BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26045

Title: Solution structure of the de novo mini protein HHH_06   PubMed: 27626386

Deposition date: 2016-04-22 Original release date: 2016-09-13

Authors: Eletsky, Alexander; Bahl, Christopher; Gilmore, Jason; Buchko, Garry; Baker, David

Citation: Bhardwaj, G.; Mulligan, V.; Bahl, C.; Gilmore, J.; Harvey, P.; Cheneval, O.; Buchko, G.; Pulavarti, S.; Kaas, Q.; Eletsky, A.; Huang, P.; Johnsen, W.; Greisen, P.; Rocklin, G.; Song, Y.; Linsky, T.; Watkins, A.; Rettie, S.; Xu, X.; Carter, L.; Bonneau, R.; Olson, J.; Coutsias, E.; Correnti, C.; Szyperski, T.; Craik, D.; Baker, D.. "Accurate de novo design of hyperstable constrained peptides."  Nature 538, 329-335 (2016).

Assembly members:
HHH_06, polymer, 44 residues, 5119.8 Da.

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

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

Entity Sequences (FASTA):
HHH_06: APCEDLKERLKKLGMSEECR QRLEKMCKEGTSEDAERMAR NCES

Data sets:
Data typeCount
13C chemical shifts155
15N chemical shifts49
1H chemical shifts303

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HHH_061

Entities:

Entity 1, HHH_06 44 residues - 5119.8 Da.

1   ALAPROCYSGLUASPLEULYSGLUARGLEU
2   LYSLYSLEUGLYMETSERGLUGLUCYSARG
3   GLNARGLEUGLULYSMETCYSLYSGLUGLY
4   THRSERGLUASPALAGLUARGMETALAARG
5   ASNCYSGLUSER

Samples:

sample_1: sodium phosphate 50 mM; DSS 4 uM; D2O, [U-99% 2H], 10%; sodium azide 0.02%; HHH_06, [U-100% 15N], 1 mM

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-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H DPFGSE TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H DPFGSE NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESY HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSY HSQCsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

vnmrj, Varian - collection

prosa, Guntert - processing

xeasy, Bartels et al. - data analysis

cara, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

cyana, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

pdbstat, pdbstat (Moseley, Montelione) - data analysis

PSVS, Bhattacharya and Montelione - RPF calculation, validation, violations

NMR spectrometers:

  • Agilent DD2 600 MHz
  • Varian INOVA 750 MHz

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