BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26603

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

Data sets:
Data typeCount
13C chemical shifts593
15N chemical shifts131
1H chemical shifts952
coupling constants94

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Microtubule-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   GLYSERMETPROPROPROGLNLYSILEPRO
2   SERVALARGPROPHELYSGLNARGLYSSER
3   LEUALAILEARGGLNGLUGLUVALALAGLY
4   ILEARGALALYSPHEPROASNLYSILEPRO
5   VALVALVALGLUARGTYRPROARGGLUTHR
6   PHELEUPROPROLEUASPLYSTHRLYSPHE
7   LEUVALPROGLNGLULEUTHRMETTHRGLN
8   PHELEUSERILEILEARGSERARGMETVAL
9   LEUARGALATHRGLUALAPHETYRLEULEU
10   VALASNASNLYSSERLEUVALSERMETSER
11   ALATHRMETALAGLUILETYRARGASPTYR
12   LYSASPGLUASPGLYPHEVALTYRMETTHR
13   TYRALASERGLNGLUTHRPHEGLY

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:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_13C15N_D2Oisotropicsample_conditions_1
2D 1H-1H NOESYsample_13C15N_D2Oisotropicsample_conditions_1
2D 1H-15N HSQCsample_15N_H2Oisotropicsample_conditions_1
3D 1H-15N TOCSYsample_15N_H2Oisotropicsample_conditions_1
3D 1H-15N NOESYsample_15N_H2Oisotropicsample_conditions_1
3D 1H-15N 1H-15N NOESYsample_15N_H2Oisotropicsample_conditions_1
3D HNHAsample_13C15N_H2Oisotropicsample_conditions_1
2D 1H-13C HSQCsample_13C15N_D2Oisotropicsample_conditions_1
3D HNCOsample_13C15N_H2Oisotropicsample_conditions_1
3D HNCAsample_13C15N_H2Oisotropicsample_conditions_1
3D HNCACBsample_13C15N_H2Oisotropicsample_conditions_1
3D CBCA(CO)NHsample_13C15N_H2Oisotropicsample_conditions_1
3D HBHA(CO)NHsample_13C15N_H2Oisotropicsample_conditions_1
3D C(CO)NHsample_13C15N_H2Oisotropicsample_conditions_1
3D H(CCO)NHsample_13C15N_H2Oisotropicsample_conditions_1
3D H(C)CH-COSYsample_13C15N_D2Oisotropicsample_conditions_1
3D (H)CCH-COSYsample_13C15N_D2Oisotropicsample_conditions_1
3D HC(C)H-TOCSYsample_13C15N_D2Oisotropicsample_conditions_1
3D 1H-13C NOESYsample_13C15N_D2Oisotropicsample_conditions_1
3D 1H-13C 1H-15N NOESYsample_13C15N_H2Oisotropicsample_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

Related Database Links:

UNP Q9BXW4

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts