BMRB Entry 50088

Title:
Structure and function of the bacterial toxin phenomycin
Deposition date:
2019-11-14
Original release date:
2020-01-10
Authors:
Nielsen, Jakob
Citation:

Citation: Hansen, Bente; Larsen, Camilla; Nielsen, Jakob; Svenningsen, Esben; Van, Lan; Jacobsen, Kristian; Bjerring, Morten; Flygaard, Rasmus; Jenner, Lasse; Nejsum, Lene; Brodersen, Ditlev; Mulder, Frans; Tyrring, Thomas; Poulsen, Thomas. "Structure and Function of the Bacterial Protein Toxin Phenomycin"  Structure 28, 528-539 (2020).
PubMed: 32220302

Assembly members:

Assembly members:
Phenomycin, polymer, 93 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Streptomyces fervens MA 564-Cl   Taxonomy ID: 66429   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces fervens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM11

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts99
1H chemical shifts619

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Phenomycin1

Entities:

Entity 1, Phenomycin 93 residues - Formula weight is not available

1   GLYALAMETALAASNPROLYSTHRILELYS
2   ALAALAALATYRASNGLNALAARGSERTHR
3   LEUALAASPALAGLYSERARGTHRALAALA
4   LYSSERHISPROILEHISGLYLYSTHRASP
5   VALPROVALSERTYRGLYTHRSERLEULEU
6   ALAALAALAARGASPGLUPHEARGGLNALA
7   ASPLYSLYSLEUPROALALYSASPLYSLYS
8   SERASPMETSERILEALAHISTYRASNALA
9   VALHISSERALAALALYSTHRMETGLYILE
10   ASPTHRTRP

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 1-2 mM; potassium phosphate 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 3.25; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 950 MHz

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