BMRB Entry 27844

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

Data sets:
Data typeCount
15N chemical shifts106
1H chemical shifts106

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PAC31

Entities:

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

1   METGLUASPTHRPROLEUVALILESERLYS
2   GLNLYSTHRGLUVALVALCYSGLYVALPRO
3   THRGLNVALVALCYSTHRALAPHESERSER
4   HISILELEUVALVALVALTHRGLNPHEGLY
5   LYSMETGLYTHRLEUVALSERLEUGLUPRO
6   SERSERVALALASERASPVALSERLYSPRO
7   VALLEUTHRTHRLYSVALLEULEUGLYGLN
8   ASPGLUPROLEUILEHISVALPHEALALYS
9   ASNLEUVALALAPHEVALSERGLNGLUALA
10   GLYASNARGALAVALVALLEUALAVALALA
11   VALLYSASPLYSSERMETGLUGLYLEULYS
12   ALALEUARGGLUVALILEARGVALCYSGLN
13   VALTRP

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_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