BMRB Entry 30875

Name: Ara h 1 leader sequence, Ara h 1.0101 (25-83) A25G
Published: 2022-03-04

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PDB ID: 7lxk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30875
MolProbity Validation Chart

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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:

Ara h 1 leader sequence, Ara h 1.0101 (25-83) A25G

Deposition date:

2021-03-03

Original release date:

2022-03-04

Authors:

Mueller, G.; London, R.

Citation:

Citation: Foo, Alexander; Nesbit, Jacqueline; Gipson, Stephen; Cheng, Hsiaopo; Bushel, Pierre; DeRose, Eugene; Schein, Catherine; Teuber, Suzanne; Hurlburt, Barry; Maleki, Soheila; Mueller, Geoffrey. "Structure, Immunogenicity, and IgE Cross-Reactivity among Walnut and Peanut Vicilin-Buried Peptides" J. Agric. Food Chem. 70, 2389-2400 (2022).
PubMed: 35139305

Assembly members:

Assembly members:
entity_1, polymer, 59 residues, 6733.499 Da.

Natural source:

Natural source: Common Name: Peanut Taxonomy ID: 3818 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arachis hypogaea

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GKSSPYQKKTENPCAQRCLQ SCQQEPDDLKQKACESRCTK LEYDPRCVYDPRGHTGTTN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	168
15N chemical shifts	48
1H chemical shifts	277

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 59 residues - 6733.499 Da.

1

GLY

LYS

SER

PRO

TYR

GLN

LYS

THR

2

GLU

ASN

PRO

CYS

ALA

GLN

ARG

CYS

LEU

GLN

3

SER

CYS

GLN

GLU

PRO

ASP

LEU

LYS

4

GLN

LYS

ALA

CYS

GLU

SER

ARG

CYS

THR

LYS

5

LEU

GLU

TYR

ASP

PRO

ARG

CYS

VAL

TYR

ASP

6

PRO

ARG

GLY

HIS

THR

GLY

THR

ASN

Samples:

sample_1: A1pro, [U-13C; U-15N], 0.5 mM; sodium chloride 137 mM; sodium phosphate 10 mM; potassium chloride 2.7 mM; DSS 0.2 uM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

Agilent DD2 600 MHz
Agilent DD2 800 MHz

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