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 15489

Title: Chemical shift assignments of paenibacillin -- a novel lantibiotic with N-terminal acetylation   PubMed: 18625234

Deposition date: 2007-09-25 Original release date: 2008-07-29

Authors: He, Zengguo; Yuan, Chunhua; Zhang, Liwen; Yousef, Ahmed

Citation: He, Zengguo; Yuan, Chunhua; Zhang, Liwen; Yousef, Ahmed. "N-terminal acetylation in paenibacillin, a novel lantibiotic"  FEBS Lett. 582, 2787-2792 (2008).

Assembly members:
paenibacillin, polymer, 30 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

Experimental source:   Production method: purified from the natural source   Host organism: Saccharomyces cerevisiae

Entity Sequences (FASTA):
paenibacillin: XXIIKXXIKVXKAVXKXLXX IXXGXXXNXK

Data sets:
Data typeCount
1H chemical shifts197
13C chemical shifts114
15N chemical shifts30

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1paenibacillin1

Entities:

Entity 1, paenibacillin 30 residues - Formula weight is not available

1   AYADHAXILEILELYSDHBXDHBXILELYSVAL
2   ALASLYSALAVALALASLYSABUXLEUABUXALAS
3   ILEALASABUXGLYALASALASDHAXASNALASLYS

Samples:

sample_1: paenibacillin 0.67 mM; D2O 100%

sample_2: paenibacillin 2.89 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 mM; pH: 4.5; pressure: 1 atm; temperature: 293.9 K

sample_conditions_2: ionic strength: 0.1 mM; pH: 4.5; pressure: 1 atm; temperature: 287.3 K

sample_conditions_3: ionic strength: 0.1 mM; pH: 4.5; pressure: 1 atm; temperature: 301.8 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HMBCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_3
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_3
2D 1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC-NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HMBCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_3
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC-ROESYsample_1isotropicsample_conditions_1
2D 1H-1H ROESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection, data analysis

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DRX 800 MHz

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