BMRB Entry 26603
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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/BMR26603
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Title: Sequence-specific 1H, 15N, and 13C resonance assignments of the autophagy-related protein LC3C PubMed: 26280529
Deposition date: 2015-07-10 Original release date: 2015-09-30
Authors: Krichel, Carsten; Weiergraeber, Oliver; Willbold, Dieter; Neudecker, Philipp
Citation: Krichel, Carsten; Weiergraeber, Oliver; Pavlidou, Marina; Mohrlueder, Jeannine; Schwarten, Melanie; Willbold, Dieter; Neudecker, Philipp. "Sequence-specific 1H, 15N, and 13C resonance assignments of the autophagy-related protein LC3C" Biomol. NMR Assignments 10, 41-43 (2016).
Assembly members:
Microtubule-associated_protein_light_chain_3C_(LC3C), polymer, 128 residues, 14783.2 Da.
Natural source: Common Name: human? Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Microtubule-associated_protein_light_chain_3C_(LC3C): GSMPPPQKIPSVRPFKQRKS
LAIRQEEVAGIRAKFPNKIP
VVVERYPRETFLPPLDKTKF
LVPQELTMTQFLSIIRSRMV
LRATEAFYLLVNNKSLVSMS
ATMAEIYRDYKDEDGFVYMT
YASQETFG
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 593 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 952 |
| coupling constants | 94 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Microtubule-associated protein light chain 3C (LC3C) | 1 |
Entities:
Entity 1, Microtubule-associated protein light chain 3C (LC3C) 128 residues - 14783.2 Da.
Residues Gly-1 and Ser0 are cloning artifacts from protease cleavage.
| 1 | GLY | SER | MET | PRO | PRO | PRO | GLN | LYS | ILE | PRO | ||||
| 2 | SER | VAL | ARG | PRO | PHE | LYS | GLN | ARG | LYS | SER | ||||
| 3 | LEU | ALA | ILE | ARG | GLN | GLU | GLU | VAL | ALA | GLY | ||||
| 4 | ILE | ARG | ALA | LYS | PHE | PRO | ASN | LYS | ILE | PRO | ||||
| 5 | VAL | VAL | VAL | GLU | ARG | TYR | PRO | ARG | GLU | THR | ||||
| 6 | PHE | LEU | PRO | PRO | LEU | ASP | LYS | THR | LYS | PHE | ||||
| 7 | LEU | VAL | PRO | GLN | GLU | LEU | THR | MET | THR | GLN | ||||
| 8 | PHE | LEU | SER | ILE | ILE | ARG | SER | ARG | MET | VAL | ||||
| 9 | LEU | ARG | ALA | THR | GLU | ALA | PHE | TYR | LEU | LEU | ||||
| 10 | VAL | ASN | ASN | LYS | SER | LEU | VAL | SER | MET | SER | ||||
| 11 | ALA | THR | MET | ALA | GLU | ILE | TYR | ARG | ASP | TYR | ||||
| 12 | LYS | ASP | GLU | ASP | GLY | PHE | VAL | TYR | MET | THR | ||||
| 13 | TYR | ALA | SER | GLN | GLU | THR | PHE | GLY |
Samples:
sample_15N_H2O: Microtubule-associated protein light chain 3C (LC3C), [U-15N], 0.35 – 0.7 mM; PIPES 20 mM; sodium chloride 150 mM; EDTA 0.1 mM; glycerol, [U-2H], 2 % v/v; H2O 90%; D2O 10%
sample_13C15N_H2O: Microtubule-associated protein light chain 3C (LC3C), [U-13C; U-15N], 0.35 – 0.7 mM; PIPES 20 mM; sodium chloride 150 mM; EDTA 0.1 mM; glycerol, U-2H], 2 % v/v; H2O 90%; D2O 10%
sample_13C15N_D2O: Microtubule-associated protein light chain 3C (LC3C), [U-13C; U-15N], 0.35 – 0.7 mM; PIPES 20 mM; sodium chloride 150 mM; EDTA 0.1 mM; glycerol, [U-2H], 2 % v/v; D2O 100%
sample_conditions_1: ionic strength: 171 mM; pH: 6.0; pressure: 1 atm; temperature: 293.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_15N_H2O | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_15N_H2O | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_15N_H2O | isotropic | sample_conditions_1 |
| 3D 1H-15N 1H-15N NOESY | sample_15N_H2O | isotropic | sample_conditions_1 |
| 3D HNHA | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 3D HNCO | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D HNCA | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_13C15N_H2O | isotropic | sample_conditions_1 |
| 3D H(C)CH-COSY | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 3D HC(C)H-TOCSY | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_13C15N_D2O | isotropic | sample_conditions_1 |
| 3D 1H-13C 1H-15N NOESY | sample_13C15N_H2O | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
Analysis, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts