BMRB Entry 4047

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4047

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Title:
1H, 13C, 15N Resonance Assignments and Secondary Structure Analysis of the HU Protein from Bacillus stearothermophilus Using Two- and Three- Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy
Deposition date:
1997-07-27
Original release date:
1999-08-18
Authors:
Vis, Hans; Boelens, Rolf; Mariani, Matteo; Stroop, Ralf; Vorgias, Constantin; Wilson, Keith; Kaptein, Robert
Citation:

Citation: Vis, Hans; Boelens, Rolf; Mariani, Matteo; Stroop, Ralf; Vorgias, Constantin; Wilson, Keith; Kaptein, Robert. "1H, 13C, 15N Resonance Assignments and Secondary Structure Analysis of the HU Protein from Bacillus stearothermophilus Using Two- and Three- Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy "  Biochemistry 33, 14858-14870 (1994).

Assembly members:

Assembly members:
HU protein, polymer, 90 residues, 19500 Da.

Natural source:

Natural source:   Common Name: B. stearothermophilus   Taxonomy ID: 1422   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Bacillus stearothermophilus

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HU protein: MNKTELINAVAETSGLSKKD ATKAVDAVFDSITEALRKGD KVQLIGFGNFEVRERAARKG RNPQTGEEMEIPASKVPAFK PGKALKDAVK

Data sets:
Data typeCount
1H chemical shifts639
13C chemical shifts418
15N chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HUBst1

Entities:

Entity 1, HUBst 90 residues - 19500 Da.

1   METASNLYSTHRGLULEUILEASNALAVAL
2   ALAGLUTHRSERGLYLEUSERLYSLYSASP
3   ALATHRLYSALAVALASPALAVALPHEASP
4   SERILETHRGLUALALEUARGLYSGLYASP
5   LYSVALGLNLEUILEGLYPHEGLYASNPHE
6   GLUVALARGGLUARGALAALAARGLYSGLY
7   ARGASNPROGLNTHRGLYGLUGLUMETGLU
8   ILEPROALASERLYSVALPROALAPHELYS
9   PROGLYLYSALALEULYSASPALAVALLYS

Samples:

sample_one: HU protein, [U-13C; U-15N], 2.2 mM; D2O 5%; H2O 95%; Phosphate buffer 50 mM; KCL 200 mM

sample_conditions_one: pH: 4.6 na; temperature: 311 K

Experiments:

NameSampleSample stateSample conditions

Software:

No software information available

NMR spectrometers:

  • Bruker AMX600 600 MHz

Related Database Links:

PDB
DBJ BAA07273 BAD76500 GAD12440 GAJ40216 GAJ58439
GB AAA22532 AAA22533 AAA22534 ABO67501 ACS24864
PRF 2106156A
REF WP_015864289 WP_017436779 WP_020755319 WP_033013995 WP_044731005
SP P0A3H0 P0A3H1 P0A3H2
AlphaFold P0A3H0 P0A3H1 P0A3H2

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