BMRB Entry 31251

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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/BMR31251
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
Honey Truffle Active Component
Deposition date:
2025-06-20
Original release date:
2026-04-20
Authors:
McFarland, C.; Connors, D.
Citation:

Citation: McFarland, C.; Alkotaini, B.; Cowen, C.; Edwards, M.; Grein, E.; Hahn, A.; Jennings, J.; Patnaik, R.; Potter, S.; Rael, L.; Sharkey, B.; Taylor, S.; Totman, R.; Van Simaeys, K.; Vo, P.; Zhao, D.; Connors, D.. "Discovery, Expression, and In Silico Safety Evaluation of Honey Truffle Sweetener, a Sweet Protein Derived from Mattirolomyces terfezioides and Produced by Heterologous Expression in Komagataella phaffii"  J. Agric. Food Chem. 72, 19470-19479 (2024).

Assembly members:

Assembly members:
entity_1, polymer, 121 residues, 13394.060 Da.

Natural source:

Natural source:   Common Name: Mattirolomyces terfezioides   Taxonomy ID: 74857   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Mattirolomyces terfezioides

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Komagataella phaffii CBS 7435

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPDLSSFITIKNNSNHVFTR TAIYSKYAAVQWSPEPQLSI SPGKWDLFILKDILSIRGTS GYVQYRVGDGPGWVRVTFSS LVGADEVAEWSSGDLPDGFV LQKPVRTGSRPLQATFEATK Q

Data sets:
Data typeCount
13C chemical shifts503
15N chemical shifts120
1H chemical shifts838

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 121 residues - 13394.060 Da.

1   METPROASPLEUSERSERPHEILETHRILE
2   LYSASNASNSERASNHISVALPHETHRARG
3   THRALAILETYRSERLYSTYRALAALAVAL
4   GLNTRPSERPROGLUPROGLNLEUSERILE
5   SERPROGLYLYSTRPASPLEUPHEILELEU
6   LYSASPILELEUSERILEARGGLYTHRSER
7   GLYTYRVALGLNTYRARGVALGLYASPGLY
8   PROGLYTRPVALARGVALTHRPHESERSER
9   LEUVALGLYALAASPGLUVALALAGLUTRP
10   SERSERGLYASPLEUPROASPGLYPHEVAL
11   LEUGLNLYSPROVALARGTHRGLYSERARG
12   PROLEUGLNALATHRPHEGLUALATHRLYS
13   GLN

Samples:

sample_1: HT-AC, [U-13C], 0.39 mg/mL; sodium phosphate monobasic 500 mM; sodium phosphate dibasic 500 mM

sample_conditions_1: ionic strength: 2.091 M; pH: 7; pressure: 550 Torr; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

XEASY, Bartels et al. - peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz

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