BMRB Entry 34570

Name: Solution NMR structure of the SH3 domain of human Caskin1
Published: 2021-02-01

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PDB ID: 7aty
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34570
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of the SH3 domain of human Caskin1 PubMed: 33467043

Deposition date: 2020-11-01 Original release date: 2021-02-01

Authors: Toke, O.; Koprivanacz, K.; Radnai, L.; Mero, B.; Juhasz, T.; Liliom, K.; Buday, L.

Citation: Toke, O.; Koprivanacz, K.; Radnai, L.; Mero, B.; Juhasz, T.; Liliom, K.; Buday, L.. "Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding" Cells 10, 173-173 (2021).

Assembly members:
entity_1, polymer, 67 residues, 7458.308 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: GSHMLQVRATKDYCNNYDLT SLNVKAGDIITVLEQHPDGR WKGCIHDNRTGNDRVGYFPS SLGEAIV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	101
15N chemical shifts	69
1H chemical shifts	400

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 67 residues - 7458.308 Da.

1

GLY

SER

HIS

MET

LEU

GLN

VAL

ARG

ALA

THR

2

LYS

ASP

TYR

CYS

ASN

TYR

ASP

LEU

THR

3

SER

LEU

ASN

VAL

LYS

ALA

GLY

ASP

ILE

4

THR

VAL

LEU

GLU

GLN

HIS

PRO

ASP

GLY

ARG

5

TRP

LYS

GLY

CYS

ILE

HIS

ASP

ASN

ARG

THR

6

GLY

ASN

ASP

ARG

VAL

GLY

TYR

PHE

PRO

SER

7

SER

LEU

GLY

GLU

ALA

ILE

VAL

Samples:

sample_1: human caskin1 SH3 domain, [U-13C; U-15N], 0.6 ± 0.1 mM; K-phosphate 20 mM; KCl 100 mM; NaN3 0.05%; TCEP 0.1 mM

sample_2: human caskin1 SH3 domain, [U-15N], 0.6 ± 0.1 mM; K-phosphate 20 mM; KCl 100 mM; NaN3 0.05%; TCEP 0.1 mM

sample_3: human caskin1 SH3 domain 1 ± 0.1 mM; K-phosphate 20 mM; KCl 100 mM; NaN3 0.05%; TCEP 0.1 mM

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CC-TOCSY-NNH	sample_1	isotropic	sample_conditions_1
3D HCC-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	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
3D Met-Met NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

Software:

VnmrJ, Varian - collection

Felix, Accelrys Software Inc. - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

Varian Uniform NMR System 600 MHz

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