BMRB Entry 16211

Title:
Solution structure of putative prolyl isomerase PpiD from E.Coli
Deposition date:
2009-03-12
Original release date:
2009-11-05
Authors:
Weininger, Ulrich; Jakob, Roman
Citation:

Citation: Weininger, Ulrich; Jakob, Roman; Kovermann, Michael; Balbach, Jochen; Schmid, Franz. "The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity."  Protein Sci. 19, 6-18 (2010).
PubMed: 19866485

Assembly members:

Assembly members:
prolyl isomerase domain, polymer, 102 residues, 11173.603 Da.

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: pET 11a

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts108
1H chemical shifts690

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1prolyl isomerase domain1

Entities:

Entity 1, prolyl isomerase domain 102 residues - 11173.603 Da.

1   THRGLNPROGLNARGTHRARGTYRSERILE
2   ILEGLNTHRLYSTHRGLUASPGLUALALYS
3   ALAVALLEUASPGLULEUASNLYSGLYGLY
4   ASPPHEALAALALEUALALYSGLULYSSER
5   ALAASPILEILESERALAARGASNGLYGLY
6   ASPMETGLYTRPLEUGLUASPALATHRILE
7   PROASPGLULEULYSASNALAGLYLEULYS
8   GLULYSGLYGLNLEUSERGLYVALILELYS
9   SERSERVALGLYPHELEUILEVALARGLEU
10   ASPASPILEGLNALAALAHISHISHISHIS
11   HISHIS

Samples:

sample_1: potassium phosphate 100 mM; entity, [U-15N], 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v2.0, Linge, O'Donoghue and Nilges - chemical shift assignment, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA11645 BAB33918 BAE76221 BAG75991 BAI23815
EMBL CAP74975 CAQ30914 CAQ97317 CAR01785 CAR06675
GB AAB40197 AAC73544 AAG54791 AAN42042 AAN79035
REF NP_308522 NP_414975 NP_706335 WP_000969091 WP_000969347
SP P0ADY1 P0ADY2
AlphaFold P0ADY2 P0ADY1

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