BMRB Entry 30094
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PDB ID: 5jzr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30094
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Title: Solid-state MAS NMR structure of Acinetobacter phage 205 (AP205) coat protein in assembled capsid particles PubMed: 27489348
Deposition date: 2016-05-17 Original release date: 2016-08-08
Authors: Jaudzems, K.; Andreas, L.; Stanek, J.; Lalli, D.; Bertarello, A.; Le Marchand, T.; Cala-De Paepe, D.; Kotelovica, S.; Akopjana, I.; Knott, B.; Wegner, S.; Engelke, F.; Lesage, A.; Emsley, L.; Tars, K.; Herrmann, T.; Pintacuda, G.
Citation: Andreas, Loren; Jaudzems, Kristaps; Stanek, Jan; Lalli, Daniela; Bertarello, Andrea; Marchand, Tanguy; Paepe, Diane; Kotelovica, Svetlana; Akopjana, Inara; Knott, Benno; Wegner, Sebastian; Engelke, Frank; Lesage, Anne; Emsley, Lyndon; Tars, Kaspars; Herrmann, Torsten; Pintacuda, Guido. "Structure of fully protonated proteins by proton-detected magic-angle spinning NMR" Proc. Natl. Acad. Sci. U. S. A. 113, 9187-9192 (2016).
Assembly members:
Coat protein, polymer, 131 residues, 14022.842 Da.
Natural source: Common Name: Acinetobacter phage AP205 Taxonomy ID: 154784 Superkingdom: Viruses Kingdom: Levivirus Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Coat protein: MANKPMQPITSTANKIVWSD
PTRLSTTFSASLLRQRVKVG
IAELNNVSGQYVSVYKRPAP
KPEGCADACVIMPNENQSIR
TVISGSAENLATLKAEWETH
KRNVDTLFASGNAGLGFLDP
TAAIVSSDTTA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 377 |
15N chemical shifts | 101 |
1H chemical shifts | 539 |
Additional metadata:
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