BMRB Entry 27418

Name: Backbone 1H, 15N, 13C assignment of Human Myc S373D, N353 to A399.
Published: 2018-04-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27418

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 15N, 13C assignment of Human Myc S373D, N353 to A399.

Deposition date:

2018-03-06

Original release date:

2018-04-11

Authors:

Macek, Pavel

Citation:

Citation: Macek, Pavel; Cliff, Matthew; Embrey, Kevin; Holdgate, Geoffrey; Nissink, J Willem; Panova, Stanislava; Waltho, Jonathan; Davies, Rick. "Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding" J. Biol. Chem. 293, 9301-9310 (2018).
PubMed: 29695509

Assembly members:

Assembly members:
cMyc_S373D, 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):
cMyc_S373D: GSNVKRRTHNVLERQRRNEL KRDFFALRDQIPELENNEKA PKVVILKKATAYILSVQAEE QKLISEEDLLRKRREQLKHK LEQLRNS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	92
15N chemical shifts	43
1H chemical shifts	43

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cMyc S373D	1

Entities:

Entity 1, cMyc S373D 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

ASP

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: cMyc S373D, [U-100% 13C; U-100% 15N], 0.15 mM; potassium phosphate 50 mM; ammonium chloride 500 mM; DTT 1 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 550 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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