BMRB Entry 18827

Name: Sequence-specific 1H,13C, and 15N resonance assignment of GATE-16
Published: 2018-01-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18827

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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,13C, and 15N resonance assignment of GATE-16

Deposition date:

2012-11-07

Original release date:

2018-01-12

Authors:

Ma, Peixiang; Hartmann, Rudolf; Matthias, Stoldt; Mohrluder, Jeannine; Schwarten, Melanie; Willbold, Dieter

Citation:

Citation: Ma, Peixiang; Schillinger, Oliver; Schwarten, Melanie; Lecher, Justin; Hartmann, Rudolf; Stoldt, Matthias; Mohrluder, Jeannine; Olubiyi, Olujide; Strodel, Birgit; Willbold, Dieter; Weiergraber, Oliver. "Conformational Polymorphism in Autophagy-Related Protein GATE-16." Biochemistry 54, 5469-5479 (2015).
PubMed: 26284781

Assembly members:

Assembly members:
GABARAPL2, polymer, 119 residues, 13813.9529 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-4T-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GABARAPL2: GSMKWMFKEDHSLEHRCVES AKIRAKYPDRVPVIVEKVSG SQIVDIDKRKYLVPSDITVA QFMWIIRKRIQLPSEKAIFL FVDKTVPQSSLTMGQLYEKE KDEDGFLYVAYSGENTFGF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	333
15N chemical shifts	106
1H chemical shifts	208

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Gate16	1

Entities:

Entity 1, Gate16 119 residues - 13813.9529 Da.

Residues 1-2 represent non-native overhang residues from thrombin cleavage.

1

GLY

SER

MET

LYS

TRP

MET

PHE

LYS

GLU

ASP

2

HIS

SER

LEU

GLU

HIS

ARG

CYS

VAL

GLU

SER

3

ALA

LYS

ILE

ARG

ALA

LYS

TYR

PRO

ASP

ARG

4

VAL

PRO

VAL

ILE

VAL

GLU

LYS

VAL

SER

GLY

5

SER

GLN

ILE

VAL

ASP

ILE

ASP

LYS

ARG

LYS

6

TYR

LEU

VAL

PRO

SER

ASP

ILE

THR

VAL

ALA

7

GLN

PHE

MET

TRP

ILE

ARG

LYS

ARG

ILE

8

GLN

LEU

PRO

SER

GLU

LYS

ALA

ILE

PHE

LEU

9

PHE

VAL

ASP

LYS

THR

VAL

PRO

GLN

SER

10

LEU

THR

MET

GLY

GLN

LEU

TYR

GLU

LYS

GLU

11

LYS

ASP

GLU

ASP

GLY

PHE

LEU

TYR

VAL

ALA

12

TYR

SER

GLY

GLU

ASN

THR

PHE

GLY

PHE

Samples:

15N_GATE-16: Gate16, [U-99% 15N], 0.236 mM; KCl 50.000 mM; NaH2PO4/Na2HPO4 25.000 mM; Ethylenediaminetetraacetic acid (EDTA) 0.050 mM; Dithiothreitol (DTT) 10.000 mM; H2O 95%; D2O 5%

15N-13C_GATE-16: Gate16, [U-99% 13C; U-99% 15N], 0.411 mM; KCl 50.000 mM; NaH2PO4/Na2HPO4 25.000 mM; Ethylenediaminetetraacetic acid (EDTA) 0.050 mM; Dithiothreitol (DTT) 10.000 mM; H2O 95%; D2O 5%

CondSet1: pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC/HMQC	15N_GATE-16	isotropic	CondSet1
3D HNCA	15N-13C_GATE-16	isotropic	CondSet1
3D HNCACB	15N-13C_GATE-16	isotropic	CondSet1
3D HNCO	15N-13C_GATE-16	isotropic	CondSet1
3D HN(CO)CA	15N-13C_GATE-16	isotropic	CondSet1
HNcaCo (H[N[ca[CO]]])	15N-13C_GATE-16	isotropic	CondSet1
3D 1H-15N NOESY	15N_GATE-16	isotropic	CondSet1
hbha_co_nh (H{[N]+[HA]})	15N-13C_GATE-16	isotropic	CondSet1
3D HCCH-COSY	15N-13C_GATE-16	isotropic	CondSet1
2D 1H-13C HSQC/HMQC	15N-13C_GATE-16	isotropic	CondSet1

Software:

ANALYSIS v2.2, CCPN - chemical shift assignment, peak picking

NMRPipe v3.0.2007.068.09.07, NIH - processing

VnmrJ v2.3A, Agilent Technologies (formerly Varian) - collection, processing

NMR spectrometers:

Varian VNMRS 900 MHz
Varian UnityInova 600 MHz
Varian VNMRS 800 MHz

UniProt	P60520
AlphaFold	Q9UQF7