BMRB Entry 30147

Name: Notch1 transmembrane and associated juxtamembrane segment
Published: 2017-05-04

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PDB ID: 5kzo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30147
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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:

Notch1 transmembrane and associated juxtamembrane segment

Deposition date:

2016-07-25

Original release date:

2017-05-04

Authors:

Deatherage, C.; Lu, Z.; Kroncke, B.

Citation:

Citation: Deatherage, Catherine; Lu, Zhenwei; Kroncke, Brett; Ma, Sirui; Smith, Jarrod; Voehler, Markus; McFeeters, Robert; Sanders, Charles. "Structural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains" Sci. Adv. 3, e1602794-e1602794 (2017).
PubMed: 28439555

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, 6849.948 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHHHHHHVQSETVEPPPPA QLHFMYVAAAAFVLLFFVGC GVLLSRKRRRQHGQLWFPE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	137
15N chemical shifts	46
1H chemical shifts	45

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 59 residues - 6849.948 Da.

1

MET

GLY

HIS

VAL

GLN

2

SER

GLU

THR

VAL

GLU

PRO

ALA

3

GLN

LEU

HIS

PHE

MET

TYR

VAL

ALA

4

ALA

PHE

VAL

LEU

PHE

VAL

GLY

CYS

5

GLY

VAL

LEU

SER

ARG

LYS

ARG

6

GLN

HIS

GLY

GLN

LEU

TRP

PHE

PRO

GLU

Samples:

sample_1: DHPC/DMPC bicelle 150 mg/mL; DTT 2 mM; EDTA 1 mM; Notch1, [U-99% 15N], 350 uM; imidazole 65 mM

sample_2: DHPC/DMPC bicelle 150 mg/mL; Notch1, [U-99% 13C; U-99% 15N], 500 uM

sample_3: DHPC/DMPC 150 mg/mL; DTT 2 mM; EDTA 1 mM; Notch1, [U-99% 13C; U-99% 15N], 500 uM; imidazole 65 mM

sample_conditions_1: ionic strength: 65 mM; pH: 5.5; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D H(CCO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

X-PLOR, Brunger - refinement

NMR spectrometers:

Bruker AvanceIII 900 MHz
Bruker AvanceIII 600 MHz

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