BMRB Entry 16215

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16215
MolProbity Validation Chart

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

Title:
Refined solution structure of des-pyro Glu brazzein
Deposition date:
2009-03-13
Original release date:
2013-01-28
Authors:
Cornilescu, Claudia; Tonelli, Marco; DeRider, Michele; Markley, John; Assadi-Porter, Fariba
Citation:

Citation: Cornilescu, Claudia; Cornilescu, Gabriel; Rao, Hongyu; Porter, Sarah; Tonelli, Marco; DeRider, Michele; Markley, John; Assadi-Porter, Fariba. "Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein."  Proteins 81, 919-925 (2013).
PubMed: 23349025

Assembly members:

Assembly members:
wt-brazzein, polymer, 53 residues, 6523.365 Da.

Natural source:

Natural source:   Common Name: Pentadiplandra brazzeana   Taxonomy ID: 43545   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Pentadiplandra brazzeana

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
wt-brazzein: DKCKKVYENYPVSKCQLANQ CNYDCKLDKHARSGECFYDE KRNLQCICDYCEY

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts59
1H chemical shifts349

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1wt-brazzein1

Entities:

Entity 1, wt-brazzein 53 residues - 6523.365 Da.

1   ASPLYSCYSLYSLYSVALTYRGLUASNTYR
2   PROVALSERLYSCYSGLNLEUALAASNGLN
3   CYSASNTYRASPCYSLYSLEUASPLYSHIS
4   ALAARGSERGLYGLUCYSPHETYRASPGLU
5   LYSARGASNLEUGLNCYSILECYSASPTYR
6   CYSGLUTYR

Samples:

cs_sample: wt-brazzein, [U-13C; U-15N], 2 ± 0.3 mM

rdc_sample: wt-brazzein, [U-15N], 1 ± 0.1 mM

cs2_sample: wt-brazzein, [U-15N], 1 ± 0.1 mM

conditions4cs: ionic strength: 20 mM; pH: 5.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCcs_sampleisotropicconditions4cs
2D 1H-13C HSQCcs_sampleisotropicconditions4cs
3D HNCOcs_sampleisotropicconditions4cs
3D HNCAcs_sampleisotropicconditions4cs
3D HNCACBcs_sampleisotropicconditions4cs
3D CBCA(CO)NHcs_sampleisotropicconditions4cs
3D HN(CO)CAcs_sampleisotropicconditions4cs
3D HBHA(CO)NHcs_sampleisotropicconditions4cs
3D HCACOcs_sampleisotropicconditions4cs
3D HCCH-COSYcs_sampleisotropicconditions4cs
3D 1H-15N TOCSYcs2_sampleisotropicconditions4cs
3D 1H-15N NOESYcs2_sampleisotropicconditions4cs
3D 1H-13C NOESYcs_sampleisotropicconditions4cs
IPAP-HSQCcs2_sampleisotropicconditions4cs
IPAP-HSQCrdc_sampleanisotropicconditions4cs

Software:

PIPP, Garrett - data analysis, NOE assignment, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, peak picking, processing

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz
  • Bruker DMX 500 MHz
  • Bruker DMX 750 MHz
  • Bruker DMX 600 MHz

Related Database Links:

BMRB 16978 18710 4067
PDB
GB ACK76425 AGM38242
SP P56552
AlphaFold P56552

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