BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5500

Title: Parkin binds the Rpn10 subunit of 26S proteasomes with the ubiquitin-like domain

Deposition date: 2002-08-13 Original release date: 2003-03-10

Authors: Sakata, Eri; Yamaguchi, Yoshiki; Kurimoto, Eiji; Kikuchi, Jun; Yokoyama, Shigeyuki; Kawahara, Hiroyuki; Yokosawa, Hideyoshi; Hattori, Nobutaka; Mizuno, Yoshikuni; Tanaka, Keiji; Kato, Koichi

Citation: Sakata, Eri; Yamaguchi, Yoshiki; Kurimoto, Eiji; Kikuchi, Jun; Yokoyama, Shigeyuki; Kawahara, Hiroyuki; Yokosawa, Hideyoshi; Hattori, Nobutaka; Mizuno, Yoshikuni; Tanaka, Keiji; Kato, Koichi. "Parkin binds the Rpn10 subunit of 26S proteasomes with the ubiquitin-like domain"  EMBO Rep. 4, 301-306 (2003).

Assembly members:
Parkin ubiquitin-like domain, polymer, 81 residues, 9235 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: GEX6P

Entity Sequences (FASTA):
Parkin ubiquitin-like domain: GPLGSMIVFVRFNSSHGFPV EVDSDTSIFQLKEVVAKRQG VPADQLRVIFAGKELRNDWT VQNCDLDQQSIVHIVQRPWR K

Data sets:
Data typeCount
1H chemical shifts148
13C chemical shifts216
15N chemical shifts72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ubl1

Entities:

Entity 1, Ubl 81 residues - 9235 Da.

1   GLYPROLEUGLYSERMETILEVALPHEVAL
2   ARGPHEASNSERSERHISGLYPHEPROVAL
3   GLUVALASPSERASPTHRSERILEPHEGLN
4   LEULYSGLUVALVALALALYSARGGLNGLY
5   VALPROALAASPGLNLEUARGVALILEPHE
6   ALAGLYLYSGLULEUARGASNASPTRPTHR
7   VALGLNASNCYSASPLEUASPGLNGLNSER
8   ILEVALHISILEVALGLNARGPROTRPARG
9   LYS

Samples:

sample_1: Parkin ubiquitin-like domain, [U-98% 13C; U-98% 15N], 0.1 mM; potasium phosphate buffer 50 mM

Ex-cond_1: pH: 6.0; temperature: 303 K; ionic strength: 0.3 M

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCnot availablenot availablenot available
2D 1H-13C HSQCnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D CBCANHnot availablenot availablenot available
3D HCACOnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D 15N-edited TOCSYnot availablenot availablenot available

Software:

XWINNMR v2.6 - raw spectral data processing, data analysis

CNS v1.1 - solution structure refinement

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ BAA25751 BAF43729 BAF85279 BAI46122
EMBL CAH90914
GB AAH22014 ABC74794 ABN46990 ACL68652 ACL98151
REF NP_001125521 NP_001274591 NP_004553 NP_054642 NP_054643
SP O60260
AlphaFold O60260

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