
Natural source: Common Name: Acinetobacter Baumannii Taxonomy ID: 470 Superkingdom: Bacteria Kingdom: not available Genus/species: Acinetobacter Baumannii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-30a(+)
Entity Sequences (FASTA):
entity_1: MHMILKCILAFLLMVNEGWK
MKILVRNLDRSVTEAEVLEL
FKAYGKVESCVVVTDKDTGK
SKGFGFVEMPNPREAIKAIK
GLNTLKVKGYGIRVKAAEEL
EHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 232 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 78 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AB-Elavl | 1 |
Entities:
Entity 1, AB-Elavl 107 residues - Formula weight is not available
| 1 | MET | HIS | MET | ILE | LEU | LYS | CYS | ILE | LEU | ALA | ||||
| 2 | PHE | LEU | LEU | MET | VAL | ASN | GLU | GLY | TRP | LYS | ||||
| 3 | MET | LYS | ILE | LEU | VAL | ARG | ASN | LEU | ASP | ARG | ||||
| 4 | SER | VAL | THR | GLU | ALA | GLU | VAL | LEU | GLU | LEU | ||||
| 5 | PHE | LYS | ALA | TYR | GLY | LYS | VAL | GLU | SER | CYS | ||||
| 6 | VAL | VAL | VAL | THR | ASP | LYS | ASP | THR | GLY | LYS | ||||
| 7 | SER | LYS | GLY | PHE | GLY | PHE | VAL | GLU | MET | PRO | ||||
| 8 | ASN | PRO | ARG | GLU | ALA | ILE | LYS | ALA | ILE | LYS | ||||
| 9 | GLY | LEU | ASN | THR | LEU | LYS | VAL | LYS | GLY | TYR | ||||
| 10 | GLY | ILE | ARG | VAL | LYS | ALA | ALA | GLU | GLU | LEU | ||||
| 11 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: AB-Elavl, [U-100% 13C; U-100% 15N], 300 uM; HEPES 20 mM; NaCl 150 mM; MgCl2 3 mM; AEBSF protease inhibitor 1 mM
sample_conditions_1: ionic strength: 0.309 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.1.3 - collection, processing
CARA v1.8 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts