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PDB ID: 2mzw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25504
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Tomlinson, Jennifer; Thompson, Gary; Kalverda, Arnout; Zhuravleva, Anastasia; O'Neill, Alex. "A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance" Sci. Rep. 6, 19524-19524 (2016).
PubMed: 26781961
Assembly members:
EF-GC3, polymer, 292 residues, 32272.721 Da.
FusB, polymer, 233 residues, 25225.330 Da.
entity_ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-29b
Entity Sequences (FASTA):
EF-GC3: MEFPEPVIHLSVEPKSKADQ
DKMTQALVKLQEEDPTFHAH
TDEETGQVIIGGMGELHLDI
LVDRMKKEFNVECNVGAPMV
SYRETFKSSAQVQGKFSRQS
GGRGQYGDVHIEFTPNETGA
GFEFENAIVGGVVPREYIPS
VEAGLKDAMENGVLAGYPLI
DVKAKLYDGSYHDVDSSEMA
FKIAASLALKEAAKKCDPVI
LEPMMKVTIEMPEEYMGDIM
GDVTSRRGRVDGMEPRGNAQ
VVNAYVPLSEMFGYATSLRS
NTQGRGTYTMYFDHYAEVPK
SIAEDIIKKNKG
FusB: MGSSHHHHHHSSGLVPNGSH
MKTMIYPHQYNYIRSVILRL
KNVYKTVNDKETVKVIQSET
YNDINEIFGHIDDDIEESLK
VLMNIRLSNKEIEAILNKFL
EYVVPFELPSPQKLQKVFKK
VKKIKIPQFEEYDLKVSSFV
GWNELASNRKYIIYYDEKKQ
LKGLYGEISNQVVKGFCTIC
NKESNVSLFMKKSKTNSDGQ
YVKKGDYICRDSIHCNKQLT
DINQFYNFIDKLD
Data type | Count |
13C chemical shifts | 246 |
15N chemical shifts | 283 |
1H chemical shifts | 283 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EF-GC3 | 1 |
2 | FusB | 2 |
3 | ZINC ION | 3 |
Entity 1, EF-GC3 292 residues - 32272.721 Da.
This is a truncated form of the protein comprising domains III-V and beginning at residue 401 of full length EF-G. Residues 694-701 represent a non-native affinity tag.
1 | MET | GLU | PHE | PRO | GLU | PRO | VAL | ILE | HIS | LEU | ||||
2 | SER | VAL | GLU | PRO | LYS | SER | LYS | ALA | ASP | GLN | ||||
3 | ASP | LYS | MET | THR | GLN | ALA | LEU | VAL | LYS | LEU | ||||
4 | GLN | GLU | GLU | ASP | PRO | THR | PHE | HIS | ALA | HIS | ||||
5 | THR | ASP | GLU | GLU | THR | GLY | GLN | VAL | ILE | ILE | ||||
6 | GLY | GLY | MET | GLY | GLU | LEU | HIS | LEU | ASP | ILE | ||||
7 | LEU | VAL | ASP | ARG | MET | LYS | LYS | GLU | PHE | ASN | ||||
8 | VAL | GLU | CYS | ASN | VAL | GLY | ALA | PRO | MET | VAL | ||||
9 | SER | TYR | ARG | GLU | THR | PHE | LYS | SER | SER | ALA | ||||
10 | GLN | VAL | GLN | GLY | LYS | PHE | SER | ARG | GLN | SER | ||||
11 | GLY | GLY | ARG | GLY | GLN | TYR | GLY | ASP | VAL | HIS | ||||
12 | ILE | GLU | PHE | THR | PRO | ASN | GLU | THR | GLY | ALA | ||||
13 | GLY | PHE | GLU | PHE | GLU | ASN | ALA | ILE | VAL | GLY | ||||
14 | GLY | VAL | VAL | PRO | ARG | GLU | TYR | ILE | PRO | SER | ||||
15 | VAL | GLU | ALA | GLY | LEU | LYS | ASP | ALA | MET | GLU | ||||
16 | ASN | GLY | VAL | LEU | ALA | GLY | TYR | PRO | LEU | ILE | ||||
17 | ASP | VAL | LYS | ALA | LYS | LEU | TYR | ASP | GLY | SER | ||||
