BMRB Entry 51558

Name: 1H, 13C, and 15N backbone resonance assignments of human VPS37A N-terminal domain from 1 to 148 residues in buffer
Published: 2024-03-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51558

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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:

1H, 13C, and 15N backbone resonance assignments of human VPS37A N-terminal domain from 1 to 148 residues in buffer

Deposition date:

2022-08-10

Original release date:

2024-03-25

Authors:

Ye, Yansheng; Tian, Fang; Wang, Hong-Gang; Wang, Guifang; Liang, Xinwen; Takahashi, Yoshinori; Bewley, Maria C.; Flanagan, John M.

Citation:

Citation: Ye, Yansheng; Liang, Xinwen; Wang, Guifang; Bewley, Maria; Hamamoto, Kouta; Liu, Xiaoming; Flanagan, John; Wang, Hong-Gang; Takahashi, Yoshinori; Tian, Fang. "Identification of membrane curvature sensing motifs essential for VPS37A phagophore recruitment and autophagosome closure" Commun. Biol. 7, 334-334 (2024).
PubMed: 38491121

Assembly members:

Assembly members:
entity_1, polymer, 148 residues, Formula weight is not available

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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSWLFPLTKSASSSAAGSPG GLTSLQQQKQRLIESLRNSH SSIAEIQKDVEYRLPFTINN LTININILLPPQFPQEKPVI SVYPPIRHHLMDKQGVYVTS PLVNNFTMHSDLGKIIQSLL DEFWKNPPVLAPTSTAFPYL YSNPSGMS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	387
15N chemical shifts	118
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VPS37A_1-148	1

Entities:

Entity 1, VPS37A_1-148 148 residues - Formula weight is not available

1

MET

SER

TRP

LEU

PHE

PRO

LEU

THR

LYS

SER

2

ALA

SER

ALA

GLY

SER

PRO

GLY

3

GLY

LEU

THR

SER

LEU

GLN

LYS

GLN

4

ARG

LEU

ILE

GLU

SER

LEU

ARG

ASN

SER

HIS

5

SER

ILE

ALA

GLU

ILE

GLN

LYS

ASP

VAL

6

GLU

TYR

ARG

LEU

PRO

PHE

THR

ILE

ASN

7

LEU

THR

ILE

ASN

ILE

ASN

ILE

LEU

PRO

8

PRO

GLN

PHE

PRO

GLN

GLU

LYS

PRO

VAL

ILE

9

SER

VAL

TYR

PRO

ILE

ARG

HIS

LEU

10

MET

ASP

LYS

GLN

GLY

VAL

TYR

VAL

THR

SER

11

PRO

LEU

VAL

ASN

PHE

THR

MET

HIS

SER

12

ASP

LEU

GLY

LYS

ILE

GLN

SER

LEU

13

ASP

GLU

PHE

TRP

LYS

ASN

PRO

VAL

LEU

14

ALA

PRO

THR

SER

THR

ALA

PHE

PRO

TYR

LEU

15

TYR

SER

ASN

PRO

SER

GLY

MET

SER

Samples:

sample_1: VPS37A_1-148, [U-100% 13C; U-100% 15N], 275 uM; Disodium Phosphate 20 mM; NaCl 150 mM; DTT 1 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRViewJ - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks