BMRB Entry 27017

Name: Backbone and sidechain chemical shift assignments of the complex of calmodulin bound to a beta calcineurin A peptide
Published: 2017-09-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27017

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone and sidechain chemical shift assignments of the complex of calmodulin bound to a beta calcineurin A peptide PubMed: 28815458

Deposition date: 2017-01-27 Original release date: 2017-09-11

Authors: Fowler, C.; Nunez Hernandez, Maria; Shea, Madeline

Citation: Fowler, C.; Nunez Hernandez, Maria; O'Donnell, Susan; Yu, Liping; Shea, Madeline. "Backbone and side-chain resonance assignments of (Ca2+)4-calmodulin bound to beta calcineurin A CaMBD peptide" Biomol. NMR Assign. 11, 275-280 (2017).

Assembly members:
calmodulin, polymer, 148 residues, Formula weight is not available
beta_calcineurin_A_peptide, polymer, 34 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

Natural source: Common Name: Paramecium tetraurelia Taxonomy ID: 5888 Superkingdom: Eukaryota Kingdom: not available Genus/species: Paramecium tetraurelia

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PT7-7

Entity Sequences (FASTA):
calmodulin: AEQLTEEQIAEFKEAFALFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLSLMARKMKEQD SEEELIEAFKVFDRDGNGLI SAAELRHVMTNLGEKLTDDE VDEMIREADIDGDGHINYEE FVRMMVSK
beta_calcineurin_A_peptide: GPGSSAAARKEIIRNKIRAI GKMARVFSVLREES

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chemical_shift_list_2

Data type	Count
13C chemical shifts	798
15N chemical shifts	199
1H chemical shifts	1231

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	calmodulin	1
2	beta calcineurin	2
3	calcium	3

Entities:

Entity 1, calmodulin 148 residues - Formula weight is not available

1

ALA

GLU

GLN

LEU

THR

GLU

GLN

ILE

ALA

2

GLU

PHE

LYS

GLU

ALA

PHE

ALA

LEU

PHE

ASP

3

LYS

ASP

GLY

ASP

GLY

THR

ILE

THR

LYS

4

GLU

LEU

GLY

THR

VAL

MET

ARG

SER

LEU

GLY

5

GLN

ASN

PRO

THR

GLU

ALA

GLU

LEU

GLN

ASP

6

MET

ILE

ASN

GLU

VAL

ASP

ALA

ASP

GLY

ASN

7

GLY

THR

ILE

ASP

PHE

PRO

GLU

PHE

LEU

SER

8

LEU

MET

ALA

ARG

LYS

MET

LYS

GLU

GLN

ASP

9

SER

GLU

LEU

ILE

GLU

ALA

PHE

LYS

10

VAL

PHE

ASP

ARG

ASP

GLY

ASN

GLY

LEU

ILE

11

SER

ALA

GLU

LEU

ARG

HIS

VAL

MET

THR

12

ASN

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

13

VAL

ASP

GLU

MET

ILE

ARG

GLU

ALA

ASP

ILE

14

ASP

GLY

ASP

GLY

HIS

ILE

ASN

TYR

GLU

15

PHE

VAL

ARG

MET

VAL

SER

LYS

Entity 2, beta calcineurin 34 residues - Formula weight is not available

First four residues (GPGS, -4 to -1) are part of a 3C protease cleavage site; beta calcineurin residue S397 is residue 5 of the peptide.

1

GLY

PRO

GLY

SER

ALA

ARG

LYS

2

GLU

ILE

ARG

ASN

LYS

ILE

ARG

ALA

ILE

3

GLY

LYS

MET

ALA

ARG

VAL

PHE

SER

VAL

LEU

4

ARG

GLU

SER

Entity 3, calcium - Ca - 40.078 Da.

1

CA

Samples:

sample_1: calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; beta calcineurin A peptide, [U-99% 13C; U-99% 15N], 0.85 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_2: calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; beta calcineurin A peptide, [U-99% 13C; U-99% 15N], 0.85 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_3: calmodulin, [U-99% 15N], 0.78 mM; beta calcineurin A peptide, [U-99% 15N], 0.78 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_4: calmodulin 0.9 mM; beta calcineurin A peptide 0.9 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_2	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_2	isotropic	sample_conditions_1
2D 1H-1H gCOSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

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

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz

NCBI	AAB20487.1 5532
UniProt	P07463 P16298
AlphaFold	A0DD49 Q8N3W4

Biological Magnetic Resonance Data Bank