BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25706

Title: 1H, 13C, and 15N Chemical Shift Assignments of PKS domains   PubMed: 26982529

Deposition date: 2015-07-14 Original release date: 2016-03-21

Authors: Dorival, Gonathan; Annaval, Thibault; Risser, Fanny; Collin, Sabrina; Roblin, Pierre; Jacob, Christophe; Gruez, Arnaud; Chagot, Benjamin; Weissman, Kira

Citation: Dorival, Gonathan; 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).

Assembly members:
entity, polymer, 84 residues, 8455.489 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GPGSYTGAGEPSQADLDALL SAVRDNRLSIEQAVTLLTPR RGGGSGGGSMDAKEILTRFK DGGLDRAAAQALLAGRTPAA APRP

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts80
1H chemical shifts518

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 84 residues - 8455.489 Da.

Residues 1-5 represent a non-native affinity tag. Residues 6-41 is from VirA protein. Residues 42-49 is an non-native fusion linker. Residues 50-88 is from VirFG protein.

1   GLYPROGLYSERTYRTHRGLYALAGLYGLU
2   PROSERGLNALAASPLEUASPALALEULEU
3   SERALAVALARGASPASNARGLEUSERILE
4   GLUGLNALAVALTHRLEULEUTHRPROARG
5   ARGGLYGLYGLYSERGLYGLYGLYSERMET
6   ASPALALYSGLUILELEUTHRARGPHELYS
7   ASPGLYGLYLEUASPARGALAALAALAGLN
8   ALALEULEUALAGLYARGTHRPROALAALA
9   ALAPROARGPRO

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 100 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
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin - collection

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.115, Goddard - chemical shift assignment

AMBER v14, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

ProcheckNMR, Laskowski and MacArthur - data analysis

TALOS v+, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GB BAF50727.1

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