BMRB Entry 25381
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25381
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Title: Structure of the E. coli threonylcarbamoyl-AMP synthase TsaC PubMed: 26060251
Deposition date: 2014-12-06 Original release date: 2015-06-15
Authors: Harris, Kimberly; Bobay, Benjamin; Sarachan, Kathryn; Sims, Alexis; Bilbille, Yann; Deutsch, Christopher; Iwata-Reuyl, Dirk; Agris, Paul
Citation: Harris, Kimberly; Bobay, Benjamin; Sarachan, Kathryn; Sims, Alexis; Bilbille, Yann; Deutsch, Christopher; Iwata-Reuyl, Dirk; Agris, Paul. "NMR-based Structural Analysis of Threonylcarbamoyl-AMP Synthase and Its Substrate Interactions" J. Biol. Chem. 290, 20032-20043 (2015).
Assembly members:
entity, polymer, 189 residues, 20655.629 Da.
Natural source: Common Name: E.coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: NNNLQRDAIAAAIDVLNEER
VIAYPTEAVFGVGCDPDSET
AVMRLLELKQRPVDKGLILI
AANYEQLKPYIDDTMLTDVQ
RETIFSRWPGPVTFVFPAPA
TTPRWLTGRFDSLAVRVTDH
PLVVALCQAYGKPLVSTSAN
LSGLPPCRTVDEVRAQFGAA
FPVVPGETGGRLNPSEIRDA
LTGELFRQG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 723 |
| 15N chemical shifts | 168 |
| 1H chemical shifts | 1102 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 189 residues - 20655.629 Da.
| 1 | ASN | ASN | ASN | LEU | GLN | ARG | ASP | ALA | ILE | ALA | ||||
| 2 | ALA | ALA | ILE | ASP | VAL | LEU | ASN | GLU | GLU | ARG | ||||
| 3 | VAL | ILE | ALA | TYR | PRO | THR | GLU | ALA | VAL | PHE | ||||
| 4 | GLY | VAL | GLY | CYS | ASP | PRO | ASP | SER | GLU | THR | ||||
| 5 | ALA | VAL | MET | ARG | LEU | LEU | GLU | LEU | LYS | GLN | ||||
| 6 | ARG | PRO | VAL | ASP | LYS | GLY | LEU | ILE | LEU | ILE | ||||
| 7 | ALA | ALA | ASN | TYR | GLU | GLN | LEU | LYS | PRO | TYR | ||||
| 8 | ILE | ASP | ASP | THR | MET | LEU | THR | ASP | VAL | GLN | ||||
| 9 | ARG | GLU | THR | ILE | PHE | SER | ARG | TRP | PRO | GLY | ||||
| 10 | PRO | VAL | THR | PHE | VAL | PHE | PRO | ALA | PRO | ALA | ||||
| 11 | THR | THR | PRO | ARG | TRP | LEU | THR | GLY | ARG | PHE | ||||
| 12 | ASP | SER | LEU | ALA | VAL | ARG | VAL | THR | ASP | HIS | ||||
| 13 | PRO | LEU | VAL | VAL | ALA | LEU | CYS | GLN | ALA | TYR | ||||
| 14 | GLY | LYS | PRO | LEU | VAL | SER | THR | SER | ALA | ASN | ||||
| 15 | LEU | SER | GLY | LEU | PRO | PRO | CYS | ARG | THR | VAL | ||||
| 16 | ASP | GLU | VAL | ARG | ALA | GLN | PHE | GLY | ALA | ALA | ||||
| 17 | PHE | PRO | VAL | VAL | PRO | GLY | GLU | THR | GLY | GLY | ||||
| 18 | ARG | LEU | ASN | PRO | SER | GLU | ILE | ARG | ASP | ALA | ||||
| 19 | LEU | THR | GLY | GLU | LEU | PHE | ARG | GLN | GLY |
Samples:
sample_1: Recombinant TsaC protein, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%
sample_2: Recombinant TsaC protein, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; potassium phosphate 20 mM; sodium chloride 100 mM; Pf1 bacteriophage 12 mg/mL; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 120 mM; 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N TOCSY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 1H-15N HSQC-IPAP | sample_2 | isotropic | sample_conditions_1 |
| 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Varian Inova 600 MHz
- Bruker Avance II 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts