BMRB Entry 50336

Name: yarp
Published: 2020-08-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50336

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
entity_1: GEKVVLWTREADRVILTMCQ EQGAQPQTFNIISQQLGNKT PAEVSHRFRELMQLFHTACE A

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	273
15N chemical shifts	69
1H chemical shifts	458

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	yarp	1

Entities:

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

1

GLY

GLU

LYS

VAL

LEU

TRP

THR

ARG

GLU

2

ALA

ASP

ARG

VAL

ILE

LEU

THR

MET

CYS

GLN

3

GLU

GLN

GLY

ALA

GLN

PRO

GLN

THR

PHE

ASN

4

ILE

SER

GLN

LEU

GLY

ASN

LYS

THR

5

PRO

ALA

GLU

VAL

SER

HIS

ARG

PHE

ARG

GLU

6

LEU

MET

GLN

LEU

PHE

HIS

THR

ALA

CYS

GLU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_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

UNP	Q3T8J9
AlphaFold	Q9HCG6