BMRB Entry 28097

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28097

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Title:
1H, 15N, 13C backbone resonance assignments of the P146A variant of beta-phosphoglucomutase in a transition state analogue complex with glucose 6-phosphate and trifluoromagnesate (MgF3-)
Deposition date:
2020-03-10
Original release date:
2020-09-03
Authors:
Baxter, Nicola; Cruz-Navarrete, F.
Citation:

Citation: Wood, Henry; Cruz-Navarrete, F; Baxter, Nicola; Trevitt, Clare; Robertson, Angus; Dix, Samuel; Hounslow, Andrea; Cliff, Matthew; Waltho, Jonathan. "Allomorphy as a mechanism of post-translational control of enzyme activity"  Nat. Commun. 11, 5538-5538 (2020).
PubMed: 33139716

Assembly members:

Assembly members:
beta-phosphoglucomutase, polymer, 221 residues, 24183.61 Da.
entity_MG, non-polymer, 24.305 Da.
entity_MGF, non-polymer, 81.300 Da.
entity_G6P, non-polymer, 260.136 Da.

Natural source:

Natural source:   Common Name: Lactococcus lactis   Taxonomy ID: 1358   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactococcus lactis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
beta-phosphoglucomutase: MFKAVLFDLDGVITDTAEYH FRAWKALAEEIGINGVDRQF NEQLKGVSREDSLQKILDLA DKKVSAEEFKELAKRKNDNY VKMIQDVSPADVYPGILQLL KDLRSNKIKIALASASKNGP FLLERMNLTGYFDAIADPAE VAASKAAPDIFIAAAHAVGV APSESIGLEDSQAGIQAIKD SGALPIGVGRPEDLGDDIVI VPDTSHYTLEFLKEVWLQKQ K

Data sets:
Data typeCount
13C chemical shifts641
15N chemical shifts211
19F chemical shifts3
1H chemical shifts211

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1bPGM-P146A1
2Mg2
3MgF33
4G6P4

Entities:

Entity 1, bPGM-P146A 221 residues - 24183.61 Da.

1   METPHELYSALAVALLEUPHEASPLEUASP
2   GLYVALILETHRASPTHRALAGLUTYRHIS
3   PHEARGALATRPLYSALALEUALAGLUGLU
4   ILEGLYILEASNGLYVALASPARGGLNPHE
5   ASNGLUGLNLEULYSGLYVALSERARGGLU
6   ASPSERLEUGLNLYSILELEUASPLEUALA
7   ASPLYSLYSVALSERALAGLUGLUPHELYS
8   GLULEUALALYSARGLYSASNASPASNTYR
9   VALLYSMETILEGLNASPVALSERPROALA
10   ASPVALTYRPROGLYILELEUGLNLEULEU
11   LYSASPLEUARGSERASNLYSILELYSILE
12   ALALEUALASERALASERLYSASNGLYPRO
13   PHELEULEUGLUARGMETASNLEUTHRGLY
14   TYRPHEASPALAILEALAASPPROALAGLU
15   VALALAALASERLYSALAALAPROASPILE
16   PHEILEALAALAALAHISALAVALGLYVAL
17   ALAPROSERGLUSERILEGLYLEUGLUASP
18   SERGLNALAGLYILEGLNALAILELYSASP
19   SERGLYALALEUPROILEGLYVALGLYARG
20   PROGLUASPLEUGLYASPASPILEVALILE
21   VALPROASPTHRSERHISTYRTHRLEUGLU
22   PHELEULYSGLUVALTRPLEUGLNLYSGLN
23   LYS

Entity 2, Mg - Mg - 24.305 Da.

1   MG

Entity 3, MgF3 - F3 Mg - 81.300 Da.

1   MGF

Entity 4, G6P - C6 H13 O9 P - 260.136 Da.

1   G6P

Samples:

sample_1: beta-phosphoglucomutase, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; potassium HEPES buffer 50 mM; magnesium chloride 5 mM; sodium azide 2 mM; H2O 90%; D2O, [U-99% 2H], 10%; EDTA 1 mM; TSP, [U-2H], 1 mM; NaF 15 mM; glucose 6-phosphate 10 mM

sample_conditions_1: ionic strength: 116 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY HNCACBsample_1isotropicsample_conditions_1
1D 19Fsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1 and 4.0, Bruker Biospin - collection, processing

Felix, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking, processing

NMR spectrometers:

  • Bruker Avance I 800 MHz
  • Bruker Avance NEO 600 MHz
  • Bruker Avance III 500 MHz

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