BMRB Entry 16781

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16781

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Title:
Backbone chemical shift assignments for the microtubule binding domain of the Dictyostelium discoideum dynein heavy chain
Deposition date:
2010-03-21
Original release date:
2010-05-03
Authors:
McNaughton, Lynn; Tikhonenko, Irina; Banavali, Nilesh; LeMaster, David; Koonce, Michael
Citation:

Citation: McNaughton, Lynn; Tikhonenko, Irina; Banavali, Nilesh; LeMaster, David; Koonce, Michael. "A low affinity ground state conformation for the Dynein microtubule binding domain."  J. Biol. Chem. 285, 15994-16002 (2010).
PubMed: 20351100

Assembly members:

Assembly members:
dynein_microtubule_binding_domain, polymer, 134 residues, 15120 Da.

Natural source:

Natural source:   Common Name: Dictyostelium discoideum   Taxonomy ID: 44689   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Dictyostelium discoideum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dynein_microtubule_binding_domain: GSHMLEDPPAIIEAQEAVST IKKKHLDEIKSLPKPPTPVK LAMEAVCLMLGGKKLEWADI RKKIMEPNFITSIINYDTKK MMTPKIREAITKGYLEDPGF DYETVNRASKACGPLVKWAT AQTYYSEILDRIKP

Data sets:
Data typeCount
13C chemical shifts364
15N chemical shifts116
1H chemical shifts116

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1dynein headpiece1

Entities:

Entity 1, dynein headpiece 134 residues - 15120 Da.

The initial 8 residues preceding the PAII... sequence are the residual sequence from a thrombin cleavage sequence

1   GLYSERHISMETLEUGLUASPPROPROALA
2   ILEILEGLUALAGLNGLUALAVALSERTHR
3   ILELYSLYSLYSHISLEUASPGLUILELYS
4   SERLEUPROLYSPROPROTHRPROVALLYS
5   LEUALAMETGLUALAVALCYSLEUMETLEU
6   GLYGLYLYSLYSLEUGLUTRPALAASPILE
7   ARGLYSLYSILEMETGLUPROASNPHEILE
8   THRSERILEILEASNTYRASPTHRLYSLYS
9   METMETTHRPROLYSILEARGGLUALAILE
10   THRLYSGLYTYRLEUGLUASPPROGLYPHE
11   ASPTYRGLUTHRVALASNARGALASERLYS
12   ALACYSGLYPROLEUVALLYSTRPALATHR
13   ALAGLNTHRTYRTYRSERGLUILELEUASP
14   ARGILELYSPRO

Samples:

sample_1: dynein microtubule binding domain, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 93%; D2O 7%; NaCl 150 mM; PIPES-d18 20 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.50; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

FELIX v2000, Accelrys Software Inc. - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAA78827
GB EAL69258
REF XP_643185
SP P34036
AlphaFold P34036

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