BMRB Entry 11075

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11075

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Title:
1H, 13C, and 15N Chemical Shift Assignments for N-terminal domain of kp60
Deposition date:
2009-08-05
Original release date:
2010-04-07
Authors:
Iwaya, Naoko; Kuwahara, Yohta; Tenno, Takeshi; Tochio, Hidehito; Shirakawa, Masahiro; Hiroaki, Hidekazu
Citation:

Citation: Iwaya, Naoko; Kuwahara, Yohta; Fujiwara, Yoshie; Goda, Natsuko; Tenno, Takeshi; Akiyama, Kohei; Mase, Shogo; Tochio, Hidehito; Ikegami, Takahisa; Shirakawa, Masahiro; Hiroaki, Hidekazu. "A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization."  J. Biol. Chem. 285, 16822-16829 (2010).
PubMed: 20339000

Assembly members:

Assembly members:
N-terminal domain of kp60, polymer, 78 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-4T3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal domain of kp60: GSDHMTMSLQMIVENVKLAR EYALLGNYDSAMVYYQGVLD QMNKYLYSVKDTHLRQKWQQ VWQEINVEAKQVKDIMKT

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts85
1H chemical shifts574

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of kp601

Entities:

Entity 1, N-terminal domain of kp60 78 residues - Formula weight is not available

1   GLYSERASPHISMETTHRMETSERLEUGLN
2   METILEVALGLUASNVALLYSLEUALAARG
3   GLUTYRALALEULEUGLYASNTYRASPSER
4   ALAMETVALTYRTYRGLNGLYVALLEUASP
5   GLNMETASNLYSTYRLEUTYRSERVALLYS
6   ASPTHRHISLEUARGGLNLYSTRPGLNGLN
7   VALTRPGLNGLUILEASNVALGLUALALYS
8   GLNVALLYSASPILEMETLYSTHR

Samples:

sample_1: N-terminal domain of kp60, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; EDTA 1 mM; H2O 95%; D2O 5%

sample_2: N-terminal domain of kp60, [U-13C; U-15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; EDTA 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

Molmol v2K.2, Koradi, Billeter and Wuthrich - chemical shift assignment, refinement

SPARKY v3.106, Goddard - chemical shift assignment, refinement

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 800 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
GB AAD42087 AAH09136 EDL03542
REF NP_035965
SP Q9WV86
AlphaFold Q9WV86

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