BMRB Entry 27041

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27041

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Title:
Backbone 1H, 13C, and 15N and partial sidechain 1H and 13C Chemical Shift
Deposition date:
2017-03-05
Original release date:
2017-06-06
Authors:
Forcada-Nadal, Alicia; Palomino-Schaetzlein, Martina; Neira, Jose Luis; Pineda-Lucena, Antonio; Rubio, Vicente
Citation:

Citation: Forcada-Nadal, Alicia; Palomino-Schaetzlein, Martina; Neira, Jose Luis; Pineda-Lucena, Antonio; Rubio, Vicente. "The PipX protein, when not bound to its targets, has its signalling C-terminal helix in a flexed conformation"  Biochemistry 56, 3211-3224 (2017).
PubMed: 28581722

Assembly members:

Assembly members:
PipX, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Synechococcus elongatus   Taxonomy ID: 32046   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechococcus elongatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTrc99A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PipX: MASENYLNHPTFGLLYQICS FGDSKELFATLYAQRLFFLV AFDARGTRFEPIGRNEARML VDNRLRQLRRDASLQEYNQL QQVFKQTFL

Data sets:
Data typeCount
13C chemical shifts170
15N chemical shifts84
1H chemical shifts531

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PipX monomer1

Entities:

Entity 1, PipX monomer 89 residues - Formula weight is not available

1   METALASERGLUASNTYRLEUASNHISPRO
2   THRPHEGLYLEULEUTYRGLNILECYSSER
3   PHEGLYASPSERLYSGLULEUPHEALATHR
4   LEUTYRALAGLNARGLEUPHEPHELEUVAL
5   ALAPHEASPALAARGGLYTHRARGPHEGLU
6   PROILEGLYARGASNGLUALAARGMETLEU
7   VALASPASNARGLEUARGGLNLEUARGARG
8   ASPALASERLEUGLNGLUTYRASNGLNLEU
9   GLNGLNVALPHELYSGLNTHRPHELEU

Samples:

sample_1: PipX, [U-99% 15N], 200 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_2: PipX, [U-99% 13C; U-99% 15N], 200 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_3: PipX, [U-99% 13C; U-99% 15N], 200 mM; sodium phosphate 50 mM; sodium phosphate 50 mM

sample_4: PipX 200 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_5: PipX 200 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 290 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_5isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_5isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - refinement

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