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Biological Magnetic Resonance Data Bank


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BMRB Entry 30094

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PDB ID:
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
MolProbity Validation Chart

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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

Data sets:
Data typeCount
13C chemical shifts377
15N chemical shifts101
1H chemical shifts539

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain 11
2entity_1, chain 21

Entities:

Entity 1, entity_1, chain 1 131 residues - 14022.842 Da.

1   METALAASNLYSPROMETGLNPROILETHR
2   SERTHRALAASNLYSILEVALTRPSERASP
3   PROTHRARGLEUSERTHRTHRPHESERALA
4   SERLEULEUARGGLNARGVALLYSVALGLY
5   ILEALAGLULEUASNASNVALSERGLYGLN
6   TYRVALSERVALTYRLYSARGPROALAPRO
7   LYSPROGLUGLYCYSALAASPALACYSVAL
8   ILEMETPROASNGLUASNGLNSERILEARG
9   THRVALILESERGLYSERALAGLUASNLEU
10   ALATHRLEULYSALAGLUTRPGLUTHRHIS
11   LYSARGASNVALASPTHRLEUPHEALASER
12   GLYASNALAGLYLEUGLYPHELEUASPPRO
13   THRALAALAILEVALSERSERASPTHRTHR
14   ALA

Samples:

sample_1: AP205 coat protein, [U-100% 13C; U-100% 15N], 500 ± 200 mg/mL; HEPES 5 ± 1 mM; PEG, [U-2H], 15 ± 5 %; sodium chloride 50 ± 5 mM

sample_conditions_1: ionic strength: 0.055 M; pH: 7.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D HhNHsample_1isotropicsample_conditions_1
3D HhCHsample_1isotropicsample_conditions_1
3D HcCH-TOCSYsample_1isotropicsample_conditions_1
3D hCCH-TOCSYsample_1isotropicsample_conditions_1
3D hNCAHsample_1isotropicsample_conditions_1
3D hNcoCAHsample_1isotropicsample_conditions_1
3D hCOCAHsample_1isotropicsample_conditions_1
3D hCANHsample_1isotropicsample_conditions_1
3D hCOnCAHsample_1isotropicsample_conditions_1
3D hcoCAcoNHsample_1isotropicsample_conditions_1

Software:

CARA v1.9, Keller and Wuthrich - chemical shift assignment

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.5, Bruker Biospin - collection, processing

UNIO v2.6, Torsten Herrmann et al. - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 1000 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts