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 50539

Title: Mechanistic basis for ubiquitin modulation of a protein energy landscape   PubMed: 33723075

Deposition date: 2020-10-28 Original release date: 2021-03-17

Authors: Carroll, Emma; Latorraca, Naomi; Lindner, Johanna; Maguire, Brendan; Pelton, Jeff; Marqusee, Susan

Citation: Carroll, Emma; Latorraca, Naomi; Lindner, Johanna; Maguire, Brendan; Pelton, Jeff; Marqusee, Susan. "Mechanistic basis for ubiquitin modulation of a protein energy landscape"  Proc. Natl. Acad. Sci. U.S.A. 118, e2025126118-e2025126118 (2021).

Assembly members:
entity_1, polymer, 92 residues, Formula weight is not available

Natural source:   Common Name: Bacillus amyloliquefaciens   Taxonomy ID: 1390   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus amyloliquefaciens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEC062

Entity Sequences (FASTA):
entity_1: GPGRRAVINGEQIRSISDLH QTLRRELALPEYYGENLDAL WDALTGWVEYPLVLEWRQFE QSKQLTENGAESVLQVFREA RAEGCDITIILS

Data sets:
Data typeCount
13C chemical shifts123
15N chemical shifts69
1H chemical shifts69

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1BarstarK60_AC11

Entities:

Entity 1, BarstarK60_AC1 92 residues - Formula weight is not available

Six mutations compared to wildtype Barstar - K1R K2R K21R K22R C40A K78R. Cloning artifact leaves GPG scar on N-terminus.

1   GLYPROGLYARGARGALAVALILEASNGLY
2   GLUGLNILEARGSERILESERASPLEUHIS
3   GLNTHRLEUARGARGGLULEUALALEUPRO
4   GLUTYRTYRGLYGLUASNLEUASPALALEU
5   TRPASPALALEUTHRGLYTRPVALGLUTYR
6   PROLEUVALLEUGLUTRPARGGLNPHEGLU
7   GLNSERLYSGLNLEUTHRGLUASNGLYALA
8   GLUSERVALLEUGLNVALPHEARGGLUALA
9   ARGALAGLUGLYCYSASPILETHRILEILE
10   LEUSER

Samples:

sample_1: BarstarK60, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.129 M; pH: 6.5; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2 - collection

CARA v1.9.1 - chemical shift assignment, data analysis

NMRPipe v8.7 - processing

NMR spectrometers:

  • Bruker-Biospin Inc. AV2 900 MHz

Related Database Links:

PDB

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