BMRB Entry 52751

Name: Aminopeptidase I N-terminal 45 residue
Published: 2024-12-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52751

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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:

Aminopeptidase I N-terminal 45 residue

Deposition date:

2024-12-10

Original release date:

2024-12-17

Authors:

Kumeta, Hiroyuki

Citation:

Citation: Yamasaki, Akinori; Watanabe, Yasunori; Adachi, Wakana; Suzuki, Kuninori; Matoba, Kazuaki; Kirisako, Hiromi; Kumeta, Hiroyuki; Nakatogawa, Hitoshi; Ohsumi, Yoshinori; Inagaki, Fuyuhiko; Noda, Nobuo. "Structural Basis for Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates." Cell Rep. 16, 19-27 (2016).
PubMed: 27320913

Assembly members:

Assembly members:
entity_1, polymer, 48 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX6p

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMEEQREILEQLKKTLQM LTVEPSKNNQIANEEKEKKE NENSWCIL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	138
15N chemical shifts	47
1H chemical shifts	47

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ape1N45	1

Entities:

Entity 1, Ape1N45 48 residues - Formula weight is not available

Residues 1-3 are cloning artifacts

1

GLY

PRO

HIS

MET

GLU

GLN

ARG

GLU

ILE

2

LEU

GLU

GLN

LEU

LYS

THR

LEU

GLN

MET

3

LEU

THR

VAL

GLU

PRO

SER

LYS

ASN

GLN

4

ILE

ALA

ASN

GLU

LYS

GLU

LYS

GLU

5

ASN

GLU

ASN

SER

TRP

CYS

ILE

LEU

Samples:

sample_1: Ape1N45, [U-99% 13C; U-99% 15N], 25 uM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 0.125 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)HA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe v2012.090.12.09 - processing

VNMR v6.3C - collection

RNMRTK v3.2.5-b9125 - processing

SPARKY v3.113 - chemical shift assignment

NMR spectrometers:

Varian Unity INOVA 600 MHz

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