18 | TYR | HIS | ASP | VAL | ASP | SER | SER | GLU | MET | ALA | ||||
19 | PHE | LYS | ILE | ALA | ALA | SER | LEU | ALA | LEU | LYS | ||||
20 | GLU | ALA | ALA | LYS | LYS | CYS | ASP | PRO | VAL | ILE | ||||
21 | LEU | GLU | PRO | MET | MET | LYS | VAL | THR | ILE | GLU | ||||
22 | MET | PRO | GLU | GLU | TYR | MET | GLY | ASP | ILE | MET | ||||
23 | GLY | ASP | VAL | THR | SER | ARG | ARG | GLY | ARG | VAL | ||||
24 | ASP | GLY | MET | GLU | PRO | ARG | GLY | ASN | ALA | GLN | ||||
25 | VAL | VAL | ASN | ALA | TYR | VAL | PRO | LEU | SER | GLU | ||||
26 | MET | PHE | GLY | TYR | ALA | THR | SER | LEU | ARG | SER | ||||
27 | ASN | THR | GLN | GLY | ARG | GLY | THR | TYR | THR | MET | ||||
28 | TYR | PHE | ASP | HIS | TYR | ALA | GLU | VAL | PRO | LYS | ||||
29 | SER | ILE | ALA | GLU | ASP | ILE | ILE | LYS | LYS | ASN | ||||
30 | LYS | GLY |
Entity 2, FusB 233 residues - 25225.330 Da.
Residues -19-0 represent a non-native affinity tag.
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
2 | SER | SER | GLY | LEU | VAL | PRO | ASN | GLY | SER | HIS | ||||
3 | MET | LYS | THR | MET | ILE | TYR | PRO | HIS | GLN | TYR | ||||
4 | ASN | TYR | ILE | ARG | SER | VAL | ILE | LEU | ARG | LEU | ||||
5 | LYS | ASN | VAL | TYR | LYS | THR | VAL | ASN | ASP | LYS | ||||
6 | GLU | THR | VAL | LYS | VAL | ILE | GLN | SER | GLU | THR | ||||
7 | TYR | ASN | ASP | ILE | ASN | GLU | ILE | PHE | GLY | HIS | ||||
8 | ILE | ASP | ASP | ASP | ILE | GLU | GLU | SER | LEU | LYS | ||||
9 | VAL | LEU | MET | ASN | ILE | ARG | LEU | SER | ASN | LYS | ||||
10 | GLU | ILE | GLU | ALA | ILE | LEU | ASN | LYS | PHE | LEU | ||||
11 | GLU | TYR | VAL | VAL | PRO | PHE | GLU | LEU | PRO | SER | ||||
12 | PRO | GLN | LYS | LEU | GLN | LYS | VAL | PHE | LYS | LYS | ||||
13 | VAL | LYS | LYS | ILE | LYS | ILE | PRO | GLN | PHE | GLU | ||||
14 | GLU | TYR | ASP | LEU | LYS | VAL | SER | SER | PHE | VAL | ||||
15 | GLY | TRP | ASN | GLU | LEU | ALA | SER | ASN | ARG | LYS | ||||
16 | TYR | ILE | ILE | TYR | TYR | ASP | GLU | LYS | LYS | GLN | ||||
17 | LEU | LYS | GLY | LEU | TYR | GLY | GLU | ILE | SER | ASN | ||||
18 | GLN | VAL | VAL | LYS | GLY | PHE | CYS | THR | ILE | CYS | ||||
19 | ASN | LYS | GLU | SER | ASN | VAL | SER | LEU | PHE | MET | ||||
20 | LYS | LYS | SER | LYS | THR | ASN | SER | ASP | GLY | GLN | ||||
21 | TYR | VAL | LYS | LYS | GLY | ASP | TYR | ILE | CYS | ARG | ||||
22 | ASP | SER | ILE | HIS | CYS | ASN | LYS | GLN | LEU | THR | ||||
23 | ASP | ILE | ASN | GLN | PHE | TYR | ASN | PHE | ILE | ASP | ||||
24 | LYS | LEU | ASP |
Entity 3, ZINC ION - Zn - 65.409 Da.
1 | ZN |
NCBI | P68790 YP_009078429 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks