BMRB Entry 50215

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50215

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Title:
1H, 13C and 15N resonance assignments for the microtubule binding region of the kinetoplastid kinetochore protein KKT4 115-174
Deposition date:
2020-03-20
Original release date:
2020-07-24
Authors:
Ludzia, Patryk; Redfield, Christina; Akiyoshi, Bungo
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, 62 residues, 7152.14 Da.

Natural source:

Natural source:   Common Name: Trypanosoma 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: SMKYGVVSVERYERLMARYK ELEKQSHRRQGKRSEPVVDT QRVLDLEEEVARLKRTIGHL QG

Data sets:
Data typeCount
13C chemical shifts218
15N chemical shifts63
1H chemical shifts325

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KKT4_115_174, monomer 11
2KKT4_115_174, monomer 21

Entities:

Entity 1, KKT4_115_174, monomer 1 62 residues - 7152.14 Da.

Residues 1-2 (113S, 114M) represent part of a remained linker after TEV protease cleavage

1   SERMETLYSTYRGLYVALVALSERVALGLU
2   ARGTYRGLUARGLEUMETALAARGTYRLYS
3   GLULEUGLULYSGLNSERHISARGARGGLN
4   GLYLYSARGSERGLUPROVALVALASPTHR
5   GLNARGVALLEUASPLEUGLUGLUGLUVAL
6   ALAARGLEULYSARGTHRILEGLYHISLEU
7   GLNGLY

Samples:

sample_1: 15N-KKT4_115_174, [U-15N], 0.35 ± 0.02 mM; HEPES 25 mM; sodium chloride 150 mM; TCEP 0.5 mM

sample_2: 13C/15N-KKT4_115_174, [U-13C; U-15N], 0.35 ± 0.02 mM; HEPES 25 mM; sodium chloride 150 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
2D BEST TROSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D BT HNCAsample_2isotropicsample_conditions_1
3D BT HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D CBCACONHsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_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