BMRB Entry 26046

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26046
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of the de novo mini protein EEH_04
Deposition date:
2016-04-22
Original release date:
2016-09-13
Authors:
Eletsky, Alexander; Bahl, Christopher; Gilmore, Jason; Buchko, Garry; Baker, David
Citation:

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).
PubMed: 27626386

Assembly members:

Assembly members:
entity, polymer, 38 residues, 4527.0 Da.

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: pet15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QCYTFRSECTNKEFTVCRPN PEEVEKEARRTKEEECRK

Data sets:
Data typeCount
13C chemical shifts109
15N chemical shifts43
1H chemical shifts247

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EEH_041

Entities:

Entity 1, EEH_04 38 residues - 4527.0 Da.

1   GLNCYSTYRTHRPHEARGSERGLUCYSTHR
2   ASNLYSGLUPHETHRVALCYSARGPROASN
3   PROGLUGLUVALGLULYSGLUALAARGARG
4   THRLYSGLUGLUGLUCYSARGLYS

Samples:

sample_1: EEH_04, [U-10% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; DSS 4 uM; D2O, [U-99% 2H], 10%; 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-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic ctsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic ctsample_1isotropicsample_conditions_1
2D 1H-1H DPFGSE TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H DPFGSE NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D 1H-15N NOESY HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSY HSQCsample_1isotropicsample_conditions_1

Software:

VNMR, 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

TALOS, Cornilescu, Delaglio and Bax - dihedral angle prediction

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

NMR spectrometers:

  • Agilent DD2 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB

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