BMRB Entry 50521

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50521

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Title:
hTS dUMP backbone and ILVM methyl assignments
Deposition date:
2020-10-19
Original release date:
2021-06-30
Authors:
Bonin, Jeffrey; Lee, Andrew
Citation:

Citation: Bonin, Jeffrey; Lee, Andrew. "Backbone and ILVM methyl resonance assignments of human thymidylate synthase in apo and substrate bound forms."  Biomol. NMR Assign. 15, 197-202 (2021).
PubMed: 33486616

Assembly members:

Assembly members:
entity_1, polymer, 313 residues, Formula weight is not available
entity_UMP, non-polymer, 308.182 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPVAGSELPRRPLPPAAQER DAEPRPPHGELQYLGQIQHI LRCGVRKDDRTGTGTLSVFG MQARYSLRDEFPLLTTKRVF WKGVLEELLWFIKGSTNAKE LSSKGVKIWDANGSRDFLDS LGFSTREEGDLGPVYGFQWR HFGAEYRDMESDYSGQGVDQ LQRVIDTIKTNPDDRRIIMC AWNPRDLPLMALPPCHALCQ FYVVNSELSCQLYQRSGDMG LGVPFNIASYALLTYMIAHI TGLKPGDFIHTLGDAHIYLN HIEPLKIQLQREPRPFPKLR ILRKVEKIDDFKAEDFQIEG YNPHPTIKMEMAV

Data typeCount
..

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hTS monomer, 11
2hTS monomer, 21
3UMP, 12
4UMP, 22

Entities:

Entity 1, hTS monomer, 1 313 residues - Formula weight is not available

1   METPROVALALAGLYSERGLULEUPROARG
2   ARGPROLEUPROPROALAALAGLNGLUARG
3   ASPALAGLUPROARGPROPROHISGLYGLU
4   LEUGLNTYRLEUGLYGLNILEGLNHISILE
5   LEUARGCYSGLYVALARGLYSASPASPARG
6   THRGLYTHRGLYTHRLEUSERVALPHEGLY
7   METGLNALAARGTYRSERLEUARGASPGLU
8   PHEPROLEULEUTHRTHRLYSARGVALPHE
9   TRPLYSGLYVALLEUGLUGLULEULEUTRP
10   PHEILELYSGLYSERTHRASNALALYSGLU
11   LEUSERSERLYSGLYVALLYSILETRPASP
12   ALAASNGLYSERARGASPPHELEUASPSER
13   LEUGLYPHESERTHRARGGLUGLUGLYASP
14   LEUGLYPROVALTYRGLYPHEGLNTRPARG
15   HISPHEGLYALAGLUTYRARGASPMETGLU
16   SERASPTYRSERGLYGLNGLYVALASPGLN
17   LEUGLNARGVALILEASPTHRILELYSTHR
18   ASNPROASPASPARGARGILEILEMETCYS
19   ALATRPASNPROARGASPLEUPROLEUMET
20   ALALEUPROPROCYSHISALALEUCYSGLN
21   PHETYRVALVALASNSERGLULEUSERCYS
22   GLNLEUTYRGLNARGSERGLYASPMETGLY
23   LEUGLYVALPROPHEASNILEALASERTYR
24   ALALEULEUTHRTYRMETILEALAHISILE
25   THRGLYLEULYSPROGLYASPPHEILEHIS
26   THRLEUGLYASPALAHISILETYRLEUASN
27   HISILEGLUPROLEULYSILEGLNLEUGLN
28   ARGGLUPROARGPROPHEPROLYSLEUARG
29   ILELEUARGLYSVALGLULYSILEASPASP
30   PHELYSALAGLUASPPHEGLNILEGLUGLY
31   TYRASNPROHISPROTHRILELYSMETGLU
32   METALAVAL

Entity 2, UMP, 1 - C9 H13 N2 O8 P - 308.182 Da.

1   UMP

Samples:

sample_1: Human Thymidylate Synthase Apo Dimer, [U-13C; U-15N; U-2H], 0.3 mM; 2'-deoxyuridine-5'-monophosphate 2.5 mM; PO4 25 mM; NaCl 20 mM; NaN3 0.01%

sample_2: Human Thymidylate Synthase Apo Dimer, {I (13CdH3), L(13CdH3,13CdH3), V(13CgH3,13CgH3), M(U-13C)} U-[2H,15N], 0.3 mM; 2'-deoxyuridine-5'-monophosphate 3 mM; PO4 25 mM; NaCl 20 mM; NaN3 0.01%

sample_conditions_1: pH: 7.5; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
dUMP_hsqc.nvsample_1isotropicsample_conditions_1
dUMP_hncocacb.nvsample_1isotropicsample_conditions_1
dUMP_hncoca.nvsample_1isotropicsample_conditions_1
dUMP_hnco.nvsample_1isotropicsample_conditions_1
dUMP_hnca.nvsample_1isotropicsample_conditions_1
dUMP_hncacb.nvsample_1isotropicsample_conditions_1
hTS_dUMP_ILVM_CCnoesy.nvsample_2isotropicsample_conditions_1
hTS_dUMP_ILVM_hmqc.nvsample_2isotropicsample_conditions_1
dUMP_hncaco.nvsample_1isotropicsample_conditions_1

Software:

NMRViewJ - chemical shift assignment, peak picking

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 850 MHz
  • Bruker AVANCE III 600 MHz