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 25235

Title: The solution structure of the FtsH periplasmic N-domain   PubMed: 25576874

Authors: Scharfenberg, Franka; Serek-Heuberger, Justyna; Martin, Joerg; Lupas, Andrei; Coles, Murray

Citation: Scharfenberg, Franka; Serek-Heuberger, Justyna; Coles, Murray; Hartmann, Marcus; Habeck, Michael; Martin, Joerg; Lupas, Andrei; Alva, Vikram. "Structure and Evolution of N-domains in AAA Metalloproteases"  J. Mol. Biol. 427, 910-923 (2015).

Assembly members:
FtsH-N, polymer, 82 residues, 9545.674 Da.

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):
FtsH-N: MASESNGRKVDYSTFLQEVN NDQVREARINGREINVTKKD SNRYTTYIPVQDPKLLDNLL TKNVKVVGEPPEEPLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts12
15N chemical shifts3
1H chemical shifts19

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1FtsH periplasmic N-domain1

Entities:

Entity 1, FtsH periplasmic N-domain 82 residues - 9545.674 Da.

Residues 97-104 represent a non-native affinity tag, residues 23-24 are a cloning artefact

1   METALASERGLUSERASNGLYARGLYSVAL
2   ASPTYRSERTHRPHELEUGLNGLUVALASN
3   ASNASPGLNVALARGGLUALAARGILEASN
4   GLYARGGLUILEASNVALTHRLYSLYSASP
5   SERASNARGTYRTHRTHRTYRILEPROVAL
6   GLNASPPROLYSLEULEUASPASNLEULEU
7   THRLYSASNVALLYSVALVALGLYGLUPRO
8   PROGLUGLUPROLEUGLUHISHISHISHIS
9   HISHIS

Samples:

15N-labelled: FtsH-N, [U-100% 15N], 0.7 mM; sodium phosphate 15 mM; sodium chloride 75 mM

13C-15N-labelled: FtsH-N, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 15 mM; sodium chloride 75 mM

sample_conditions_1: ionic strength: 0.105 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NH13C-15N-labelledisotropicsample_conditions_1
3D HNCACB13C-15N-labelledisotropicsample_conditions_1
3D HNCO13C-15N-labelledisotropicsample_conditions_1
3D HN(CA)CO13C-15N-labelledisotropicsample_conditions_1
3D C(CO)NH13C-15N-labelledisotropicsample_conditions_1
3D HCCH-TOCSY13C-15N-labelledisotropicsample_conditions_1
3D CCH NOESY13C-15N-labelledisotropicsample_conditions_1
3D CNH NOESY13C-15N-labelledisotropicsample_conditions_1
3D 1H-15N NOESY15N-labelledisotropicsample_conditions_1
3D 1H-13C NOESY13C-15N-labelledisotropicsample_conditions_1
3D HNHA15N-labelledisotropicsample_conditions_1
3D HNHB15N-labelledisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

X-PLOR_NIH v2.9.4, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR-SPIRIT v1.1, In house - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker DMX 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

GB CDL26129.1