BMRB Entry 18151
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18151
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Title: 1H, 13C, and 15N chemical shift assignments for CdnL from Myxoccoccus xanthus PubMed: 22392343
Deposition date: 2011-12-19 Original release date: 2012-03-09
Authors: Jimenez, M. Angeles; Padmanabhan, S.; Mirassou, Yasmina
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, polymer, 167 residues, 18982.7 Da.
Natural source: Common Name: Myxococcus 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: GSHMQTSFKTGDKAVYPGQG
VGEVMGIEHTEVAGQRQSFY
VLRILENGMRIMIPINKVGS
VGLREIISEEDVKQVYSILK
EKDISVDSTTWNRRYREYME
KIKTGSVFEIAEVLRDLYLL
KGDKDLSFGERKMLDTARSL
LIKELSLAKDCSEDEIESDL
KKIFNLA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 539 |
15N chemical shifts | 166 |
1H chemical shifts | 1082 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | CdnL | 1 |
Entities:
Entity 1, CdnL 167 residues - 18982.7 Da.
GSH is the N-terminal cloning tag
1 | GLY | SER | 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 | VAL | LYS | GLN | VAL | TYR | SER | ILE | LEU | LYS | ||||
9 | GLU | LYS | ASP | ILE | SER | VAL | ASP | SER | THR | THR | ||||
10 | TRP | ASN | ARG | ARG | TYR | ARG | GLU | TYR | MET | GLU | ||||
11 | LYS | ILE | LYS | THR | GLY | SER | VAL | PHE | GLU | ILE | ||||
12 | ALA | GLU | VAL | LEU | ARG | ASP | LEU | TYR | LEU | LEU | ||||
13 | LYS | GLY | ASP | LYS | ASP | LEU | SER | PHE | GLY | GLU | ||||
14 | ARG | LYS | MET | LEU | ASP | THR | ALA | ARG | SER | LEU | ||||
15 | LEU | ILE | LYS | GLU | LEU | SER | LEU | ALA | LYS | ASP | ||||
16 | CYS | SER | GLU | ASP | GLU | ILE | GLU | SER | ASP | LEU | ||||
17 | LYS | LYS | ILE | PHE | ASN | LEU | ALA |
Samples:
sample_1: CdnL 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM
sample_2: CdnL 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM
sample_3: CdnL, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM
sample_4: CdnL, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM
sample_5: CdnL 0.25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.1 mM
sample_6: CdnL 0.25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.1 mM
sample_7: CdnL, [U-100% 13C; U-100% 15N], 0.25 mM; sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 0.05%; beta-mercaptoethanol 2 mM; DSS 0.5 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 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 CBCA(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-1H COSY | sample_5 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_5 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_5 | isotropic | sample_conditions_1 |
2D 1H-1H COSY | sample_6 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_6 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_6 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_7 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_7 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
BMRB | 15977 |
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