BMRB Entry 17626

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Act2-EF34 in complex with palladin peptide
Published: 2011-10-12

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17626

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for Act2-EF34 in complex with palladin peptide

Deposition date:

2011-05-05

Original release date:

2011-10-12

Authors:

Beck, Moriah; Campbell, Sharon

Citation:

Citation: Beck, Moriah; Otey, Carol; Campbell, Sharon. "Structural characterization of the interactions between palladin and -actinin." J. Mol. Biol. 413, 712-725 (2011).
PubMed: 21925511

Assembly members:

Assembly members:
Act2-EF34, polymer, 75 residues, 8071.05 Da.
palladin, polymer, 17 residues, 1777 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
palladin: HGQTPAAFLSALLPSQP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	103
15N chemical shifts	54
1H chemical shifts	54

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	ligand	2

Entities:

Entity 1, protein 75 residues - 8071.05 Da.

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

Entity 2, ligand 17 residues - 1777 Da.

Residues 235-252 of 90kDa (isoform #4) of palladin

1

HIS

GLY

GLN

THR

PRO

ALA

PHE

LEU

SER

2

ALA

LEU

PRO

SER

GLN

PRO

Samples:

sample_1: Act2-EF34, [U-100% 15N], 0.2 – 0.5 mM; palladin0.5 – 2 mM; D2O 10%; sodium azide 0.05 mM; TCEP2 – 5 mM; MOPS 20 mM; sodium chloride 10 mM; H2O 90%

sample_2: Act2-EF34, [U-100% 13C; U-100% 15N], 0.2 – 0.5 mM; palladin0.5 – 2 mM; D2O 10%; sodium azide 0.05 mM; TCEP2 – 5 mM; MOPS 20 mM; sodium chloride 10 mM; H2O 90%

sample_conditions_1: ionic strength: 0.01 M; pH: 6.6; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRViewJ v8.1, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 700 MHz
Varian INOVA 700 MHz

BMRB	17627 4453 4454
PDB	1H8B 4D1E
DBJ	BAB22865 BAD92758 BAG37672 BAH11921 BAH12587 BAA76836 BAG09933
EMBL	CAB61269
GB	AAA51583 AAF76325 AAH47901 AAH51770 AAH89579 AAG00079 EDL87206
REF	NP_001029807 NP_001094 NP_001163796 NP_001230595 NP_001265272 XP_004852973 XP_004852974 XP_005003446 XP_005369855 XP_005369857
SP	P35609 Q3ZC55 Q9JI91
AlphaFold	P35609 Q3ZC55 Q9JI91