BMRB Entry 26720

Name: Backbone and triple resonance 1H, 13C, and 15N Chemical Shift Assignments for residues 420-500 of Saccharomyces cerevisiae transcription factor Ash1 when 10 fold phosphorylated
Published: 2018-02-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26720

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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 and triple resonance 1H, 13C, and 15N Chemical Shift Assignments for residues 420-500 of Saccharomyces cerevisiae transcription factor Ash1 when 10 fold phosphorylated

Deposition date:

2015-12-11

Original release date:

2018-02-23

Authors:

Martin, Erik; Grace, Christy R.; Mittag, Tanja

Citation:

Citation: Martin, Erik; Holehouse, Alex; Grace, Christy; Hughes, Alex; Pappu, Rohit; Mittag, Tanja. "Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation" J. Am. Chem. Soc. 138, 15323-15335 (2016).
PubMed: 27807972

Assembly members:

Assembly members:
pAsh1_420-500, polymer, 83 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: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
pAsh1_420-500: GASASSSPSPSTPTKSGKMR SRSSSPVRPKAYTPSPRSPN YHRFALDSPPQSPRRSSNSS ITKKGSRRSSGSSPTRHTTR VCV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	210
15N chemical shifts	73
1H chemical shifts	70

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pAsh1 420-500	1

Entities:

Entity 1, pAsh1 420-500 83 residues - Formula weight is not available

1

GLY

ALA

SER

ALA

SER

PRO

SER

PRO

2

SER

THR

PRO

THR

LYS

SER

GLY

LYS

MET

ARG

3

SER

ARG

SER

PRO

VAL

ARG

PRO

LYS

4

ALA

TYR

THR

PRO

SER

PRO

ARG

SER

PRO

ASN

5

TYR

HIS

ARG

PHE

ALA

LEU

ASP

SER

PRO

6

GLN

SER

PRO

ARG

SER

ASN

SER

7

ILE

THR

LYS

GLY

SER

ARG

SER

8

GLY

SER

PRO

THR

ARG

HIS

THR

ARG

9

VAL

CYS

VAL

Samples:

sample_1: pAsh1 420-500, [U-100% 13C; U-100% 15N], 0.6 ± 0.1 mM; NaCl 137 mM; KCl 7.2 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.167 M; pH: 6.95; pressure: 1 atm; temperature: 278 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)N(COCA)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D NCO	sample_1	isotropic	sample_conditions_1
3D (HA)CANCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 800 MHz

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