BMRB Entry 4352

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Inhibitor-Bound DNase Domain of Colicin E9.
Deposition date:
1999-06-14
Original release date:
2006-10-27
Authors:
Whittaker, Sara; Czisch, Michael; Wechselberger, Rainer; Kaptein, Robert; Hemmings, Andrew; James, Richard; Kleanthous, Colin; Moore, Geoffrey
Citation:

Citation: Whittaker, Sara; Czisch, Michael; Wechselberger, Rainer; Kaptein, Robert; Hemmings, Andrew; James, Richard; Kleanthous, Colin; Moore, Geoffrey. "Slow Conformational Dynamics of an Endonuclease Persist in its Complex with its Natural Protein Inhibitor"  Protein Sci. 9, 713-720 (2000).

Assembly members:

Assembly members:
DNase domain of colicin E9, polymer, 134 residues, 15090 Da.
Immunity protein of colicin E9, polymer, 86 residues, 9582 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: Eschericia coli   Vector: pRJ353

Data typeCount
13C chemical shifts420
15N chemical shifts156
1H chemical shifts472

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E9 DNase1
2Im92

Entities:

Entity 1, E9 DNase 134 residues - 15090 Da.

1   METGLUSERLYSARGASNLYSPROGLYLYS
2   ALATHRGLYLYSGLYLYSPROVALGLYASP
3   LYSTRPLEUASPASPALAGLYLYSASPSER
4   GLYALAPROILEPROASPARGILEALAASP
5   LYSLEUARGASPLYSGLUPHELYSSERPHE
6   ASPASPPHEARGLYSALAVALTRPGLUGLU
7   VALSERLYSASPPROGLULEUSERLYSASN
8   LEUASNPROSERASNLYSSERSERVALSER
9   LYSGLYTYRSERPROPHETHRPROLYSASN
10   GLNGLNVALGLYGLYARGLYSVALTYRGLU
11   LEUHISHISASPLYSPROILESERGLNGLY
12   GLYGLUVALTYRASPMETASPASNILEARG
13   VALTHRTHRPROLYSARGHISILEASPILE
14   HISARGGLYLYS

Entity 2, Im9 86 residues - 9582 Da.

1   METGLULEULYSHISSERILESERASPTYR
2   THRGLUALAGLUPHELEUGLNLEUVALTHR
3   THRILECYSASNALAASPTHRSERSERGLU
4   GLUGLULEUVALLYSLEUVALTHRHISPHE
5   GLUGLUMETTHRGLUHISPROSERGLYSER
6   ASPLEUILETYRTYRPROLYSGLUGLYASP
7   ASPASPSERPROSERGLYILEVALASNTHR
8   VALLYSGLNTRPARGALAALAASNGLYLYS
9   SERGLYPHELYSGLNGLY

Samples:

sample_one: DNase domain of colicin E9, [U-99% 13C; U-99% 15N], 2.0 mM; Immunity protein of colicin E9 2.5 mM; Potassium_phosphate 50.0 mM; H20 90%; D20 10%; Sodium_azide 0.01%

sample_conditions_one: pH: 6.2; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_onenot availablesample_conditions_one
1H-1H-15N NOESY-HSQCsample_onenot availablesample_conditions_one
HNCOsample_onenot availablesample_conditions_one
HNCAsample_onenot availablesample_conditions_one
CBCA(CO)NHsample_onenot availablesample_conditions_one
HBHA(CBCACO)NHsample_onenot availablesample_conditions_one

Software:

FELIX v95.0 - Simultaneous analysis of triple resonance spectra. Very useful for analysing multiple data sets simultaneously.

NMRPipe - Data processing.

XEASY v1.2 - Defining strips for 3D NOESY to aid sequential assignment.

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 600 MHz
  • Varian UNITY 750 MHz

Related Database Links:

BMRB 4293
PDB
EMBL CAA31104 CAA33862
GB ACM07430
PRF 1615299E
REF WP_012644886 WP_044860894 YP_002533537
SP P09883
AlphaFold P09883

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