BMRB Entry 27692

Name: Backbone Chemical Shift Assignments for Ca+-Bound Calmodulin Mutant (D21A/D23A/D25A/E32A D57A/D59A/N61A/E68A) Bound to CaV1.2 IQ Motif
Published: 2019-03-28

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PDB ID: 7l8v
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27692
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:

Backbone Chemical Shift Assignments for Ca+-Bound Calmodulin Mutant (D21A/D23A/D25A/E32A D57A/D59A/N61A/E68A) Bound to CaV1.2 IQ Motif

Deposition date:

2018-11-16

Original release date:

2019-03-28

Authors:

Ames, James; Salveson, Ian

Citation:

Citation: Salveson, Ian; Anderson, David; Hell, Johannes; Ames, James. "Chemical shift assignments of a calmodulin intermediate with two Ca2+ bound in complex with the IQ-motif of voltage-gated Ca2+ channels (CaV1.2)" Biomol. NMR Assign. 13, 233-237 (2019).
PubMed: 30788773

Assembly members:

Assembly members:
Calmodulin, polymer, 149 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calmodulin: MADQLTEEQIAEFKEAFSLF AKAGAGTITTKALGTVMRSL GQNPTEAELQDMINEVAAAG AGTIDFPAFLTMMARKMKDT DSEEEIREAFRVFDKDGNGY ISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYE EFVQMMTAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	442
15N chemical shifts	124
1H chemical shifts	538

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Calmodulin	1

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

ALA

LYS

ALA

GLY

ALA

GLY

THR

ILE

THR

4

LYS

ALA

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

ALA

GLY

7

ALA

GLY

THR

ILE

ASP

PHE

PRO

ALA

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

Samples:

sample_1: Calmodulin, [U-100% 13C; U-100% 15N; U-80% 2H], 0.75 mM; CaV1.2 IQ motif 1 mM; CaCl2 2mM mM

sample_2: Calmodulin, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; CaV1.2 IQ motif 0.75 mM; CaCl2 2 mM

sample_conditions_1: ionic strength: 0.2338 M; pH: 7.5; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 0.15992 M; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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