BMRB Entry 51447

Name: Calmodulin bound to the C-terminal calmodulin-binding site of the beta-subunit of the retinal cyclic nucleotide-gated cation channel
Published: 2022-09-19

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PDB ID: 8dgh
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51447
MolProbity Validation Chart

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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:

Calmodulin bound to the C-terminal calmodulin-binding site of the beta-subunit of the retinal cyclic nucleotide-gated cation channel

Deposition date:

2022-05-16

Original release date:

2022-09-19

Authors:

Bej, Aritra; Ames, James

Citation:

Citation: Bej, Aritra; Ames, James. "NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel" Biochemistry 61, 1955-1965 (2022).
PubMed: 36070238

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: 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: pET11b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MADQLTEEQIAEFKEAFSLF DKDGDGTITTKELGTVMRSL GQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDT DSEEEIREAFRVFDKDGNGY ISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYE EFVQMMTAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	498
15N chemical shifts	138
1H chemical shifts	814

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Calmodulin	1
2	Ca ion, 1	2
3	Ca ion, 2	2
4	Ca ion, 3	2
5	Ca ion, 4	2

Entities:

Entity 1, Calmodulin 149 residues - Formula weight is not available

1

MET

ALA

ASP

GLN

LEU

THR

GLU

GLN

ILE

2

ALA

GLU

PHE

LYS

GLU

ALA

PHE

SER

LEU

PHE

3

ASP

LYS

ASP

GLY

ASP

GLY

THR

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

THR

MET

ALA

ARG

LYS

MET

LYS

ASP

THR

9

ASP

SER

GLU

ILE

ARG

GLU

ALA

PHE

10

ARG

VAL

PHE

ASP

LYS

ASP

GLY

ASN

GLY

TYR

11

ILE

SER

ALA

GLU

LEU

ARG

HIS

VAL

MET

12

THR

ASN

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

13

GLU

VAL

ASP

GLU

MET

ILE

ARG

GLU

ALA

ASP

14

ILE

ASP

GLY

ASP

GLY

GLN

VAL

ASN

TYR

GLU

15

GLU

PHE

VAL

GLN

MET

THR

ALA

LYS

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

1

CA

Samples:

sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 400 uM; TRIS, [U-99% 2H], 20 mM; CaCl2 1 mM

sample_2: Calmodulin, [U-99% 13C; U-99% 15N], 400 uM; TRIS, [U-99% 2H], 20 mM; CaCl2 1 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 308 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HBHANH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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