BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50957

Title: 1H, 15 N, and 13 C resonance assignments of the SH3-like tandem domain of human KIN17 protein

Deposition date: 2021-06-01 Original release date: 2021-06-04

Authors: Lourenco, Isabella; Seixas, Flavio; Almeida, Fabio; Fossey, Marcelo; Souza, Fatima; Caruso, Icaro

Citation: Lourenco, Isabella; Seixas, Flavio; Almeida, Fabio; Fossey, Marcelo; Souza, Fatima; Caruso, Icaro. "1H, 15 N, and 13 C resonance assignments of the SH3-like tandem domain of human KIN17 protein"  Biomol. NMR Assignments ., .-..

Assembly members:
entity_1, polymer, 127 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-4T-1

Entity Sequences (FASTA):
entity_1: GEEEKKRTARTDYWLQPEII VKIITKKLGEKYHKKKAIVK EVIDKYTAVVKMIDSGDKLK LDQTHLETVIPAPGKRILVL NGGYRGNEGTLESINEKTFS ATIVIETGPLKGRRVEGIQY EDISKLA

Data sets:
Data typeCount
13C chemical shifts587
15N chemical shifts127
1H chemical shifts954

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 tandem domain of KIN protein1

Entities:

Entity 1, SH3 tandem domain of KIN protein 127 residues - Formula weight is not available

1   GLYGLUGLUGLULYSLYSARGTHRALAARG
2   THRASPTYRTRPLEUGLNPROGLUILEILE
3   VALLYSILEILETHRLYSLYSLEUGLYGLU
4   LYSTYRHISLYSLYSLYSALAILEVALLYS
5   GLUVALILEASPLYSTYRTHRALAVALVAL
6   LYSMETILEASPSERGLYASPLYSLEULYS
7   LEUASPGLNTHRHISLEUGLUTHRVALILE
8   PROALAPROGLYLYSARGILELEUVALLEU
9   ASNGLYGLYTYRARGGLYASNGLUGLYTHR
10   LEUGLUSERILEASNGLULYSTHRPHESER
11   ALATHRILEVALILEGLUTHRGLYPROLEU
12   LYSGLYARGARGVALGLUGLYILEGLNTYR
13   GLUASPILESERLYSLEUALA

Samples:

sample_1: SH3 tandem domain of KIN protein, [U-13C; U-15N], 0.35 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 0.5 mM; sodium azide 0.02%; EDTA 3 mM; DSS 0.33 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRbox - data analysis

NMRDraw - processing

ANALYSIS - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts