BMRB Entry 15008

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15008

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Title:
Backbone and Side Chain 1H, 13C and 15N Chemical Shift Assignments for Sporulation Phosphotransferase F Mutant H101A
Deposition date:
2006-11-01
Original release date:
2007-05-09
Authors:
McLaughlin, Patrick; Bobay, Benjamin; Regel, Erin; Thompson, Richele; Hoch, James; Cavanagh, John
Citation:

Citation: McLaughlin, Patrick; Bobay, Benjamin; Regel, Erin; Thompson, Richele; Hoch, James; Cavanagh, John. "Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition"  FEBS Lett. 581, 1425-1429 (2007).
PubMed: 17350627

Assembly members:

Assembly members:
Spo0FH101A, polymer, 132 residues, Formula weight is not available

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: pET23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Spo0FH101A: MMNEKILIVDDQYGIRILLN EVFNKEGYQTFQAANGLQAL DIVTKERPDLVLLDMKIPGM DGIEILKRMKVIDENIRVII MTAYGELDMIQESKELGALT AFAKPFDIDEIRDAVKKYLP LKSNLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts519
15N chemical shifts127
1H chemical shifts746

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Spo0FH101A monomer1

Entities:

Entity 1, Spo0FH101A monomer 132 residues - Formula weight is not available

1   METMETASNGLULYSILELEUILEVALASP
2   ASPGLNTYRGLYILEARGILELEULEUASN
3   GLUVALPHEASNLYSGLUGLYTYRGLNTHR
4   PHEGLNALAALAASNGLYLEUGLNALALEU
5   ASPILEVALTHRLYSGLUARGPROASPLEU
6   VALLEULEUASPMETLYSILEPROGLYMET
7   ASPGLYILEGLUILELEULYSARGMETLYS
8   VALILEASPGLUASNILEARGVALILEILE
9   METTHRALATYRGLYGLULEUASPMETILE
10   GLNGLUSERLYSGLULEUGLYALALEUTHR
11   ALAPHEALALYSPROPHEASPILEASPGLU
12   ILEARGASPALAVALLYSLYSTYRLEUPRO
13   LEULYSSERASNLEUGLUHISHISHISHIS
14   HISHIS

Samples:

sample_1: Spo0FH101A, [U-99% 13C; U-99% 15N], 1.0 – 2.0 mM; TRIS, none, 25 mM; potassium chloride, none, 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

NMRView v5, B Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15009 15010 15011
PDB
DBJ BAI87374 BAM55796 BAM59808 GAK81027
EMBL CAA27217 CAA89872 CAB15730 CCU60811 CEI59521
GB AAA16802 AAA22787 ADM39703 ADP34224 ADV94523
PRF 1306301A
REF NP_391594 WP_003221952 WP_003227621 WP_003326524 WP_010328945
SP P06628
AlphaFold P06628

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