BMRB Entry 50336

Title:
yarp
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, 61 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):

Data sets:
Data typeCount
13C chemical shifts273
15N chemical shifts69
1H chemical shifts458

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1yarp1

Entities:

Entity 1, yarp 61 residues - Formula weight is not available

1   GLYGLULYSVALVALLEUTRPTHRARGGLU
2   ALAASPARGVALILELEUTHRMETCYSGLN
3   GLUGLNGLYALAGLNPROGLNTHRPHEASN
4   ILEILESERGLNGLNLEUGLYASNLYSTHR
5   PROALAGLUVALSERHISARGPHEARGGLU
6   LEUMETGLNLEUPHEHISTHRALACYSGLU
7   ALA

Samples:

sample_1: YARP, [U-99% 13C; U-99% 15N], 0.3 ± 0.05 mM; YARP, [U-99% 15N], 0.3 ± 0.05 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 HCACOsample_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 HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, peak picking

CYANA - structure solution

YASARA - refinement

NMR spectrometers:

  • Agilent Uniform NMR System 800 MHz

Related Database Links:

UNP Q3T8J9
AlphaFold Q9HCG6

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