BMRB Entry 18580

Name: 1H, 13C, and 15N backbone and side chain resonance assignments of the C-terminal DNA binding and dimerization domain of v-Myc
Published: 2013-02-08

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18580

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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 backbone and side chain resonance assignments of the C-terminal DNA binding and dimerization domain of v-Myc

Deposition date:

2012-07-09

Original release date:

2013-02-08

Authors:

Kizilsavas, Gonul; Saxena, Saurabh; Zerko, Szymon; Kozminski, Wiktor; Bister, Klaus; Konrat, Robert

Citation:

Citation: Kzlsava, Gonul; Saxena, Saurabh; erko, Szymon; Komiski, Wiktor; Bister, Klaus; Konrat, Robert. "1H, 13C, and 15N backbone and side chain resonance assignments of the C-terminal DNA binding and dimerization domain of v-Myc." Biomol. NMR Assignments 7, 321-324 (2013).
PubMed: 23179058

Assembly members:

Assembly members:
c-Terminal_v-Myc, polymer, 131 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: Myelocytomatosis virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: petM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c-Terminal_v-Myc: MKHHHHHHPMSDYDIPTTEN LYFQGAMVSNNRKCSSPRTL DSEENDKRRTHNVLERQRRN ELKLRFFALRDQIPEVANNE KAPKVVILKKATEYVLSLQS DEHKLIAEKEQLRRRREQLK HNLEQLRNSRA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	418
15N chemical shifts	120
1H chemical shifts	629

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

Entity 1, c-Terminal v-Myc 131 residues - Formula weight is not available

1

MET

LYS

HIS

PRO

MET

2

SER

ASP

TYR

ASP

ILE

PRO

THR

GLU

ASN

3

LEU

TYR

PHE

GLN

GLY

ALA

MET

VAL

SER

ASN

4

ASN

ARG

LYS

CYS

SER

PRO

ARG

THR

LEU

5

ASP

SER

GLU

ASN

ASP

LYS

ARG

THR

6

HIS

ASN

VAL

LEU

GLU

ARG

GLN

ARG

ASN

7

GLU

LEU

LYS

LEU

ARG

PHE

ALA

LEU

ARG

8

ASP

GLN

ILE

PRO

GLU

VAL

ALA

ASN

GLU

9

LYS

ALA

PRO

LYS

VAL

ILE

LEU

LYS

10

ALA

THR

GLU

TYR

VAL

LEU

SER

LEU

GLN

SER

11

ASP

GLU

HIS

LYS

LEU

ILE

ALA

GLU

LYS

GLU

12

GLN

LEU

ARG

GLU

GLN

LEU

LYS

13

HIS

ASN

LEU

GLU

GLN

LEU

ARG

ASN

SER

ARG

14

ALA

Samples:

sample_1: c-Terminal v-Myc, [U-95% 13C; U-90% 15N], 0.7 mM; DTT 1 mM; EDTA 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.6; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
5D HN(CA)CONH	sample_1	isotropic	sample_conditions_1
5D (HACA)CON(CA)CONH	sample_1	isotropic	sample_conditions_1
5D (H)NCO(NCA)CONH	sample_1	isotropic	sample_conditions_1
5D HNCACOCB	sample_1	isotropic	sample_conditions_1
5D HabCabCONH	sample_1	isotropic	sample_conditions_1
5D H(CC-tocsy)CONH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Agilent Direct Drive 700 MHz

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