BMRB Entry 4528

Title:
1H, 13C, and 15N Chemical Shift Assignments for the N-terminal receiver domain of NtrC (phosphorylated)
Deposition date:
1999-11-05
Original release date:
2000-06-16
Authors:
Kern, D.; Volkman, B.; Luginbuhl, P.; Nohaile, M.; Kustu, S.; Wemmer, D.
Citation:

Citation: Kern, D.; Volkman, B.; Luginbuhl, P.; Nohaile, M.; Kustu, S.; Wemmer, D.. "Structure of a Transiently Phosphorylated "Switch" in Bacterial Signal Transduction"  Nature 402, 894-898 (1999).

Assembly members:

Assembly members:
NITROGEN REGULATION PROTEIN, polymer, 124 residues, Formula weight is not available
PO4, non-polymer, 94.971 Da.

Natural source:

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 602   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

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

Data sets:
Data typeCount
1H chemical shifts750
13C chemical shifts363
15N chemical shifts113

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P-NtrCr1
2PO42

Entities:

Entity 1, P-NtrCr 124 residues - Formula weight is not available

1   METGLNARGGLYILEVALTRPVALVALASP
2   ASPASPSERSERILEARGTRPVALLEUGLU
3   ARGALALEUALAGLYALAGLYLEUTHRCYS
4   THRTHRPHEGLUASNGLYASNGLUVALLEU
5   ALAALALEUALASERLYSTHRPROASPVAL
6   LEULEUSERASPILEARGMETPROGLYMET
7   ASPGLYLEUALALEULEULYSGLNILELYS
8   GLNARGHISPROMETLEUPROVALILEILE
9   METTHRALAHISSERASPLEUASPALAALA
10   VALSERALATYRGLNGLNGLYALAPHEASP
11   TYRLEUPROLYSPROPHEASPILEASPGLU
12   ALAVALALALEUVALGLUARGALAILESER
13   HISTYRGLNGLU

Entity 2, PO4 - O4 P - 94.971 Da.

1   PO4

Samples:

sample_1: NITROGEN REGULATION PROTEIN, [U-15N], 0.3 mM; Na phosphate 200 mM; MgCl2 50 mM; Carbamoylphosphate 200 mM

sample_2: NITROGEN REGULATION PROTEIN, [U-15N; U-13C], 0.3 mM; Na phosphate 200 mM; MgCl2 50 mM; Carbamoylphosphate 200 mM

sample_cond_1: pH: 6.75; temperature: 298 K; ionic strength: 375 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 15N-SEPARATED_NOESYnot availablenot availablesample_cond_1
3D 13C-SEPARATED_NOESYnot availablenot availablesample_cond_1
2D NOESYnot availablenot availablesample_cond_1

Software:

DYANA v1.5 - STRUCTURE SOLUTION, DATA ANALYSIS

FELIX v95.0 - PROCESSING

XWINNMR v1.5 - COLLECTION

XEASY v1.3.13 - DATA ANALYSIS

NMR spectrometers:

  • Bruker DMX 750 MHz

Related Database Links:

BMRB 25124 25125 4527
PDB
DBJ BAB38213 BAE77441 BAG79675 BAI27885 BAI33008
EMBL CAA28808 CAA59425 CAD03095 CAP78325 CAQ34219
GB AAB03002 AAC76865 AAG59057 AAL22844 AAN45373
PIR AC0950 E86074
REF NP_312817 NP_418304 NP_458044 NP_462885 NP_709666
SP P0AFB8 P0AFB9 P41789
AlphaFold P41789 P0AFB9 P0AFB8

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