BMRB Entry 50228

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50228

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Title:
1H, 13C and 15N resonance assignments for the microtubule binding region of the kinetoplastid kinetochore protein KKT4 145-232
Deposition date:
2020-04-09
Original release date:
2020-07-24
Authors:
Ludzia, Patryk; Akiyoshi, Bungo; Redfield, Christina
Citation:

Citation: Ludzia, Patryk; Akiyoshi, Bungo; Redfield, Christina. "1 H, 13 C and 15 N resonance assignments for the microtubule-binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei"  Biomol. NMR Assignments 14, 309-315 (2020).
PubMed: 32696260

Assembly members:

Assembly members:
entity_1, polymer, 90 residues, 10335.71 Da.

Natural source:

Natural source:   Common Name: Trypanosoma brucei brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSF_Duet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SMRSEPVVDTQRVLDLEEEV ARLKRTIGHLQGVVEEKESA LEKHATQHNLEVHEMKKNYE LKIKSLTQTHEAAVRKLVSA QELVTAARNY

Data sets:
Data typeCount
13C chemical shifts249
15N chemical shifts92
1H chemical shifts100

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KKT4 145-2321

Entities:

Entity 1, KKT4 145-232 90 residues - 10335.71 Da.

Residues 1-2 (143S, 144M) represent part of a remained linker after TEV protease cleavage.

1   SERMETARGSERGLUPROVALVALASPTHR
2   GLNARGVALLEUASPLEUGLUGLUGLUVAL
3   ALAARGLEULYSARGTHRILEGLYHISLEU
4   GLNGLYVALVALGLUGLULYSGLUSERALA
5   LEUGLULYSHISALATHRGLNHISASNLEU
6   GLUVALHISGLUMETLYSLYSASNTYRGLU
7   LEULYSILELYSSERLEUTHRGLNTHRHIS
8   GLUALAALAVALARGLYSLEUVALSERALA
9   GLNGLULEUVALTHRALAALAARGASNTYR

Samples:

sample_1: 2H/13C/15N-KKT4_145_232, [U-13C; U-15N; U-2H], 0.35 ± 0.02 mM; HEPES 25 ± 0 mM; sodium chloride 150 ± 0 mM; TCEP 0.5 ± 0 mM

sample_2: 13C/15N-KKT4_145_232, [U-13C; U-15N], 0.35 ± 0.02 mM; HEPES 25 ± 0 mM; sodium chloride 150 ± 0 mM; TCEP 0.5 ± 0 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D BEST TROSYsample_2isotropicsample_conditions_1
2D BEST TROSYsample_1isotropicsample_conditions_1
2D BEST TROSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D BT HNCAsample_1isotropicsample_conditions_1
3D BT HN(CO)CACBsample_1isotropicsample_conditions_1
3D BT HNCACBsample_1isotropicsample_conditions_1
3D BT HNCOsample_1isotropicsample_conditions_1
3D BT HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.4.2 - chemical shift assignment

NMRPipe v9.7 - processing

hmsIST vv211_64b - processing

TOPSPIN v3.2 - collection

NMR spectrometers:

  • Bruker Avance III HD 750 MHz
  • Bruker Avance III HD 950 MHz

Related Database Links:

UniProt A0A3L6L4L8
AlphaFold A0A3L6L4L8

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