BMRB Entry 50277

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50277

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Title:
Backbone assignments of Ca 2+ /calmodulin-dependent protein kinase 1D
Deposition date:
2020-05-16
Original release date:
2020-08-25
Authors:
Tong, Michael; Jeeves, Mark; Rajesh, Sundaresan; Ludwig, Christian; Lenoir, Marc; Kumar, Jitendra; McClelland, Darren; Berditchevski, Fedor; Hubbard, Julia; Kenyon, Colin; Butterworth, Sam; Knapp, Stefan; Overduin, Michael
Citation:

Citation: Tong, Michael; Jeeves, Mark; Rajesh, Sundaresan; Ludwig, Christian; Lenoir, Marc; Kumar, Jitendra; McClelland, Darren; Berditchevski, Fedor; Hubbard, Julia; Kenyon, Colin; Butterworth, Sam; Knapp, Stefan; Overduin, Michael. "Backbone resonance assignments of the catalytic and regulatory domains of Ca 2+/calmodulin-dependent protein kinase 1D"  Biomol. NMR Assignments 14, 221-225 (2020).
PubMed: 32535836

Assembly members:

Assembly members:
entity_1, polymer, 334 residues, Formula weight is not available

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: pNIC28-Bsa4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMARENGESSSSWKKQAEDI KKIFEFKETLGTGAFSEVVL AEEKATGKLFAVKCIPKKAL KGKESSIENEIAVLRKIKHE NIVALEDIYESPNHLYLVMQ LVSGGELFDRIVEKGFYTEK DASTLIRQVLDAVYYLHRMG IVHRDLKPENLLYYSQDEES KIMISDFGLSKMEGKGDVMS TACGTPGYVAPEVLAQKPYS KAVDCWSIGVIAYILLCGYP PFYDENDSKLFEQILKAEYE FDSPYWDDISDSAKDFIRNL MEKDPNKRYTCEQAARHPWI AGDTALNKNIHESVSAQIRK NFAKSKWRQAFNATAVVRHM RKLHLGSSLDSSNA

Data sets:
Data typeCount
13C chemical shifts823
15N chemical shifts254
1H chemical shifts254

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 334 residues - Formula weight is not available

sequence starts at Met

1   SERMETALAARGGLUASNGLYGLUSERSER
2   SERSERTRPLYSLYSGLNALAGLUASPILE
3   LYSLYSILEPHEGLUPHELYSGLUTHRLEU
4   GLYTHRGLYALAPHESERGLUVALVALLEU
5   ALAGLUGLULYSALATHRGLYLYSLEUPHE
6   ALAVALLYSCYSILEPROLYSLYSALALEU
7   LYSGLYLYSGLUSERSERILEGLUASNGLU
8   ILEALAVALLEUARGLYSILELYSHISGLU
9   ASNILEVALALALEUGLUASPILETYRGLU
10   SERPROASNHISLEUTYRLEUVALMETGLN
11   LEUVALSERGLYGLYGLULEUPHEASPARG
12   ILEVALGLULYSGLYPHETYRTHRGLULYS
13   ASPALASERTHRLEUILEARGGLNVALLEU
14   ASPALAVALTYRTYRLEUHISARGMETGLY
15   ILEVALHISARGASPLEULYSPROGLUASN
16   LEULEUTYRTYRSERGLNASPGLUGLUSER
17   LYSILEMETILESERASPPHEGLYLEUSER
18   LYSMETGLUGLYLYSGLYASPVALMETSER
19   THRALACYSGLYTHRPROGLYTYRVALALA
20   PROGLUVALLEUALAGLNLYSPROTYRSER
21   LYSALAVALASPCYSTRPSERILEGLYVAL
22   ILEALATYRILELEULEUCYSGLYTYRPRO
23   PROPHETYRASPGLUASNASPSERLYSLEU
24   PHEGLUGLNILELEULYSALAGLUTYRGLU
25   PHEASPSERPROTYRTRPASPASPILESER
26   ASPSERALALYSASPPHEILEARGASNLEU
27   METGLULYSASPPROASNLYSARGTYRTHR
28   CYSGLUGLNALAALAARGHISPROTRPILE
29   ALAGLYASPTHRALALEUASNLYSASNILE
30   HISGLUSERVALSERALAGLNILEARGLYS
31   ASNPHEALALYSSERLYSTRPARGGLNALA
32   PHEASNALATHRALAVALVALARGHISMET
33   ARGLYSLEUHISLEUGLYSERSERLEUASP
34   SERSERASNALA

Samples:

sample_1: human calmodulin-dependent protein kinase 1D (CAMK1D), [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 50 mM; sodium chloride 75 mM; TCEP 0.5 mM; sodium azide 0.02%

sample_2: human calmodulin-dependent protein kinase 1D (CAMK1D), [U-13C; U-15N; U-2H], 1.2 mM; sodium phosphate 50 mM; sodium chloride 75 mM; TCEP 0.5 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 125 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1

Software:

NMRPipe - processing

CcpNmr Analysis - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

UNP Q8IU85
AlphaFold Q9HD31

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