BMRB Entry 26982

Name: Chemical shift assignments of the RYBP NZF domain
Published: 2018-02-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26982

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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:

Chemical shift assignments of the RYBP NZF domain

Deposition date:

2016-12-21

Original release date:

2018-02-09

Authors:

Lee, Brian; Spyracopoulos, Leo

Citation:

Citation: Ali, Mohammad; Strickfaden, Hilmar; Lee, Brian; Spyracopoulos, Leo; Hendzel, Michael. "RYBP Is a K63-Ubiquitin-Chain-Binding Protein that Inhibits Homologous Recombination Repair" Cell Rep. 22, 383-395 (2018).
PubMed: 29320735

Assembly members:

Assembly members:
RYBP_NZF_domain, polymer, 37 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

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: pGEX-6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RYBP_NZF_domain: GPLGSDEGFWDCSVCTFRNS AEAFKCSICDVRKGTST

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	144
15N chemical shifts	35
1H chemical shifts	197

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RYBP NZF domain	1
2	ZINC ION	2

Entities:

Entity 1, RYBP NZF domain 37 residues - Formula weight is not available

1

GLY

PRO

LEU

GLY

SER

ASP

GLU

GLY

PHE

TRP

2

ASP

CYS

SER

VAL

CYS

THR

PHE

ARG

ASN

SER

3

ALA

GLU

ALA

PHE

LYS

CYS

SER

ILE

CYS

ASP

4

VAL

ARG

LYS

GLY

THR

SER

THR

Entity 2, ZINC ION - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: RYBP NZF domain, [U-13C; U-15N], 0.2 mM; DSS, [U-2H], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 273 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-13C TOCSY aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

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