BMRB Entry 16863

Title:
1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis
Deposition date:
2010-04-13
Original release date:
2010-06-15
Authors:
Hynson, Robert; Kwan, Ann; Jacques, David; Mackay, Joel; Trewhella, Jill
Citation:

Citation: Hynson, Robert; Kwan, Ann; Jacques, David; Mackay, Joel; Trewhella, Jill. "1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis."  Biomol. NMR Assignments 4, 167-169 (2010).
PubMed: 20524093

Assembly members:

Assembly members:
KipI-N, polymer, 101 residues, 11.55 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32a

Data sets:
Data typeCount
13C chemical shifts394
15N chemical shifts111
1H chemical shifts704

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KipI-N1

Entities:

Entity 1, KipI-N 101 residues - 11.55 Da.

GS at the beginning of the sequence is the remaining part of the tag that was cleaved off.

1   GLYSERMETTHRVALARGTYRGLNILEGLU
2   GLNLEUGLYASPSERALAMETMETILEARG
3   PHEGLYGLUGLUILEASNGLUGLNVALASN
4   GLYILEVALHISALAALAALAALATYRILE
5   GLUGLUGLNPROPHEPROGLYPHEILEGLU
6   CYSILEPROALAPHETHRSERLEUTHRVAL
7   PHETYRASPMETTYRGLUVALTYRLYSHIS
8   LEUPROGLNGLYILESERSERPROPHEGLU
9   SERVALLYSARGASPVALGLUGLUARGLEU
10   ALAGLUILEALAGLUASPTYRGLUVALASN
11   ARG

Samples:

sample_1: KipI-N, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM

sample_2: KipI-N, [U-100% 15N], 1 mM; sodium phosphate 20 mM

sample_3: KipI-N 1 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NH TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
3D 1H-1H TOCSYsample_1isotropicsample_conditions_1
HBCBCGCEHEsample_1isotropicsample_conditions_1
HBCBCGCDHDsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1-2.5, Bruker Biospin - collection, data analysis

SPARKY, Goddard - chemical shift assignment, data analysis

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA07361 BAA09039 BAI83890 BAM49343 BAM56613
EMBL CAB12216 CCU59687 CEI55532 CEJ75957 CJR85854
GB ADV95341 AEP89488 AFI26965 AFQ56347 AGA23688
PRF 2208409M
REF NP_388290 WP_003234420 WP_014475832 WP_014478855 WP_014662801
SP P60495
AlphaFold P60495

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