BMRB Entry 27024

Name: Ascl1 fragment B
Published: 2017-04-21

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27024

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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:

Ascl1 fragment B

Deposition date:

2017-02-06

Original release date:

2017-04-21

Authors:

Baronti, Lorenzo; Hosek, Tomas; Gil-Caballero, Sergio; Raveh-Amit, Hadas; Calcada, Eduardo; Ayala, Isabel; Dinnyes, Andras; Felli, Isabella; Pierattelli, Roberta; Brutscher, Bernhard

Citation:

Citation: Baronti, Lorenzo; Hosek, Tomas; Gil-Caballero, Sergio; Raveh-Amit, Hadas; Calcada, Eduardo; Ayala, Isabel; Dinnyes, Andras; Felli, Isabella; Pierattelli, Roberta; Brutscher, Bernhard. "Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1'" Biophys. J. 112, 1366-1373 (2017).
PubMed: 28402879

Assembly members:

Assembly members:
Ascl1_fragment_B, polymer, 126 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ascl1_fragment_B: MASHHHHHHMESSAKMESGG AGQQPQPQPQQPFLPPAACF FATAAAAAAAAAAAAAQSAQ QQQQQQQQQQQAPQLRPAAD GQPSGGGHKSAPKQVKRQRS SSPELMRCKRRLNFSGFGYS LPQQQP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	315
15N chemical shifts	97
1H chemical shifts	97

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ascl1 trascription factor, Fragment B	1

Entities:

Entity 1, Ascl1 trascription factor, Fragment B 126 residues - Formula weight is not available

Residues 1-9 represent the artificial affinity tag. Ascl1 fragment B chemical shift assignment start from residue 10 (residue 1 in the assignment file).

1

MET

ALA

SER

HIS

MET

2

GLU

SER

ALA

LYS

MET

GLU

SER

GLY

3

ALA

GLY

GLN

PRO

GLN

PRO

GLN

PRO

GLN

4

GLN

PRO

PHE

LEU

PRO

ALA

CYS

PHE

5

PHE

ALA

THR

ALA

6

ALA

GLN

SER

ALA

GLN

7

GLN

8

GLN

ALA

PRO

GLN

LEU

ARG

PRO

ALA

ASP

9

GLY

GLN

PRO

SER

GLY

HIS

LYS

SER

10

ALA

PRO

LYS

GLN

VAL

LYS

ARG

GLN

ARG

SER

11

SER

PRO

GLU

LEU

MET

ARG

CYS

LYS

ARG

12

ARG

LEU

ASN

PHE

SER

GLY

PHE

GLY

TYR

SER

13

LEU

PRO

GLN

PRO

Samples:

sample_1: Ascl1 fragment B, [U-100% 13C; U-100% 15N], 250 uM; TRIS 50 mM; TCEP 5 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D BEST-TROSY HCNs	sample_1	isotropic	sample_conditions_1
3D BEST-TROSY HNNs	sample_1	isotropic	sample_conditions_1
HADAMAC	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 950 MHz
Bruker Avance 850 MHz
Bruker Avance 700 MHz
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