BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18814

Title: 13C and 15N NMR chemical shifts of E. coli full-length H-NS protein   PubMed: 23601147

Authors: Renault, Marie; Garcia, Jesus; Cordeiro, Tiago; Baldus, Marc; Pons, Miquel

Citation: Renault, Marie; Garcia, Jesus; Cordeiro, Tiago; Baldus, Marc; Pons, Miquel. "Protein oligomers studied by solid-state NMR--the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein."  FEBS J. 280, 2916-2928 (2013).

Assembly members:
H-NS, polymer, 137 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
H-NS: MSEALKILNNIRTLRAQARE CTLETLEEMLEKLEVVVNER REEESAAAAEVEERTRKLQQ YREMLIADGIDPNELLNSLA AVKSGTKAKRAQRPAKYSYV DENGETKTWTGQGRTPAVIK KAMDEQGKSLDDFLIKQ

Data sets:
Data typeCount
13C chemical shifts155
15N chemical shifts7

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H-NS 1-1371

Entities:

Entity 1, H-NS 1-137 137 residues - Formula weight is not available

1   METSERGLUALALEULYSILELEUASNASN
2   ILEARGTHRLEUARGALAGLNALAARGGLU
3   CYSTHRLEUGLUTHRLEUGLUGLUMETLEU
4   GLULYSLEUGLUVALVALVALASNGLUARG
5   ARGGLUGLUGLUSERALAALAALAALAGLU
6   VALGLUGLUARGTHRARGLYSLEUGLNGLN
7   TYRARGGLUMETLEUILEALAASPGLYILE
8   ASPPROASNGLULEULEUASNSERLEUALA
9   ALAVALLYSSERGLYTHRLYSALALYSARG
10   ALAGLNARGPROALALYSTYRSERTYRVAL
11   ASPGLUASNGLYGLUTHRLYSTHRTRPTHR
12   GLYGLNGLYARGTHRPROALAVALILELYS
13   LYSALAMETASPGLUGLNGLYLYSSERLEU
14   ASPASPPHELEUILELYSGLN

Samples:

H-NS_(1-137): H-NS, [U-100% 13C; U-100% 15N], 10 mg

H-NS_(1-47): H-NS, [U-100% 13C; U-100% 15N], 15 mg

sample_conditions_1: ionic strength: 0.25 M; pH: 7.0; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C PDSDH-NS_(1-47)solidsample_conditions_1
2D 15N-13C NCACXH-NS_(1-47)solidsample_conditions_1
2D 15N-13C NCOCXH-NS_(1-47)solidsample_conditions_1
2D 13C-13C PDSDH-NS_(1-137)solidsample_conditions_1
2D 15N-13C NCACXH-NS_(1-137)solidsample_conditions_1
2D 15N-13C NCOCXH-NS_(1-137)solidsample_conditions_1
3D 15N-13C-13C NCOCXH-NS_(1-137)solidsample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

DBJ BAA36117 BAB35162 BAG76811 BAI25048 BAI30173
EMBL CAA30530 CAA31522 CAA40507 CAA42565 CAA47322
GB AAC74319 AAG56094 AAN42850 AAN80168 AAP16735
PRF 1607341A
REF NP_309766 NP_415753 NP_707143 WP_000004409 WP_000330568
SP P09120 P0ACF8 P0ACF9 P0ACG0