BMRB Entry 27725

Title:
1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli
Deposition date:
2018-12-12
Original release date:
2019-02-07
Authors:
Jia, Moye; Hu, Yunfei; Jin, Changwen
Citation:

Citation: Jia, Moye; Hu, Yunfei; Jin, Changwen. "1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli"  Biomol. NMR Assignments 13, 183-186 (2019).
PubMed: 30684235

Assembly members:

Assembly members:
SurA_P2, polymer, 115 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28a(+)

Data sets:
Data typeCount
13C chemical shifts495
15N chemical shifts116
1H chemical shifts776

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1SurA_P21

Entities:

Entity 1, SurA_P2 115 residues - Formula weight is not available

The first Met residue is artificially added at the N-terminus of the recombinant protein. K278-A391 is the remainder based on Uniprot P0ABZ6.

1   METLYSASNILESERVALTHRGLUVALHIS
2   ALAARGHISILELEULEULYSPROSERPRO
3   ILEMETTHRASPGLUGLNALAARGVALLYS
4   LEUGLUGLNILEALAALAASPILELYSSER
5   GLYLYSTHRTHRPHEALAALAALAALALYS
6   GLUPHESERGLNASPPROGLYSERALAASN
7   GLNGLYGLYASPLEUGLYTRPALATHRPRO
8   ASPILEPHEASPPROALAPHEARGASPALA
9   LEUTHRARGLEUASNLYSGLYGLNMETSER
10   ALAPROVALHISSERSERPHEGLYTRPHIS
11   LEUILEGLULEULEUASPTHRARGASNVAL
12   ASPLYSTHRASPALA

Related Database Links:

UNP P0ABZ6
AlphaFold Q8KMY0

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