BMRB Entry 26603

Name: Sequence-specific 1H, 15N, and 13C resonance assignments of the autophagy-related protein LC3C
Published: 2015-09-30

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PDB ID: 2ncn
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Sequence-specific 1H, 15N, and 13C resonance assignments of the autophagy-related protein LC3C

Deposition date:

2015-07-10

Original release date:

2015-09-30

Authors:

Krichel, Carsten; Weiergraeber, Oliver; Willbold, Dieter; Neudecker, Philipp

Citation:

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).
PubMed: 26280529

Assembly members:

Assembly members:
Microtubule-associated_protein_light_chain_3C_(LC3C), polymer, 128 residues, 14783.2 Da.

Natural source:

Natural source: Common Name: human? Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Microtubule-associated_protein_light_chain_3C_(LC3C): GSMPPPQKIPSVRPFKQRKS LAIRQEEVAGIRAKFPNKIP VVVERYPRETFLPPLDKTKF LVPQELTMTQFLSIIRSRMV LRATEAFYLLVNNKSLVSMS ATMAEIYRDYKDEDGFVYMT YASQETFG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
coupling_constants
- coupling_constant_list_1

Data type	Count
13C chemical shifts	593
15N chemical shifts	131
1H chemical shifts	952
coupling constants	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

GLN

LYS

ILE

PRO

2

SER

VAL

ARG

PRO

PHE

LYS

GLN

ARG

LYS

SER

3

LEU

ALA

ILE

ARG

GLN

GLU

VAL

ALA

GLY

4

ILE

ARG

ALA

LYS

PHE

PRO

ASN

LYS

ILE

PRO

5

VAL

GLU

ARG

TYR

PRO

ARG

GLU

THR

6

PHE

LEU

PRO

LEU

ASP

LYS

THR

LYS

PHE

7

LEU

VAL

PRO

GLN

GLU

LEU

THR

MET

THR

GLN

8

PHE

LEU

SER

ILE

ARG

SER

ARG

MET

VAL

9

LEU

ARG

ALA

THR

GLU

ALA

PHE

TYR

LEU

10

VAL

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

UNP	Q9BXW4
AlphaFold	A2RUP0