BMRB Entry 25721

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25721

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Title:
1H, 15n, 13C chemical shifts assignments of VirA DD in complex with VirFGDD
Deposition date:
2015-07-20
Original release date:
2016-11-01
Authors:
Dorival, Jonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira
Citation:

Citation: Dorival, Jonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira. "Characterization of Intersubunit Communication in the Virginiamycin trans-Acyl Transferase Polyketide Synthase"  J. Am. Chem. Soc. 138, 4155-4167 (2016).
PubMed: 26982529

Assembly members:

Assembly members:
VirADD, polymer, 41 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 1961   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces virginiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBG102 (pet27 derivative)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VirADD: GPGSYTGAGEPSQADLDALL SAVRDNRLSIEQAVTLLTPR R

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts43
1H chemical shifts275

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1VirA DD1

Entities:

Entity 1, VirA DD 41 residues - Formula weight is not available

1   GLYPROGLYSERTYRTHRGLYALAGLYGLU
2   PROSERGLNALAASPLEUASPALALEULEU
3   SERALAVALARGASPASNARGLEUSERILE
4   GLUGLNALAVALTHRLEULEUTHRPROARG
5   ARG

Samples:

sample_1: VirADD, [U-100% 13C; U-100% 15N], 1.2 mM; VirFGDD 2.4 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks