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 6533

Title: 1H, 13C, and 15N Chemical Shift Assignments for the DNA binding domain of STPA from E. coli

Deposition date: 2005-03-04 Original release date: 2006-02-23

Authors: Ono, Shusuke; Ladbury, John; Williams, Mark

Citation: Ono, Shusuke; Leonard, Paul; Williams, Mark; Ladbury, John. "Characterization of the bacterial nucleoid protein STPA: Structure, self-association and interaction with H-NS"  The BMRB entry is the only known published source for the data..

Assembly members:
DNA binding domain of STPA, polymer, 44 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Vector: pET14b

Entity Sequences (FASTA):
DNA binding domain of STPA: QPRPAKYKFTDVNGETKTWT GQGRTPKPIAQALAEGKSLD DFLI

Data sets:
Data typeCount
13C chemical shifts198
15N chemical shifts44
1H chemical shifts313

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DNA binidng domain of STPA1

Entities:

Entity 1, DNA binidng domain of STPA 44 residues - Formula weight is not available

Residues 91 to 134 of the DNA packaing protein STPA

1   GLNPROARGPROALALYSTYRLYSPHETHR
2   ASPVALASNGLYGLUTHRLYSTHRTRPTHR
3   GLYGLNGLYARGTHRPROLYSPROILEALA
4   GLNALALEUALAGLUGLYLYSSERLEUASP
5   ASPPHELEUILE

Samples:

sample_1: DNA binding domain of STPA, [U-98% 13C; U-98% 15N], 1.5 ± 0.1 mM; sodium chloride 100 ± 5 mM; sodium phosphate 10 ± 0.5 mM; EDTA 0.1 ± 0.05 mM

conditions_1: pH*: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsample_1not availableconditions_1
1H13C_CT_HSQCsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
C(CO)HNsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
HC(CO)NHsample_1not availableconditions_1
HBCDsample_1not availableconditions_1
1H15N_TOCSY_HSQCsample_1not availableconditions_1
1H15N_NOESY_HSQCsample_1not availableconditions_1

Software:

NMRPipe v2.1, Frank Delaglio, NIH - spectral processing

ANSIG v3.3, University of Cambridge - spectral visualisation

NMR spectrometers:

  • Varian Unity Plus 600 MHz
  • Varian Unity Plus 500 MHz

Related Database Links:

BMRB 18400
PDB
DBJ BAA16535 BAB36953 BAG78446 BAI26931 BAI31961
EMBL CAA49146 CAP77108 CAQ33006 CAQ87964 CAQ99591
GB AAA64940 AAC75716 AAG57777 AAN44190 AAN81670
REF NP_289219 NP_311557 NP_417155 NP_708483 NP_755100
SP P0ACG1 P0ACG2 P0ACG3
AlphaFold P0ACG2 P0ACG1 P0ACG3

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