BMRB Entry 27780

Name: 1H, 13C and 15N resonance assignments for the N-terminal extended region and first CUE domain from chromatin remodeler SMARCAD1
Published: 2019-04-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27780

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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:

1H, 13C and 15N resonance assignments for the N-terminal extended region and first CUE domain from chromatin remodeler SMARCAD1

Deposition date:

2019-02-11

Original release date:

2019-04-12

Authors:

Redfield, Christina; Biasutto, Antonio; Mancini, Erika; West, Phillip

Citation:

Citation: Biasutto, Antonio; West, Phillip; Mancini, Erika; Redfield, Christina. "1H, 13C and 15N resonance assignments for the tandem CUE domains from chromatin remodeler SMARCAD1" Biomol. NMR Assignments 13, 261-265 (2019).
PubMed: 30919308

Assembly members:

Assembly members:
eCUE, polymer, 108 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: popinE

Entity Sequences (FASTA):

Entity Sequences (FASTA):
eCUE: MTVQEKTFNKDTVIIVSEPS EDEESQGLPTMARRNDDISE LEDLSELEDLKDAKLQTLKE LFPQRSDNDLLKLIESTSTM DGAIAAALLMFGDAGGGPRK RKHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	402
15N chemical shifts	99
1H chemical shifts	672

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	eCUE	1

Entities:

Entity 1, eCUE 108 residues - Formula weight is not available

Residues 108 is a non-native Met. Residues 210-215 are a non-native His6 tag.

1

MET

THR

VAL

GLN

GLU

LYS

THR

PHE

ASN

LYS

2

ASP

THR

VAL

ILE

VAL

SER

GLU

PRO

SER

3

GLU

ASP

GLU

SER

GLN

GLY

LEU

PRO

THR

4

MET

ALA

ARG

ASN

ASP

ILE

SER

GLU

5

LEU

GLU

ASP

LEU

SER

GLU

LEU

GLU

ASP

LEU

6

LYS

ASP

ALA

LYS

LEU

GLN

THR

LEU

LYS

GLU

7

LEU

PHE

PRO

GLN

ARG

SER

ASP

ASN

ASP

LEU

8

LEU

LYS

LEU

ILE

GLU

SER

THR

SER

THR

MET

9

ASP

GLY

ALA

ILE

ALA

LEU

MET

10

PHE

GLY

ASP

ALA

GLY

PRO

ARG

LYS

11

ARG

LYS

HIS

Samples:

sample_1: eCUE, [U-99% 15N], 0.5 ± 0.05 mM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_2: eCUE, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; sodium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 160 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

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

CCPN_Analysis, CCPN - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz
Bruker Avance 750 MHz

UNP	Q9H4L7
AlphaFold	Q9ULU7