BMRB Entry 30310

Title:
Solution Structure of XPH2, a Hybrid Sequence of Xfaso 1 and Pfl 6, Two Cro Proteins With Different Folds
Deposition date:
2017-06-22
Original release date:
2018-07-03
Authors:
Kumirov, V.; Dykstra, E.; Cordes, M.
Citation:

Citation: Kumirov, V.; Dykstra, E.; Hall, B.; Anderson, W.; Szyszka, T.; Cordes, M.. "Multistep mutational transformation of a protein fold through structural intermediates"  Protein Sci. 27, 1767-1779 (2018).
PubMed: 30051937

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7887.996 Da.

Natural source:

Natural source:   Common Name: Pseudomonas fluorescens PF5   Taxonomy ID: 1218948   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas fluorescens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts227
15N chemical shifts64
1H chemical shifts416

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 70 residues - 7887.996 Da.

1   METLYSLYSILEPROLEUSERLYSTYRLEU
2   GLUGLUHISGLYTHRGLNSERALALEUALA
3   ALAALALEUGLYVALASNGLNSERALAILE
4   SERGLNMETVALARGALAGLYARGCYSILE
5   ASPILEGLULEUTYRTHRASPGLYARGVAL
6   GLUCYSARGGLULEUARGPROASPVALPHE
7   GLYALALEUGLUHISHISHISHISHISHIS

Samples:

sample_1: DSS 0.1 mM; XPH2, [U-13C; U-15N], 0.8 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%; trimethylamine oxide, [U-2H], 1 M

sample_2: DSS 0.1 mM; XPH2, [U-13C; U-15N], 0.6 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%; trimethylamine oxide, [U-2H], 1 M

sample_3: DSS 0.1 mM; XPH2, [U-15N], 0.9 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%

sample_4: DSS 0.1 mM; XPH2, [U-10% 13C], 1.6 mM; potassium chloride 150 mM; potassium phosphate 50 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_3isotropicsample_conditions_1
3D_13C-separated_NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

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