BMRB Entry 52071

Name: Backbone assignment of Ca2+ bound Arabidopsis thaliana Calmodulin1
Published: 2023-09-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52071

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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 assignment of Ca2+ bound Arabidopsis thaliana Calmodulin1

Deposition date:

2023-08-07

Original release date:

2023-09-30

Authors:

Pedretti, Marco; Favretto, Filippo; Troilo, Francesca; Giovannoni, Moira; Conter, Carolina; Mattei, Benedetta; Dominici, Paola; Travaglini-Allocatelli, Carlo; Di Matteo, Adele; Astegno, Alessandra

Citation:

Citation: Pedretti, Marco; Favretto, Filippo; Troilo, Francesca; Giovannoni, Moira; Conter, Carolina; Mattei, Benedetta; Dominici, Paola; Travaglini-Allocatelli, Carlo; Di Matteo, Adele; Astegno, Alessandra. "Role of myristoylation in modulating PCaP1 interaction with calmodulin" Plant Physiol. Biochem. 203, 108003-108003 (2023).
PubMed: 37717348

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET12b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MADQLTDEQISEFKEAFSLF DKDGDGCITTKELGTVMRSL GQNPTEAELQDMINEVDADG NGTIDFPEFLNLMAKKMKDT DSEEELKEAFRVFDKDQNGF ISAAELRHVMTNLGEKLTDE EVEEMIREADVDGDGQINYE EFVKIMMAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	427
15N chemical shifts	144
1H chemical shifts	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AtCaM1 calcium bound	1
2	calcium ion, 1	2
3	calcium ion, 2	2
4	calcium ion, 3	2
5	calcium ion, 4	2

Entities:

Entity 1, AtCaM1 calcium bound 149 residues - Formula weight is not available

1

MET

ALA

ASP

GLN

LEU

THR

ASP

GLU

GLN

ILE

2

SER

GLU

PHE

LYS

GLU

ALA

PHE

SER

LEU

PHE

3

ASP

LYS

ASP

GLY

ASP

GLY

CYS

ILE

THR

4

LYS

GLU

LEU

GLY

THR

VAL

MET

ARG

SER

LEU

5

GLY

GLN

ASN

PRO

THR

GLU

ALA

GLU

LEU

GLN

6

ASP

MET

ILE

ASN

GLU

VAL

ASP

ALA

ASP

GLY

7

ASN

GLY

THR

ILE

ASP

PHE

PRO

GLU

PHE

LEU

8

ASN

LEU

MET

ALA

LYS

MET

LYS

ASP

THR

9

ASP

SER

GLU

LEU

LYS

GLU

ALA

PHE

10

ARG

VAL

PHE

ASP

LYS

ASP

GLN

ASN

GLY

PHE

11

ILE

SER

ALA

GLU

LEU

ARG

HIS

VAL

MET

12

THR

ASN

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

13

GLU

VAL

GLU

MET

ILE

ARG

GLU

ALA

ASP

14

VAL

ASP

GLY

ASP

GLY

GLN

ILE

ASN

TYR

GLU

15

GLU

PHE

VAL

LYS

ILE

MET

ALA

LYS

Entity 2, calcium ion, 1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: AtCaM1 Ca2+, [U-100% 13C; U-100% 15N], 1.6 mM; KCl 50 mM; TRIS 50 mM; DTT 0.5 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5.2 - chemical shift assignment, peak picking

NMRPipe v9.9 - processing

NMR spectrometers:

Bruker AVANCE III 600 MHz

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