BMRB Entry 11490

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11490

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Title:
Backbone and side-chain 1H, 15N and 13C resonance assignments of the microtubule-binding domains of yeast cytoplasmic dynein in the high affinity state
Deposition date:
2012-03-09
Original release date:
2014-01-14
Authors:
Takarada, Osamu
Citation:

Citation: Takarada, Osamu; Nishida, Noritaka; Kikkawa, Masahide; Shimada, Ichio. "Backbone and side-chain 1H, 15N and 13C resonance assignments of the microtubule-binding domain of yeast cytoplasmic dynein in the high and low-affinity states."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23975349

Assembly members:

Assembly members:
dynein_microtubule-binding_domain, polymer, 141 residues, 16500 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dynein_microtubule-binding_domain: GSHMKSIQDCEPTILEAQRG VKNIKKQQLTEIRSMVNPPS GVKIVMEAVCAILGYQFSNW RDIQQFIRKDDFIHNIVHYD TTLHMKPQIRKYMEEEFLSD PNFTYETINRASKACGPLYQ WVNAQINFSKCLENVDPLRQ E

Data sets:
Data typeCount
13C chemical shifts435
15N chemical shifts123
1H chemical shifts840

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Microtubule-binding domain1

Entities:

Entity 1, Microtubule-binding domain 141 residues - 16500 Da.

Residues 3092-3095 represent a cut end of non-native tag

1   GLYSERHISMETLYSSERILEGLNASPCYS
2   GLUPROTHRILELEUGLUALAGLNARGGLY
3   VALLYSASNILELYSLYSGLNGLNLEUTHR
4   GLUILEARGSERMETVALASNPROPROSER
5   GLYVALLYSILEVALMETGLUALAVALCYS
6   ALAILELEUGLYTYRGLNPHESERASNTRP
7   ARGASPILEGLNGLNPHEILEARGLYSASP
8   ASPPHEILEHISASNILEVALHISTYRASP
9   THRTHRLEUHISMETLYSPROGLNILEARG
10   LYSTYRMETGLUGLUGLUPHELEUSERASP
11   PROASNPHETHRTYRGLUTHRILEASNARG
12   ALASERLYSALACYSGLYPROLEUTYRGLN
13   TRPVALASNALAGLNILEASNPHESERLYS
14   CYSLEUGLUASNVALASPPROLEUARGGLN
15   GLU

Samples:

sample_1: dynein microtubule-binding domain, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 10 mM; sodium chloride 200 mM; H2O 90%; D2O 10%

sample_2: dynein microtubule-binding domain, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 10 mM; sodium chloride 200 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

SPARKY v3.114, Goddard - chemical shift assignment

TOPSPIN v3.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 11495
DBJ GAA24775
EMBL CAA79923 CAA82132 CAY81134
GB AAA16055 AHY76290 AJP40084 AJS30282 AJS30583
REF NP_012980
SP P36022
TPG DAA09205
AlphaFold P36022

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