BMRB Entry 25235
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25235
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Title: The solution structure of the FtsH periplasmic N-domain PubMed: 25576874
Deposition date: 2014-09-18 Original release date: 2015-01-27
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
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 12 |
15N chemical shifts | 3 |
1H chemical shifts | 19 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | FtsH periplasmic N-domain | 1 |
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 | MET | ALA | SER | GLU | SER | ASN | GLY | ARG | LYS | VAL | ||||
2 | ASP | TYR | SER | THR | PHE | LEU | GLN | GLU | VAL | ASN | ||||
3 | ASN | ASP | GLN | VAL | ARG | GLU | ALA | ARG | ILE | ASN | ||||
4 | GLY | ARG | GLU | ILE | ASN | VAL | THR | LYS | LYS | ASP | ||||
5 | SER | ASN | ARG | TYR | THR | THR | TYR | ILE | PRO | VAL | ||||
6 | GLN | ASP | PRO | LYS | LEU | LEU | ASP | ASN | LEU | LEU | ||||
7 | THR | LYS | ASN | VAL | LYS | VAL | VAL | GLY | GLU | PRO | ||||
8 | PRO | GLU | GLU | PRO | LEU | GLU | HIS | HIS | HIS | HIS | ||||
9 | HIS | HIS |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D CBCA(CO)NH | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D HNCACB | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D HNCO | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D HN(CA)CO | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D C(CO)NH | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D CCH NOESY | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D CNH NOESY | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | 15N-labelled | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | 13C-15N-labelled | isotropic | sample_conditions_1 |
3D HNHA | 15N-labelled | isotropic | sample_conditions_1 |
3D HNHB | 15N-labelled | isotropic | sample_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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts