BMRB Entry 27701

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Myc bHLH-LZ domain in presence of 3.2 M GdmCl
Published: 2019-08-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27701

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Myc bHLH-LZ domain in presence of 3.2 M GdmCl

Deposition date:

2018-11-24

Original release date:

2019-08-15

Authors:

Panova, Stanislava; Cliff, Matthew; Macek, Pavel; Blackledge, Martin; Jensen, Malene; Nissink, J. Willem; Embrey, Kevin; Davies, Rick; Waltho, Jonathan

Citation:

Citation: Panova, Stanislava; Cliff, Matthew; Macek, Pavel; Blackledge, Martin; Jensen, Malene; Nissink, J. Willem; Embrey, Kevin; Davies, Rick; Waltho, Jonathan. "Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration" Structure 27, 1537-1546 (2019).
PubMed: 31402220

Assembly members:

Assembly members:
bHLHZip_domain_of_Myc, polymer, 87 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
bHLHZip_domain_of_Myc: GSNVKRRTHNVLERQRRNEL KRSFFALRDQIPELENNEKA PKVVILKKATAYILSVQAEE QKLISEEDLLRKRREQLKHK LEQLRNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	255
15N chemical shifts	84
1H chemical shifts	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	bHLHZip domain of Myc	1

Entities:

Entity 1, bHLHZip domain of Myc 87 residues - Formula weight is not available

1

GLY

SER

ASN

VAL

LYS

ARG

THR

HIS

ASN

2

VAL

LEU

GLU

ARG

GLN

ARG

ASN

GLU

LEU

3

LYS

ARG

SER

PHE

ALA

LEU

ARG

ASP

GLN

4

ILE

PRO

GLU

LEU

GLU

ASN

GLU

LYS

ALA

5

PRO

LYS

VAL

ILE

LEU

LYS

ALA

THR

6

ALA

TYR

ILE

LEU

SER

VAL

GLN

ALA

GLU

7

GLN

LYS

LEU

ILE

SER

GLU

ASP

LEU

8

ARG

LYS

ARG

GLU

GLN

LEU

LYS

HIS

LYS

9

LEU

GLU

GLN

LEU

ARG

ASN

SER

Samples:

sample_1: bHLHZip domain of Myc, [U-13C; U-15N], 1 ± 0.1 mM; sodium phosphate 20 ± 2 mM; TSP 1 ± 0.1 mM; GdmCl 3.2 ± 0.1 M

sample_conditions_1: ionic strength: 3.2 M; pH: 6.5; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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
(H)N(CA)NNH	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR v2.4.2, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 800 MHz

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