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 26664

Title: UBXD1   PubMed: 26475856

Deposition date: 2015-09-19 Original release date: 2015-11-09

Authors: Trusch, Franziska

Citation: Trusch, Franziska; Matena, Anja; Vuk, Maja; Koerver, Lisa; Knaevelsrud, Helene; Freemont, Paul; Meyer, Hemmo; Bayer, Peter. "The N-terminal Region of the UBX Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97"  J. Biol. Chem. 290, 29414-29427 (2015).

Assembly members:
UBXD1-N, polymer, 120 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
UBXD1-N: MKKFFQEFKADIKFKSAGPG QKLKESVGEKAHKEKPNQPA PRPPRQGPTNEAQMAAAAAL ARLEQKQSRAWGPTSQDTIR NQVRKELQAEATVSGSPEAP GTNVVSEPREEGSAHLAVPG

Data sets:
Data typeCount
13C chemical shifts196
15N chemical shifts91
1H chemical shifts178

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBXD1-N1

Entities:

Entity 1, UBXD1-N 120 residues - Formula weight is not available

1   METLYSLYSPHEPHEGLNGLUPHELYSALA
2   ASPILELYSPHELYSSERALAGLYPROGLY
3   GLNLYSLEULYSGLUSERVALGLYGLULYS
4   ALAHISLYSGLULYSPROASNGLNPROALA
5   PROARGPROPROARGGLNGLYPROTHRASN
6   GLUALAGLNMETALAALAALAALAALALEU
7   ALAARGLEUGLUGLNLYSGLNSERARGALA
8   TRPGLYPROTHRSERGLNASPTHRILEARG
9   ASNGLNVALARGLYSGLULEUGLNALAGLU
10   ALATHRVALSERGLYSERPROGLUALAPRO
11   GLYTHRASNVALVALSERGLUPROARGGLU
12   GLUGLYSERALAHISLEUALAVALPROGLY

Samples:

UBXD1-N_sample: UBXD1-N, [U-13C; U-15N], 250 uM; potassium phosphate buffer 50 mM; H2O 90%; D2O 10%

UBXD1-N_condition: ionic strength: 0.050 M; pH: 6.5; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCUBXD1-N_sampleisotropicUBXD1-N_condition
2D 1H-1H NOESYUBXD1-N_sampleisotropicUBXD1-N_condition
3D CBCA(CO)NHUBXD1-N_sampleisotropicUBXD1-N_condition
3D HNCACBUBXD1-N_sampleisotropicUBXD1-N_condition
3D HNCAUBXD1-N_sampleisotropicUBXD1-N_condition
3D HNCOUBXD1-N_sampleisotropicUBXD1-N_condition
3D HN(CO)CAUBXD1-N_sampleisotropicUBXD1-N_condition
3D HCACOUBXD1-N_sampleisotropicUBXD1-N_condition
3D 1H-15N TOCSYUBXD1-N_sampleisotropicUBXD1-N_condition
3D 1H-15N NOESYUBXD1-N_sampleisotropicUBXD1-N_condition

Software:

Auremol, Bruker Biospin - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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