BMRB Entry 30204

Title:
Solution structure of the de novo mini protein gHH_44
Deposition date:
2016-11-15
Original release date:
2017-09-25
Authors:
Buchko, G.; Bahl, C.; Baker, D.
Citation:

Citation: Bhardwaj, Gaurav; Mulligan, Vikram Khipple; Bahl, Christopher; Gilmore, Jason; Harvey, Peta; Cheneval, Olivier; Buchko, Garry; Pulavarti, Surya; Kaas, Quentin; Eletsky, Alexander; Huang, Po-Ssu; Johnsen, William; Greisen, Per Jr; Rocklin, Gabriel; Song, Yifan; Linsky, Thomas; Watkins, Andrew; Rettie, Stephen; Xu, Xianzhong; Carter, Lauren; Bonneau, Richard; Olson, James; Coutsias, Evangelos; Correnti, Colin; Szyperski, Thomas; Craik, David; Baker, David. "Accurate de novo design of hyperstable constrained peptides"  Nature 538, 329-335 (2016).
PubMed: 27626386

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 3366.862 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AEDCERIRKELEKNPNDEIK KKLEKCQA

Data sets:
Data typeCount
13C chemical shifts117
15N chemical shifts29
1H chemical shifts164

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 28 residues - 3366.862 Da.

1   ALAGLUASPCYSGLUARGILEARGLYSGLU
2   LEUGLULYSASNPROASNASPGLUILELYS
3   LYSLYSLEUGLULYSCYSGLNALA

Samples:

sample_1: HH2, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium acetate, none, 25 ± 1 mM; sodium chloride, none, 50 ± 2 mM

sample_2: HH2, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium acetate, none, 25 ± 1 mM; sodium chloride, none, 50 ± 2 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 4.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D C(CO)NHsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1anisotropicsample_conditions_1
3D HNCAsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1anisotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
D20 exchangesample_2anisotropicsample_conditions_1

Software:

CNS v1.1, Brunger A. T. et.al. - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - chemical shift assignment

SPARKY v3.115, Goddard - data analysis

NMR spectrometers:

  • Varian VXRS 600 MHz
  • Varian VXRS 800 MHz
  • Varian INOVA 500 MHz

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