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PDB ID: 2l55
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17266
MolProbity Validation Chart
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Bersch, Beate; Derfoufi, Kheiro-Mouna; De Angelis, Fabien; Auquier, Vanessa; Ngonlong Ekende, Elisabeth; Mergeay, Max; Ruysschaert, Jean-Marie; Vandenbussche, Guy. "Structural and Metal Binding Characterization of the C-Terminal Metallochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34." Biochemistry 50, 2194-2204 (2011).
PubMed: 21299248
Assembly members:
SilB(440-521), polymer, 82 residues, 8540.854 Da.
Natural source: Common Name: Cupriavidus metallidurans Taxonomy ID: not available Superkingdom: Bacteria Kingdom: not available Genus/species: Cupriavidus metallidurans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30b
Entity Sequences (FASTA):
SilB(440-521): GPEHRAVGRIQSIGERSLII
AHEAIPSAQWGAMTMEFAAP
PAGLPQGLKAGDRVAFSFRL
DPHGMATLVTVAPQVQTAGA
KP
Data type | Count |
13C chemical shifts | 335 |
15N chemical shifts | 89 |
1H chemical shifts | 545 |
heteronuclear NOE values | 68 |
T1 relaxation values | 64 |
T2 relaxation values | 66 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SilB(440-521) | 1 |
Entity 1, SilB(440-521) 82 residues - 8540.854 Da.
residues 440 to 521 in the unprocessed protein sequence have been renumbered from 1 to 82 in this pdb entry and associated data
1 | GLY | PRO | GLU | HIS | ARG | ALA | VAL | GLY | ARG | ILE | ||||
2 | GLN | SER | ILE | GLY | GLU | ARG | SER | LEU | ILE | ILE | ||||
3 | ALA | HIS | GLU | ALA | ILE | PRO | SER | ALA | GLN | TRP | ||||
4 | GLY | ALA | MET | THR | MET | GLU | PHE | ALA | ALA | PRO | ||||
5 | PRO | ALA | GLY | LEU | PRO | GLN | GLY | LEU | LYS | ALA | ||||
6 | GLY | ASP | ARG | VAL | ALA | PHE | SER | PHE | ARG | LEU | ||||
7 | ASP | PRO | HIS | GLY | MET | ALA | THR | LEU | VAL | THR | ||||
8 | VAL | ALA | PRO | GLN | VAL | GLN | THR | ALA | GLY | ALA | ||||
9 | LYS | PRO |
PDB | 2L55 |
EMBL | CAI11314 |
GB | ABF12994 ELA00440 |
REF | WP_008642712 WP_011229392 WP_017510653 YP_145665 |
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