BMRB Entry 26664

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26664

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Title:
UBXD1
Deposition date:
2015-09-19
Original release date:
2015-11-09
Authors:
Trusch, Franziska
Citation:

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).
PubMed: 26475856

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET41b

Entity Sequences (FASTA):

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