BMRB Entry 18121
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18121
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Title: 1H, 13C, and 15N chemical shift assignments for CdnLNt from Myxoccoccus xanthus PubMed: 22392343
Deposition date: 2011-12-07 Original release date: 2012-03-09
Authors: Jimenez, M. Angeles; Padmanabhan, S.
Citation: Mirassou, Yasmina; Elias-Arnanz, Montserrat; Padmanabhan, S.; Jimenez, M. Angeles. "(1)H, (13)C and (15)N assignments of CdnL, an essential protein in Myxococcus xanthus." Biomol. NMR Assignments 7, 51-55 (2013).
Assembly members:
CdnL_N-terminal_domain, polymer, 71 residues, 7776.9 Da.
Natural source: Common Name: Myxoccoccus xanthus Taxonomy ID: 34 Superkingdom: Bacteria Kingdom: not available Genus/species: Myxoccoccus xanthus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CdnL_N-terminal_domain: AGHMQTSFKTGDKAVYPGQG
VGEVMGIEHTEVAGQRQSFY
VLRILENGMRIMIPINKVGS
VGLREIISEED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 138 |
| 1H chemical shifts | 628 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CdnLNt | 1 |
Entities:
Entity 1, CdnLNt 71 residues - 7776.9 Da.
AGH is the N-terminal cloning tag
| 1 | ALA | GLY | HIS | MET | GLN | THR | SER | PHE | LYS | THR | ||||
| 2 | GLY | ASP | LYS | ALA | VAL | TYR | PRO | GLY | GLN | GLY | ||||
| 3 | VAL | GLY | GLU | VAL | MET | GLY | ILE | GLU | HIS | THR | ||||
| 4 | GLU | VAL | ALA | GLY | GLN | ARG | GLN | SER | PHE | TYR | ||||
| 5 | VAL | LEU | ARG | ILE | LEU | GLU | ASN | GLY | MET | ARG | ||||
| 6 | ILE | MET | ILE | PRO | ILE | ASN | LYS | VAL | GLY | SER | ||||
| 7 | VAL | GLY | LEU | ARG | GLU | ILE | ILE | SER | GLU | GLU | ||||
| 8 | ASP |
Samples:
sample_1: CdnL N-terminal domain 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.5 mM
sample_2: CdnL N-terminal domain 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.5 mM
sample_3: CdnL N-terminal domain, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.5 mM
sample_4: CdnL N-terminal domain, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.5 mM
sample_5: CdnL N-terminal domain, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; DSS 0.25 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_5 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_5 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_5 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_2 |
| 3D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 18151 |
| PDB | |
| GB | ABF89955 ADO71151 AEI66063 AFE08291 AGC44335 |
| REF | WP_002617724 WP_002625147 WP_002639129 WP_011552697 WP_013939202 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts