BMRB Entry 25124
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25124
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Title: Solution Structure and Chemical Shift Assignments for BeF3 activated Receiver Domain of Nitrogen Regulatory Protein C ( NtrC ) at 35C PubMed: 26073309
Deposition date: 2014-08-04 Original release date: 2015-06-29
Authors: Clarkson, Michael; Pontiggia, Francesco; Villali, Janice; Kern, Dorothee
Citation: Pontiggia, Francesco; Pachov, Dimitar; Clarkson, Michael; Villali, Janice; Hagan, Michael; Pande, Vijay; Kern, Dorothee. "Free energy landscape of activation in a signalling protein at atomic resolution" Nat. Commun. 6, 7284-7284 (2015).
Assembly members:
Receiver_Domain_of_NtrC, polymer, 124 residues, 13636.716 Da.
Natural source: Common Name: salmonella Taxonomy ID: 90371 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Receiver_Domain_of_NtrC: MQRGIVWVVDDDSSIRWVLE
RALAGAGLTCTTFENGNEVL
AALASKTPDVLLSDIRMPGM
DGLALLKQIKQRHPMLPVII
MTAHSDLDAAVSAYQQGAFD
YLPKPFDIDEAVALVERAIS
HYQE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 549 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 890 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Receiver_Domain_of_NtrC | 1 |
Entities:
Entity 1, Receiver_Domain_of_NtrC 124 residues - 13636.716 Da.
| 1 | MET | GLN | ARG | GLY | ILE | VAL | TRP | VAL | VAL | ASP | ||||
| 2 | ASP | ASP | SER | SER | ILE | ARG | TRP | VAL | LEU | GLU | ||||
| 3 | ARG | ALA | LEU | ALA | GLY | ALA | GLY | LEU | THR | CYS | ||||
| 4 | THR | THR | PHE | GLU | ASN | GLY | ASN | GLU | VAL | LEU | ||||
| 5 | ALA | ALA | LEU | ALA | SER | LYS | THR | PRO | ASP | VAL | ||||
| 6 | LEU | LEU | SER | ASP | ILE | ARG | MET | PRO | GLY | MET | ||||
| 7 | ASP | GLY | LEU | ALA | LEU | LEU | LYS | GLN | ILE | LYS | ||||
| 8 | GLN | ARG | HIS | PRO | MET | LEU | PRO | VAL | ILE | ILE | ||||
| 9 | MET | THR | ALA | HIS | SER | ASP | LEU | ASP | ALA | ALA | ||||
| 10 | VAL | SER | ALA | TYR | GLN | GLN | GLY | ALA | PHE | ASP | ||||
| 11 | TYR | LEU | PRO | LYS | PRO | PHE | ASP | ILE | ASP | GLU | ||||
| 12 | ALA | VAL | ALA | LEU | VAL | GLU | ARG | ALA | ILE | SER | ||||
| 13 | HIS | TYR | GLN | GLU |
Samples:
sample_1: Receiver Domain of NtrC, [U-100% 13C; U-100% 15N], 0.3 mM; sodium phosphate 50 mM; beryllium chloride 4.4 mM; sodium fluoride 29 mM; magnesium chloride 7.2 mM; H20 93%; D20 7%
sample_conditions_1: ionic strength: 50 mM; pH: 6.75; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH3-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCD)HD | sample_1 | isotropic | sample_conditions_1 |
| 2D (HB)CB(CGCDCE)HE | 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 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CARA, Professor Kurt W thrich - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Agilent INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 25125 4527 4528 |
| PDB | |
| DBJ | BAB38213 BAE77441 BAG79675 BAI27885 BAI33008 |
| EMBL | CAA28808 CAA59425 CAD03095 CAP78325 CAQ34219 |
| GB | AAB03002 AAC76865 AAG59057 AAL22844 AAN45373 |
| PIR | AC0950 E86074 |
| REF | NP_312817 NP_418304 NP_458044 NP_462885 NP_709666 |
| SP | P0AFB8 P0AFB9 P41789 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts