BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16882

Title: Solution Structure of the Ubiquitin-Binding Motif of Human Polymerase Iota   PubMed: 20159559

Deposition date: 2010-04-19 Original release date: 2010-06-15

Authors: Bomar, Martha; D'Souza, Sanjay; Bienko, Marzena; Dikic, Ivan; Walker, Graham

Citation: Bomar, Martha; Bienko, Sanjay; Dikic, Marzena; Walker, Ivan; Zhou, Graham. "Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1."  Mol. Cell 37, 408-417 (2010).

Assembly members:
Ubiquitin-Binding Motif, polymer, 108 residues, 3753.299 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: pET30-GB1-fusion

Entity Sequences (FASTA):
Ubiquitin-Binding Motif: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTEGSDE KITFPSDIDPQVFYELPEAV QKELLAEWKRTGSDFHIGHK LEHHHHHH

Data sets:
Data typeCount
13C chemical shifts435
15N chemical shifts103
1H chemical shifts694

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBM21

Entities:

Entity 1, UBM2 108 residues - 3753.299 Da.

Residues 1-56 represent the GB1-tag. Residues 57-58, 101-108 are cloning artifacts (including the His6-tag)

1   METGLNTYRLYSLEUILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALPHE
4   LYSGLNTYRALAASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLUGLYSERASPGLU
7   LYSILETHRPHEPROSERASPILEASPPRO
8   GLNVALPHETYRGLULEUPROGLUALAVAL
9   GLNLYSGLULEULEUALAGLUTRPLYSARG
10   THRGLYSERASPPHEHISILEGLYHISLYS
11   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: UBM2, [U-100% 13C; U-100% 15N], 1 – 4 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15156 15380 16444 16627 16873 17810 18397 26630
PDB

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