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 5298

Title: 1H, 13C, and 15N Chemical Shift Assignments for the PPIase domain from E. coli trigger factor

Authors: Kozlov, Guennadi; Trempe, Jean-Francois; Perreault, Audry; Wong, Molly; Denisov, Aleksej; Ghandi, Shaifali; Gehring, Kalle; Ekiel, Irena

Citation: Kozlov, Guennadi; Trempe, Jean-Francois; Perreault, Audry; Wong, Molly; Denisov, Aleksej; Ghandi, Shaifali; Gehring, Kalle; Ekiel, Irena. "Solution structure of the closed form of a peptidyl-prolyl isomerase reveals the mechanism of protein folding "  . ., .-..

Assembly members:
peptidyl-prolyl isomerase, polymer, 106 residues, 11647 Da.

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

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

Entity Sequences (FASTA):
peptidyl-prolyl isomerase: GSHMQATWKEKDGAVEAEDR VTIDFTGSVDGEEFEGGKAS DFVLAMGQGRMIPGFEDGIK GHKAGEEFTIDVTFPEEYHA ENLKGKAAKFAINLKKVEER ELPELT

Data sets:
Data typeCount
1H chemical shifts536
13C chemical shifts187
15N chemical shifts98
coupling constants82

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PPIase1

Entities:

Entity 1, PPIase 106 residues - 11647 Da.

1   GLYSERHISMETGLNALATHRTRPLYSGLU
2   LYSASPGLYALAVALGLUALAGLUASPARG
3   VALTHRILEASPPHETHRGLYSERVALASP
4   GLYGLUGLUPHEGLUGLYGLYLYSALASER
5   ASPPHEVALLEUALAMETGLYGLNGLYARG
6   METILEPROGLYPHEGLUASPGLYILELYS
7   GLYHISLYSALAGLYGLUGLUPHETHRILE
8   ASPVALTHRPHEPROGLUGLUTYRHISALA
9   GLUASNLEULYSGLYLYSALAALALYSPHE
10   ALAILEASNLEULYSLYSVALGLUGLUARG
11   GLULEUPROGLULEUTHR

Samples:

sample_1: peptidyl-prolyl isomerase2.0 – 3.0 mM; NaCl 100 mM

sample_2: peptidyl-prolyl isomerase, [U-15N], 2.0 – 3.0 mM; NaCl 100 mM

sample_3: peptidyl-prolyl isomerase, [U-13C; U-15N], 2.0 – 3.0 mM; NaCl 100 mM

conditions_1: pH: 6.8; temperature: 303 K; ionic strength: 0.1 M; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available
3D 1H-1H-15N TOCSYnot availablenot availablenot available
3D HNHAnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available

Software:

XWINNMR v2.1 - data collection

GIFA v4.31 - data processing

XEASY v1.3.13 - peak assignments

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 19835 19836 19837
PDB
DBJ BAB33913 BAD98926 BAE76216 BAG75986 BAH62052
EMBL CAP74970 CAQ30908 CAQ90076 CAQ97312 CAR01780
GB AAA62791 AAB40192 AAC73539 AAG54786 AAN42037
REF NP_286178 NP_308517 NP_414970 NP_706330 NP_752485
SP A1A8A5 A6T5H9 A7ZIJ4 A7ZX94 A8AK17