BMRB Entry 25235

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PDB ID: 2muy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25235
MolProbity Validation Chart

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Title:
The solution structure of the FtsH periplasmic N-domain
Deposition date:
2014-09-18
Original release date:
2015-01-27
Authors:
Scharfenberg, Franka; Serek-Heuberger, Justyna; Martin, Joerg; Lupas, Andrei; Coles, Murray
Citation:

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).
PubMed: 25576874

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

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:

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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

Related Database Links:

GB CDL26129.1

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