BMRB Entry 30850

Name: The isolated chicken ASIC1a thumb domain (ATD-c1a) retains the structure and ligand binding properties of the full length chicken ASIC1a
Published: 2022-08-05

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PDB ID: 7lie
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30850
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:

The isolated chicken ASIC1a thumb domain (ATD-c1a) retains the structure and ligand binding properties of the full length chicken ASIC1a

Deposition date:

2021-01-27

Original release date:

2022-08-05

Authors:

Mishra, B.; Mobli, M.

Citation:

Citation: Mishra, B.; Mobli, M.. "A reductionist approach for studying the ASIC thumb domain to screen for channel modulators as novel therapeutic leads" .

Assembly members:

Assembly members:
entity_1, polymer, 78 residues, 8921.990 Da.

Natural source:

Natural source: Common Name: Chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SCKATTGDSEFYDTYSITAC RIDCETRYLVENCNCRMVHM PGDAPYCTPEQYKECADPAL DFLVEKDNEYCVCEMPCN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	342
15N chemical shifts	80
1H chemical shifts	502

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 78 residues - 8921.990 Da.

1

SER

CYS

LYS

ALA

THR

GLY

ASP

SER

GLU

2

PHE

TYR

ASP

THR

TYR

SER

ILE

THR

ALA

CYS

3

ARG

ILE

ASP

CYS

GLU

THR

ARG

TYR

LEU

VAL

4

GLU

ASN

CYS

ASN

CYS

ARG

MET

VAL

HIS

MET

5

PRO

GLY

ASP

ALA

PRO

TYR

CYS

THR

PRO

GLU

6

GLN

TYR

LYS

GLU

CYS

ALA

ASP

PRO

ALA

LEU

7

ASP

PHE

LEU

VAL

GLU

LYS

ASP

ASN

GLU

TYR

8

CYS

VAL

CYS

GLU

MET

PRO

CYS

ASN

Samples:

sample_1: Acid-sensing ion channel 1, [U-100% 13C; U-100% 15N], 320 uM; Bis-Tris 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v4.0.7, Bruker Biospin - collection

Rowland NMR Toolkit (RNMRTK) v3.0, Hoch and Stern - processing

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE 900 MHz

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