BMRB Entry 11585

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for c-Myb R2R3 V103L/C130I
Published: 2015-12-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11585

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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-Myb R2R3 V103L/C130I

Deposition date:

2014-11-28

Original release date:

2015-12-09

Authors:

Inaba, Satomi; Ikegami, Takahisa; Oda, Masayuki

Citation:

Citation: Inaba, Satomi; Maeno, Akihiro; Sakurai, Kazumasa; Puthenpurackal, Sunilkumar; Ikegami, Takahisa; Akasaka, Kazuyuki; Oda, Masayuki. "Molecular strategy of c-Myb DNA-binding domain for function: Low-populated unfolding species revealed from temperature-dependent (NMR) studies" Biophys. J. ., .-..

Assembly members:

Assembly members:
c-Myb R2R3 V103L/C130I, polymer, 104 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
c-Myb R2R3 V103L/C130I: LIKGPWTKEEDQRLIKLVQK YGPKRWSVIAKHLKGRIGKQ IRERWHNHLNPEVKKTSWTE EEDRIIYQAHKRLGNRWAEI AKLLPGRTDNAIKNHWNSTM RRKV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	70
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	c-Myb R2R3 V103L/C130I	1

Entities:

Entity 1, c-Myb R2R3 V103L/C130I 104 residues - Formula weight is not available

1

LEU

ILE

LYS

GLY

PRO

TRP

THR

LYS

GLU

2

ASP

GLN

ARG

LEU

ILE

LYS

LEU

VAL

GLN

LYS

3

TYR

GLY

PRO

LYS

ARG

TRP

SER

VAL

ILE

ALA

4

LYS

HIS

LEU

LYS

GLY

ARG

ILE

GLY

LYS

GLN

5

ILE

ARG

GLU

ARG

TRP

HIS

ASN

HIS

LEU

ASN

6

PRO

GLU

VAL

LYS

THR

SER

TRP

THR

GLU

7

GLU

ASP

ARG

ILE

TYR

GLN

ALA

HIS

8

LYS

ARG

LEU

GLY

ASN

ARG

TRP

ALA

GLU

ILE

9

ALA

LYS

LEU

PRO

GLY

ARG

THR

ASP

ASN

10

ALA

ILE

LYS

ASN

HIS

TRP

ASN

SER

THR

MET

11

ARG

LYS

VAL

Samples:

sample_1: c-Myb R2R3 V103L/C130I, [U-99% 15N], 1.0 mM; TRIS 25 mM; potassium chloride 20 mM; H2O 90%; D2O, U-2H, 10%

sample_conditions_1: ionic strength: 45 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 950 MHz

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