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 27350

Title: Conformation and dynamics of intrinsically disordered microtubule associated protein 2c (MAP2c)   PubMed: 29925592

Authors: Melkova, Katerina; Zapletal, Vojtech; Jansen, Severine; Nomilner, Erik; Zachrdla, Milan; Hritz, Jozef; Zachrdla, Milan; Zweckstetter, Markus; Ringkobing-Jensen, Malene; Blackledge, Martin; Zidek, Lukas

Citation: Melkova, Katerina; Zapletal, Vojtech; Jansen, Severine; Nomilner, Erik; Zachrdla, Milan; Hritz, Jozef; Novacek, Jiri; Zweckstetter, Markus; Ringkobing Jensen, Malene; Blackledge, Martin; Zidek, Lukas. "Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics"  J. Biol. Chem. 293, .-13297 (13309).

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

Entity Sequences (FASTA):
map2c: MADERKDEGKAPHWTSASLT EAAAHPHSPEMKDQGGSGEG LSRSANGFPYREEEEGAFGE HGSQGTYSDTKENGINGELT SADRETAEEVSARIVQVVTA EAVAVLKGEQEKEAQHKDQP AALPLAAEETVNLPPSPPPS PASEQTAALEEATSGESAQA PSAFKQAKDKVTDGITKSPE KRSSLPRPSSILPPRRGVSG DREENSFSLNSSISSARRTT RSEPIRRAGKSGTSTPTTPG STAITPGTPPSYSSRTPGTP GTPSYPRTPGTPKSGILVPS EKKVAIIRTPPKSPATPKQL RLINQPLPDLKNVKSKIGST DNIKYQPKGGQVQIVTKKID LSHVTSKCGSLKNIRHRPGG GRVKIESVKLDFKEKAQAKV GSLDNAHHVPGGGNVKIDSQ KLNFREHAKARVDHGAEIIT QSPSRSSVASPRRLSNVSSS GSINLLESPQLATLAEDVTA ALAKQGL

Data typeCount
T1 relaxation values1404
T2 relaxation values1429
dipole-dipole cross correlation relaxation values366
heteronuclear NOE values1030

Additional metadata:

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

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   LYSARGSERSERLEUPROARGPROSERSER
20   ILELEUPROPROARGARGGLYVALSERGLY
21   ASPARGGLUGLUASNSERPHESERLEUASN
22   SERSERILESERSERALAARGARGTHRTHR
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   PROARGARGLEUSERASNVALSERSERSER
45   GLYSERILEASNLEULEUGLUSERPROGLN
46   LEUALATHRLEUALAGLUASPVALTHRALA
47   ALALEUALALYSGLNGLYLEU

Samples:

sample_1: map2c, [U-100% 13C; U-100% 15N], 1.0 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.9; pressure: 1 atm; temperature: 300.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links: