BMRB Entry 17627

Name: 1H, 13C, and 15N chemical shift assignments for apo actinin-2 C-terminal EF-hand (Act2-EF34)
Published: 2011-06-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17627

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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:

1H, 13C, and 15N chemical shift assignments for apo actinin-2 C-terminal EF-hand (Act2-EF34)

Deposition date:

2011-05-05

Original release date:

2011-06-03

Authors:

Au, Yunghan; Beck, Moriah; Campbell, Sharon; Pastore, Annalisa

Citation:

Citation: Au, Yunghan; Pastore, Annalisa. "The Interaction of alpha-Actinin-2 with ZASP and Titin" (2004).

Assembly members:

Assembly members:
Act2-EF34, polymer, 75 residues, 8071.05 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 Vector: pET9d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Act2-EF34: GAMADTDTAEQVIASFRILA SDKPYILAEELRRELPPDQA QYCIKRMPAYSGPGSVPGAL DYAAFSSALYGESDL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	135
15N chemical shifts	67
1H chemical shifts	276

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ef-Hands 3,4 From Alpha-Actinin	1

Entities:

Entity 1, Ef-Hands 3,4 From Alpha-Actinin 75 residues - 8071.05 Da.

N-terminal residue of natural sequence replaced by M N-terminal GA left after cleavage from fusion protein

1

GLY

ALA

MET

ALA

ASP

THR

ASP

THR

ALA

GLU

2

GLN

VAL

ILE

ALA

SER

PHE

ARG

ILE

LEU

ALA

3

SER

ASP

LYS

PRO

TYR

ILE

LEU

ALA

GLU

4

LEU

ARG

GLU

LEU

PRO

ASP

GLN

ALA

5

GLN

TYR

CYS

ILE

LYS

ARG

MET

PRO

ALA

TYR

6

SER

GLY

PRO

GLY

SER

VAL

PRO

GLY

ALA

LEU

7

ASP

TYR

ALA

PHE

SER

ALA

LEU

TYR

8

GLY

GLU

SER

ASP

LEU

Samples:

sample_1: Act2-EF34, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; D2O, [U-2H], 10%; sodium phosphate 20 mM; sodium azide 0.02 mM; H2O 90%

sample_2: Act2-EF34, [U-100% 15N], 0.5 – 1 mM; D2O, [U-2H], 10%; sodium phosphate 20 mM; sodium azide 0.02 mM; H2O 90%

sample_conditions_1: ionic strength: 20 mM; pH: 6.6; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HNHB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking, processing

XEASY, Bartels et al. - data analysis

NMR spectrometers:

Varian Unity 500 MHz
Varian Unity 600 MHz
Varian INOVA 600 MHz
Varian INOVA 800 MHz

BMRB	17626 4453 4454
PDB	1H8B 4D1E
DBJ	BAB22865 BAD92758 BAG37672 BAH11921 BAH12587
EMBL	CAB61269
GB	AAA51583 AAF76325 AAH47901 AAH51770 AAH89579
REF	NP_001029807 NP_001094 NP_001163796 NP_001230595 NP_001265272
SP	P35609 Q3ZC55 Q9JI91
AlphaFold	P35609 Q3ZC55 Q9JI91