BMRB Entry 27269

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27269

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for gHEEE_02 in presence of 10 mM TCEP
Deposition date:
2017-10-02
Original release date:
2018-09-04
Authors:
Pulavarti, Surya V. S. R. K; Shaw, Elizabeth; Bahl, Christopher; Garry, Buchko; Baker, David; Szyperski, Thomas
Citation:

Citation: Buchko, Garry; Pulavarti, Surya; Ovchinnikov, Victor; Shaw, Elizabeth; Rettie, Stephen; Myler, Peter; Karplus, Martin; Szyperski, Thomas; Baker, David; Bahl, Christopher. "Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides"  Protein Sci. 27, 1611-1623 (2018).
PubMed: 30152054

Assembly members:

Assembly members:
gHEEE_02, polymer, 41 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pCDB364

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gHEEE_02: SQETRKKCTEMKKKFKNCEV RCDESNHCVEVRCSDTKYTL C

Data sets:
Data typeCount
13C chemical shifts176
15N chemical shifts39
1H chemical shifts270

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gHEEE_021

Entities:

Entity 1, gHEEE_02 41 residues - Formula weight is not available

1   SERGLNGLUTHRARGLYSLYSCYSTHRGLU
2   METLYSLYSLYSPHELYSASNCYSGLUVAL
3   ARGCYSASPGLUSERASNHISCYSVALGLU
4   VALARGCYSSERASPTHRLYSTYRTHRLEU
5   CYS

Samples:

sample_1: gHEEE_02, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 0.05 mM; D2O, [U-100% 2H], 10%; TCEP 10 mM; sodium phosphate 50 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC, with wide spectral widthsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic, constant timesample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromatic, constant timesample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

VNMR v4.1, agilent - data acquisition

PROSA v6, Guntert - processing

XEASY, Bartels et al. - data analysis, processing

CARA v1.8, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Agilent DD2 600 MHz

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