BMRB Entry 50329

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50329

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NPAT
Deposition date:
2020-06-17
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, 31 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KKKKIKKKKLPSSFPAGMDV DKFLLSLHYDE

Data sets:
Data typeCount
13C chemical shifts128
15N chemical shifts29
1H chemical shifts247

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NPAT1

Entities:

Entity 1, NPAT 31 residues - Formula weight is not available

1   LYSLYSLYSLYSILELYSLYSLYSLYSLEU
2   PROSERSERPHEPROALAGLYMETASPVAL
3   ASPLYSPHELEULEUSERLEUHISTYRASP
4   GLU

Samples:

sample_1: NPAT 1.5 ± 0.3 mM; TRIS-d11 25 mM; KCl 250 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - data analysis

CYANA v3.97 - structure solution

YASARA v17.1 - refinement

NMR spectrometers:

  • Agilent Uniform NMR System 800 MHz

Related Database Links:

UNP Q14207
AlphaFold Q8IWE9

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