BMRB Entry 1520

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR1520

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Title:
Characterization of a Partially Denatured State of a Protein by Two-Dimensional NMR: Reduction of the Hydrophobic Interactions in Ubiquitin
Deposition date:
1995-07-31
Original release date:
1995-07-31
Authors:
Harding, Margaret; Williams, Dudley; Woolfson, Derek
Citation:

Citation: Harding, Margaret; Williams, Dudley; Woolfson, Derek. "Characterization of a Partially Denatured State of a Protein by Two-Dimensional NMR: Reduction of the Hydrophobic Interactions in Ubiquitin"  Biochemistry 30, 3120-3128 (1991).

Assembly members:

Assembly members:
ubiquitin, polymer, 70 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: cow   Taxonomy ID: 9909   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos primigenius

Experimental source:

Experimental source:   Production method: not available

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin: XQIFVKTXXXXTITLEVXXX XXXXXVXXXXXXXEXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXTXHXV

Data sets:
Data typeCount
1H chemical shifts79

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin1

Entities:

Entity 1, ubiquitin 70 residues - Formula weight is not available

1   XGLNILEPHEVALLYSTHRXXX
2   XTHRILETHRLEUGLUVALXXX
3   XXXXXVALXXXX
4   XXXGLUXXXXXX
5   XXXXXXXXXX
6   XXXXXXXXXX
7   XXXXXTHRXHISXVAL

Samples:

sample_one:

sample_condition_set_one: pH: 2 na; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
unknownsample_oneisotropicsample_condition_set_one

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz