BMRB Entry 26663

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for c-Myc-1-88, pS62
Published: 2015-12-17

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26663

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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 c-Myc-1-88, pS62

Deposition date:

2015-09-17

Original release date:

2015-12-17

Authors:

Helander, Sara; Montecchio, Meri; Sunnerhagen, Maria

Citation:

Citation: Helander, Sara; Montecchio, Meri; Pilstal, Robert; Su, Yulong; Kuruvilla, Jacob; Elven, Malin; Ziauddin, Javed; Anandapadamanaban, Madhanagopal; Cristobal, Susana; Lundstrom, Patrik; Sears, Rosalie; Wallner, Bjorn; Sunnerhagen, Maria. "Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity" Structure 23, 2267-2279 (2015).
PubMed: 26655473

Assembly members:

Assembly members:
c-Myc, polymer, 94 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: pETMCSIII

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c-Myc: HHHHHHMPLNVSFTNRNYDL DYDSVQPYFYCDEEENFYQQ QQQSELQPPAPSEDIWKKFE LLPTPPLXPSRRSGLCSPSY VAVTPFSLRGDNDG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	236
15N chemical shifts	83
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	c-Myc	1

Entities:

Entity 1, c-Myc 94 residues - Formula weight is not available

1

HIS

MET

PRO

LEU

ASN

2

VAL

SER

PHE

THR

ASN

ARG

ASN

TYR

ASP

LEU

3

ASP

TYR

ASP

SER

VAL

GLN

PRO

TYR

PHE

TYR

4

CYS

ASP

GLU

ASN

PHE

TYR

GLN

5

GLN

SER

GLU

LEU

GLN

PRO

ALA

6

PRO

SER

GLU

ASP

ILE

TRP

LYS

PHE

GLU

7

LEU

PRO

THR

PRO

LEU

SEP

PRO

SER

8

ARG

SER

GLY

LEU

CYS

SER

PRO

SER

TYR

9

VAL

ALA

VAL

THR

PRO

PHE

SER

LEU

ARG

GLY

10

ASP

ASN

ASP

GLY

Samples:

sample_1: c-Myc, [U-99% 13C; U-99% 15N], 80-250 uM; DTT 5 mM; glycerol 5%; H2O 90%; D2O 10%; HEPES 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 273 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HACAN	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Analysis of data processing

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

NMR spectrometers:

Varian INOVA 600 MHz

UNP	P01106
AlphaFold	Q14026