BMRB Entry 50335

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50335

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Title:
FLASH_1923
Deposition date:
2020-06-22
Original release date:
2020-08-25
Authors:
Bucholc, Katarzyna; Skrajna, Aleksandra; Adamska, Kinga; Yang, Xiao-Cui; Krajewski, Krzysztof; Poznanski, Jaroslaw; Dadlez, Michal; Dominski, Zbigniew; Zhukov, Igor
Citation:

Citation: Bucholc, Katarzyna; Skrajna, Aleksandra; Adamska, Kinga; Yang, Xiao-Cui; Krajewski, Krzysztof; Poznanski, Jaroslaw; Dadlez, Michal; Dominski, Zbigniew; Zhukov, Igor. "Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations"  Int. J. Mol. Sci. 21, 5268-5268 (2020).
PubMed: 32722282

Assembly members:

Assembly members:
entity_1, polymer, 60 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEIIILWTRNDDREILLECQ KRGPSFKTFAYLAAKLDKNP NQVSERFQQLMKLFEKSKCR

Data sets:
Data typeCount
13C chemical shifts290
15N chemical shifts66
1H chemical shifts475

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FLASH 19231

Entities:

Entity 1, FLASH 1923 60 residues - Formula weight is not available

1   GLYGLUILEILEILELEUTRPTHRARGASN
2   ASPASPARGGLUILELEULEUGLUCYSGLN
3   LYSARGGLYPROSERPHELYSTHRPHEALA
4   TYRLEUALAALALYSLEUASPLYSASNPRO
5   ASNGLNVALSERGLUARGPHEGLNGLNLEU
6   METLYSLEUPHEGLULYSSERLYSCYSARG

Samples:

sample_1: FLASH, [U-99% 13C; U-99% 15N], 0.4 ± 0.1 mM; FLASH, [U-99% 15N], 0.4 ± 0.1 mM; TRIS-d11 25 mM; KCl 250 mM; Arg+Glu 50 mM; TCEP 40 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.2; 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 HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

CYANA - structure solution

Chimera - data analysis

YASARA - refinement

NMR spectrometers:

  • Agilent Uniform NMR System 800 MHz

Related Database Links:

UNP Q9UKL3
AlphaFold Q9Y563

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