BMRB Entry 31017

Title:
NMR solution structure of the De novo designed small beta-barrel protein 29_bp_sh3
Deposition date:
2022-05-04
Original release date:
2023-03-14
Authors:
Peterson, F.; Kim, D.; Jensen, D.; Saleem, A.; Chow, C.; Volkman, B.; Baker, D.
Citation:

Citation: Kim, D.; Jensen, D.; Feldman, D.; Tischer, D.; Saleem, A.; Chow, C.; Li, X.; Carter, L.; Milles, L.; Nguyen, H.; Kang, A.; Bera, A.; Peterson, F.; Volkman, B.; Ovchinnikov, S.; Baker, D.. "De novo design of small beta barrel proteins"  Proc. Natl. Acad. Sci. U. S. A. 120, e2207974120-e2207974120 (2023).
PubMed: 36897987

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, 6886.716 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET29

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts263
15N chemical shifts65
1H chemical shifts432

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 61 residues - 6886.716 Da.

1   SERGLUVALGLUTHRVALLEUARGLYSALA
2   ALAGLUARGASNLYSTHRVALASPILEHIS
3   THRLYSSERGLYTHRTHRVALARGVALASN
4   VALLYSARGVALASPSERLYSSERVALLYS
5   VALGLUARGASNGLYGLNASPLEUGLUILE
6   SERLEUASPGLNILETHRHISVALASPGLY
7   TRP

Samples:

sample_1: 29_bp_sh3, [U-13C; U-15N], 1.25 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02 % w/v

sample_conditions_1: ionic strength: 132 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TopSpin v3.6, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - data analysis

GARANT, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE III HD 600 MHz

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