BMRB Entry 27844

Name: Backbone 1H and 15N Chemical Shift Assignments for Proteasome Assembling Chaperone 3
Published: 2019-05-22

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR27844

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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:

Backbone 1H and 15N Chemical Shift Assignments for Proteasome Assembling Chaperone 3

Deposition date:

2019-03-20

Original release date:

2019-05-22

Authors:

Yagi-Utsumi, Maho; Kato, Koichi; Okamoto, Kenta

Citation:

Citation: Satoh, Tadashi; Yagi-Utsumi, Maho; Okamoto, Kenta; Kurimoto, Eiji; Tanaka, Keiji; Kato, Koichi. "Molecular and Structural Basis of the Proteasome alpha Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer" Int. J. Mol. Sci. 20, E2231-E2231 (2019).
PubMed: 31067643

Assembly members:

Assembly members:
proteasome_assembly_chaperone, polymer, 122 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
proteasome_assembly_chaperone: MEDTPLVISKQKTEVVCGVP TQVVCTAFSSHILVVVTQFG KMGTLVSLEPSSVASDVSKP VLTTKVLLGQDEPLIHVFAK NLVAFVSQEAGNRAVVLAVA VKDKSMEGLKALREVIRVCQ VW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	106
1H chemical shifts	106

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PAC3	1

Entities:

Entity 1, PAC3 122 residues - Formula weight is not available

1

MET

GLU

ASP

THR

PRO

LEU

VAL

ILE

SER

LYS

2

GLN

LYS

THR

GLU

VAL

CYS

GLY

VAL

PRO

3

THR

GLN

VAL

CYS

THR

ALA

PHE

SER

4

HIS

ILE

LEU

VAL

THR

GLN

PHE

GLY

5

LYS

MET

GLY

THR

LEU

VAL

SER

LEU

GLU

PRO

6

SER

VAL

ALA

SER

ASP

VAL

SER

LYS

PRO

7

VAL

LEU

THR

LYS

VAL

LEU

GLY

GLN

8

ASP

GLU

PRO

LEU

ILE

HIS

VAL

PHE

ALA

LYS

9

ASN

LEU

VAL

ALA

PHE

VAL

SER

GLN

GLU

ALA

10

GLY

ASN

ARG

ALA

VAL

LEU

ALA

VAL

ALA

11

VAL

LYS

ASP

LYS

SER

MET

GLU

GLY

LEU

LYS

12

ALA

LEU

ARG

GLU

VAL

ILE

ARG

VAL

CYS

GLN

13

VAL

TRP

Samples:

sample_1: proteasome assembly chaperone, [U-100% 13C; U-100% 15N], 0.2 mM; sodium phosphate 20 mM; EDTA 1 mM; D2O 10%; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 303 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 500 MHz
Bruker DMX 500 MHz

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