BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 26960

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26960

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Title: Quantitative mapping of MAP2c phosphorylation and 14-3-3 binding sites reveals key differences between MAP2c and Tau   PubMed: 28258221

Deposition date: 2016-11-29 Original release date: 2017-03-20

Authors: Jansen, Severine; Melkova, Katerina; Trosanova, Zuzana; Hanakova, Katerina; Zachrdla, Milan; Novacek, Jiri; Zupa, Erik; Mladek, Arnost; Zdrahal, Zbynek; Hritz, Jozef; Zidek, Lukas

Citation: Jansen, Severine; Melkova, Katerina; Trosanova, Zuzana; Hanakova, Katerina; Zachrdla, Milan; Novacek, Jiri; Zupa, Erik; Zdrahal, Zbynek; Hritz, Jozef; Zidek, Lukas. "Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3& Zeta binding sites reveals key differences between MAP2c and its homolog Tau"  J. Biol. Chem. 292, 6715-6727 (2017).

Assembly members:
MAP2c, polymer, 467 residues, Formula weight is not available

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

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

Entity Sequences (FASTA):
MAP2c: MADERKDEGKAPHWTSASLT EAAAHPHSPEMKDQGGSGEG LSRSANGFPYREEEEGAFGE HGSQGTYSDTKENGINGELT SADRETAEEVSARIVQVVTA EAVAVLKGEQEKEAQHKDQP AALPLAAEETVNLPPSPPPS PASEQTAALEEATSGESAQA PSAFKQAKDKVTDGITKSPE KRSXLPRPSSILPPRRGVSG DREENSFSLNSSISSARRTX RSEPIRRAGKSGTSTPTTPG STAITPGTPPSYSSRTPGTP GTPSYPRTPGTPKSGILVPS EKKVAIIRTPPKSPATPKQL RLINQPLPDLKNVKSKIGST DNIKYQPKGGQVQIVTKKID LSHVTSKCGSLKNIRHRPGG GRVKIESVKLDFKEKAQAKV GSLDNAHHVPGGGNVKIDSQ KLNFREHAKARVDHGAEIIT QSPSRSSVASPRRLXNVSSS GSINLLESPQLATLAEDVTA ALAKQGL

Data sets:
Data typeCount
13C chemical shifts1807
15N chemical shifts464
1H chemical shifts2744

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1MAP2c1

Entities:

Entity 1, MAP2c 467 residues - Formula weight is not available

1   METALAASPGLUARGLYSASPGLUGLYLYS
2   ALAPROHISTRPTHRSERALASERLEUTHR
3   GLUALAALAALAHISPROHISSERPROGLU
4   METLYSASPGLNGLYGLYSERGLYGLUGLY
5   LEUSERARGSERALAASNGLYPHEPROTYR
6   ARGGLUGLUGLUGLUGLYALAPHEGLYGLU
7   HISGLYSERGLNGLYTHRTYRSERASPTHR
8   LYSGLUASNGLYILEASNGLYGLULEUTHR
9   SERALAASPARGGLUTHRALAGLUGLUVAL
10   SERALAARGILEVALGLNVALVALTHRALA
11   GLUALAVALALAVALLEULYSGLYGLUGLN
12   GLULYSGLUALAGLNHISLYSASPGLNPRO
13   ALAALALEUPROLEUALAALAGLUGLUTHR
14   VALASNLEUPROPROSERPROPROPROSER
15   PROALASERGLUGLNTHRALAALALEUGLU
16   GLUALATHRSERGLYGLUSERALAGLNALA
17   PROSERALAPHELYSGLNALALYSASPLYS
18   VALTHRASPGLYILETHRLYSSERPROGLU
19   LYSARGSERSEPLEUPROARGPROSERSER
20   ILELEUPROPROARGARGGLYVALSERGLY
21   ASPARGGLUGLUASNSERPHESERLEUASN
22   SERSERILESERSERALAARGARGTHRTPO
23   ARGSERGLUPROILEARGARGALAGLYLYS
24   SERGLYTHRSERTHRPROTHRTHRPROGLY
25   SERTHRALAILETHRPROGLYTHRPROPRO
26   SERTYRSERSERARGTHRPROGLYTHRPRO
27   GLYTHRPROSERTYRPROARGTHRPROGLY
28   THRPROLYSSERGLYILELEUVALPROSER
29   GLULYSLYSVALALAILEILEARGTHRPRO
30   PROLYSSERPROALATHRPROLYSGLNLEU
31   ARGLEUILEASNGLNPROLEUPROASPLEU
32   LYSASNVALLYSSERLYSILEGLYSERTHR
33   ASPASNILELYSTYRGLNPROLYSGLYGLY
34   GLNVALGLNILEVALTHRLYSLYSILEASP
35   LEUSERHISVALTHRSERLYSCYSGLYSER
36   LEULYSASNILEARGHISARGPROGLYGLY
37   GLYARGVALLYSILEGLUSERVALLYSLEU
38   ASPPHELYSGLULYSALAGLNALALYSVAL
39   GLYSERLEUASPASNALAHISHISVALPRO
40   GLYGLYGLYASNVALLYSILEASPSERGLN
41   LYSLEUASNPHEARGGLUHISALALYSALA
42   ARGVALASPHISGLYALAGLUILEILETHR
43   GLNSERPROSERARGSERSERVALALASER
44   PROARGARGLEUSEPASNVALSERSERSER
45   GLYSERILEASNLEULEUGLUSERPROGLN
46   LEUALATHRLEUALAGLUASPVALTHRALA
47   ALALEUALALYSGLNGLYLEU

Samples:

sample_1: MAP2c, [U-100% 13C; U-100% 15N], 1.1 mM; MOPS 50 mM; sodium chloride 150 mM; TCEP 0.7 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.9; pressure: 1 atm; temperature: 301.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
5D CACONCACOsample_1isotropicsample_conditions_1
5D HC(CC-TOCSY)CACONsample_1isotropicsample_conditions_1
3D(H)CANCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 950 MHz

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