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Biological Magnetic Resonance Data Bank


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BMRB Entry 4802

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4802

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Title: 1H, 13C, and 15N sequential assignment of the triple labelled N-terminal domain of the Histone like Nucleoid Structuring protein (H-NS) from Salmonella typhimurium (first 64 residues of the protein)

Deposition date: 2000-08-09 Original release date: 2001-01-23

Authors: Renzoni, Debora; Esposito, Diego; Pfuhl, Mark; Higgins, Christopher; Driscoll, Paul; Ladbury, John

Citation: Renzoni, Debora; Esposito, Diego; Pfuhl, Mark; Higgins, Christopher; Driscoll, Paul; Ladbury, John. "Structural Insight to the Oligomerisation of the Bacterial Chromatin-Structuring Protein H-N"  . ., .-..

Assembly members:
Oligomerisation domain of the 'histone' like nucleoid structuring protein, polymer, 64 residues, 7958 Da.

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

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

Entity Sequences (FASTA):
Oligomerisation domain of the 'histone' like nucleoid structuring protein: SEALKILNNIRTLRAQARES TLETLEEMLEKLEVVVNERR EEESAAAAEVEERTRKLQQY REML

Data sets:
Data typeCount
1H chemical shifts123
13C chemical shifts168
15N chemical shifts62

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H-NS(1-64) monomer 11
2H-NS(1-64) monomer 21
3H-NS(1-64) monomer 31

Entities:

Entity 1, H-NS(1-64) monomer 1 64 residues - 7958 Da.

1   SERGLUALALEULYSILELEUASNASNILE
2   ARGTHRLEUARGALAGLNALAARGGLUSER
3   THRLEUGLUTHRLEUGLUGLUMETLEUGLU
4   LYSLEUGLUVALVALVALASNGLUARGARG
5   GLUGLUGLUSERALAALAALAALAGLUVAL
6   GLUGLUARGTHRARGLYSLEUGLNGLNTYR
7   ARGGLUMETLEU

Samples:

sample_1: Oligomerisation domain of the 'histone' like nucleoid structuring protein, [U-13C; U-15N; U-2H], 1.5 mM

Ex-cond_1: pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-1H NOESYsample_1not availableEx-cond_1
1H-1H TOCSYsample_1not availableEx-cond_1
1H-15N HSQCsample_1not availableEx-cond_1
15N NOESY-HSQCsample_1not availableEx-cond_1
15N TOCSY-HSQCsample_1not availableEx-cond_1
15N-15N HSQC-NOESY-HSQCsample_1not availableEx-cond_1
HNHAsample_1not availableEx-cond_1
13C NOESY-HSQCsample_1not availableEx-cond_1
13C HCCH-TOCSYsample_1not availableEx-cond_1
HNCAsample_1not availableEx-cond_1
HNCOsample_1not availableEx-cond_1
HNCOCAsample_1not availableEx-cond_1
HNCACOsample_1not availableEx-cond_1
HNCACBsample_1not availableEx-cond_1
HNCOCACBsample_1not availableEx-cond_1
HCCH 13C-13C NOEsample_1not availableEx-cond_1
The triple resonance experiments were recorded on triple labelled samples (2H/15N/13C).sample_1not availableEx-cond_1

Software:

NMRPIPE - data processing

AZARA v2.0 -

ANSIG - peak assignment

NMR spectrometers:

  • Varian UNITYplus 500 MHz
  • Varian UNITYplus 600 MHz
  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 18814 5390
PDB
DBJ BAA36117 BAB35162 BAG76811 BAI25048 BAI30173
EMBL CAA30530 CAA31522 CAA32549 CAA40507 CAA42565
GB AAB61148 AAC74319 AAG56094 AAL20669 AAN42850
PIR AC0650
PRF 1607341A
REF NP_287482 NP_309766 NP_415753 NP_455749 NP_460710
SP P09120 P0A1S2 P0A1S3 P0ACF8 P0ACF9

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts