BMRB Entry 11057

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11057

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Title:
MICROTUBULE BINDING DOMAIN OF DYNEIN-C
Deposition date:
2008-11-17
Original release date:
2012-07-19
Authors:
Kato, Y.; Yagi, T.; Ohki, S.; Burgess, S.; Honda, S.; Kamiya, R.; Tanokura, M.
Citation:

Citation: Kato, Y.; Yagi, T.; Ohki, S.; Harris, S.; Yura, K.; Shimizu, Y.; Honda, S.; Kamiya, R.; Burgess, S.; Tanokura, M.. "Structure of the Microtubule-Binding Domain of Flagellar Dynein"  .

Assembly members:

Assembly members:
the microtubule-binding domain of dynein heavy chain 9, polymer, 155 residues, 17391.582 Da.

Natural source:

Natural source:   Common Name: Chlamydomonas reinhardtii   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the microtubule-binding domain of dynein heavy chain 9: GSQADLAEALPLLEAALKAL DTLKPADITEVKGMKSPPAG VRRVLEAICIMKGVKPARVK DTASGRMVDDYWEASKKMLM EFDFLDSLRKFDKDHIPPEV IVKIRPFAQDPEFQPKVIEK QSVACAGLCSWVIALEKYDK VIKEVEPKRQKLREA

Data sets:
Data typeCount
13C chemical shifts500
15N chemical shifts149
1H chemical shifts1115

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1the microtubule-binding domain of dynein heavy chain 91

Entities:

Entity 1, the microtubule-binding domain of dynein heavy chain 9 155 residues - 17391.582 Da.

1   GLYSERGLNALAASPLEUALAGLUALALEU
2   PROLEULEUGLUALAALALEULYSALALEU
3   ASPTHRLEULYSPROALAASPILETHRGLU
4   VALLYSGLYMETLYSSERPROPROALAGLY
5   VALARGARGVALLEUGLUALAILECYSILE
6   METLYSGLYVALLYSPROALAARGVALLYS
7   ASPTHRALASERGLYARGMETVALASPASP
8   TYRTRPGLUALASERLYSLYSMETLEUMET
9   GLUPHEASPPHELEUASPSERLEUARGLYS
10   PHEASPLYSASPHISILEPROPROGLUVAL
11   ILEVALLYSILEARGPROPHEALAGLNASP
12   PROGLUPHEGLNPROLYSVALILEGLULYS
13   GLNSERVALALACYSALAGLYLEUCYSSER
14   TRPVALILEALALEUGLULYSTYRASPLYS
15   VALILELYSGLUVALGLUPROLYSARGGLN
16   LYSLEUARGGLUALA

Samples:

sample_1: the microtubule-binding domain of dynein heavy chain 9, [U-15N], 0.4 mM; DTT, [U-100% 2H], 1 mM; arginine 50 mM; glutamate 50 mM; sodium phosphate 10 mM; sodium chloride 100 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: the microtubule-binding domain of dynein heavy chain 9, [U-13C; U-15N], 0.4 mM; DTT, [U-100% 2H], 1 mM; arginine 50 mM; glutamate 50 mM; sodium phosphate 10 mM; sodium chloride 100 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: the microtubule-binding domain of dynein heavy chain 9, [U-13C; U-15N], 0.4 mM; DTT, [U-100% 2H], 1 mM; arginine 50 mM; glutamate 50 mM; sodium phosphate 10 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O 100%

sample_conditions_1: ionic strength: 1.42 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-13C-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA, GUNTERT, MUMENTHALER, WUTHRICH - refinement, structure solution

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • VARIAN INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAE19786

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