BMRB Entry 54056

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR54056

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

Title:
Backbone chemical shifts of apo yeast chorismate mutase
Deposition date:
2026-10-13
Original release date:
2026-10-30
Authors:
Sapienza, Paul; Lee, Andrew
Citation:

Citation: Sapienza, Paul; Bonin, Jeffrey; Jinasena, H; Li, Kelin; Dieckhaus, Henry; Popov, Konstantin; Aube, Jeffrey; Lee, Andrew. "Mixed, nonclassical behavior in a classic allosteric protein. "  Proc. Natl. Acad. Sci. U. S. A. 120, e2308338120-e2308338120 (2023).
PubMed: 37695919

Assembly members:

Assembly members:
chorismate mutase apo, polymer, 256 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
chorismate mutase apo: MDFTKPETVLNLQNIRDELV RMEDSIIFKFIERSHFATCP SVYEANHPGLEIPNFKGSFL DWALSNLEIAHSRIRRFESP DETPFFPDKIQKSFLPSINY PQILAPYAPEVNYNDKIKKV YIEKIIPLISKRDGDDKNNF GSVATRDIECLQSLSRRIHF GKFVAEAKFQSDIPLYTKLI KSKDVEGIMKNITNSAVEEK ILERLTKKAEVYGVDPTNES GERRITPEYLVKIYKEIVIP ITKEVEVEYLLRRLEE

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts145
1H chemical shifts145

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1chorismate mutase apo, chain 11
2chorismate mutase apo, chain 21

Entities:

Entity 1, chorismate mutase apo, chain 1 256 residues - Formula weight is not available

1   METASPPHETHRLYSPROGLUTHRVALLEU
2   ASNLEUGLNASNILEARGASPGLULEUVAL
3   ARGMETGLUASPSERILEILEPHELYSPHE
4   ILEGLUARGSERHISPHEALATHRCYSPRO
5   SERVALTYRGLUALAASNHISPROGLYLEU
6   GLUILEPROASNPHELYSGLYSERPHELEU
7   ASPTRPALALEUSERASNLEUGLUILEALA
8   HISSERARGILEARGARGPHEGLUSERPRO
9   ASPGLUTHRPROPHEPHEPROASPLYSILE
10   GLNLYSSERPHELEUPROSERILEASNTYR
11   PROGLNILELEUALAPROTYRALAPROGLU
12   VALASNTYRASNASPLYSILELYSLYSVAL
13   TYRILEGLULYSILEILEPROLEUILESER
14   LYSARGASPGLYASPASPLYSASNASNPHE
15   GLYSERVALALATHRARGASPILEGLUCYS
16   LEUGLNSERLEUSERARGARGILEHISPHE
17   GLYLYSPHEVALALAGLUALALYSPHEGLN
18   SERASPILEPROLEUTYRTHRLYSLEUILE
19   LYSSERLYSASPVALGLUGLYILEMETLYS
20   ASNILETHRASNSERALAVALGLUGLULYS
21   ILELEUGLUARGLEUTHRLYSLYSALAGLU
22   VALTYRGLYVALASPPROTHRASNGLUSER
23   ILEGLUARGARGILETHRPROGLUTYRLEU
24   VALLYSILETYRLYSGLUILEVALILEPRO
25   ILETHRLYSGLUVALGLUVALGLUTYRLEU
26   LEUARGARGLEUGLUGLU

Samples:

sample_1: chorismate mutase apo, [U-13C; U-15N; U-2H], 0.5 ± 0.1 mM; sodium chloride 150 mM; sodium phosphate 25 mM; EDTA 1 mM; DTT 1 mM

sample_conditions_1: ionic strength: 175 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRViewJ - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700, 850 MHz

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