BMRB Entry 30753

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30753
MolProbity Validation Chart

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Title:
Solution NMR structure of de novo designed TMB2.3
Deposition date:
2020-05-19
Original release date:
2021-02-15
Authors:
Liang, B.; Vorobieva, A.; Chow, C.; Baker, D.; Tamm, L.
Citation:

Citation: Vorobieva, Anastassia; White, Paul; Liang, Binyong; Horne, Jim; Bera, Asim; Chow, Cameron; Gerben, Stacey; Marx, Sinduja; Kang, Alex; Stiving, Alyssa; Harvey, Sophie; Marx, Dagan; Khan, G Nasir; Fleming, Karen; Wysocki, Vicki; Brockwell, David; Tamm, Lukas; Radford, Sheena; Baker, David. "De novo design of transmembrane beta-barrels"  Science 371, eabc8182-eabc8182 (2021).
PubMed: 33602829

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 13547.988 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: MQDGPGTLDVFVAAGWNTDN TIEITGGATYQLSPYIMVKA GYGWNNSSLNRFEFGGGLQY KVTPDLEPYAWAGATYNTDN TLVPAAGAGFRYKVSPEVKL VVEYGWNNSSLQFLQAGLSY RIQP

Data sets:
Data typeCount
13C chemical shifts333
15N chemical shifts108
1H chemical shifts108

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 124 residues - 13547.988 Da.

1   METGLNASPGLYPROGLYTHRLEUASPVAL
2   PHEVALALAALAGLYTRPASNTHRASPASN
3   THRILEGLUILETHRGLYGLYALATHRTYR
4   GLNLEUSERPROTYRILEMETVALLYSALA
5   GLYTYRGLYTRPASNASNSERSERLEUASN
6   ARGPHEGLUPHEGLYGLYGLYLEUGLNTYR
7   LYSVALTHRPROASPLEUGLUPROTYRALA
8   TRPALAGLYALATHRTYRASNTHRASPASN
9   THRLEUVALPROALAALAGLYALAGLYPHE
10   ARGTYRLYSVALSERPROGLUVALLYSLEU
11   VALVALGLUTYRGLYTRPASNASNSERSER
12   LEUGLNPHELEUGLNALAGLYLEUSERTYR
13   ARGILEGLNPRO

Samples:

sample_1: TMB2.3, [U-98% 13C; U-98% 15N, U-98% 2H], 1.8 ± 0.1 mM; DPC 200 ± 10 mM; HEPES 10 ± 0.1 mM; MES 10 ± 0.1 mM; sodium acetate 10 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; sodium azide 0.05 ± 0.001 % w/v

sample_conditions_1: ionic strength: 50 mM; pH: 6.3; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D NOESY-TROSYsample_1isotropicsample_conditions_1
3D HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1
1H-15N hetNOEsample_1isotropicsample_conditions_1
1D protonsample_1isotropicsample_conditions_1

Software:

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

Sparky, Goddard, TD, and Kneller, DG - data analysis

hmsIST, S. G. Hyberts, A. G. Milbradt, A. B. Wagner, H. Arthanari, G. Wagner, - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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