BMRB Entry 17264

Click here to enlarge.

PDB ID: 2l53
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17264
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel NaV1.5

Deposition date:

2010-10-24

Original release date:

2010-12-22

Authors:

Chagot, Benjamin; Chazin, Walter

Citation:

Citation: Chagot, Benjamin; Chazin, Walter. "Solution NMR Structure of Apo-Calmodulin in Complex with the IQ Motif of Human Cardiac Sodium Channel NaV1.5." J. Mol. Biol. 406, 106-119 (2011).
PubMed: 21167176

Assembly members:

Assembly members:
calmodulin, polymer, 148 residues, 16721.465 Da.
IQ_motif, polymer, 31 residues, 3529.137 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
IQ_motif: GPGSEEVSAMVIQRAFRRHL LQRSLKHASFL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	713
15N chemical shifts	193
1H chemical shifts	1236

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	calmodulin	1
2	IQ_motif	2

Entities:

Entity 1, calmodulin 148 residues - 16721.465 Da.

1

ALA

ASP

GLN

LEU

THR

GLU

GLN

ILE

ALA

2

GLU

PHE

LYS

GLU

ALA

PHE

SER

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

THR

8

MET

ALA

ARG

LYS

MET

LYS

ASP

THR

ASP

9

SER

GLU

ILE

ARG

GLU

ALA

PHE

ARG

10

VAL

PHE

ASP

LYS

ASP

GLY

ASN

GLY

TYR

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

GLN

VAL

ASN

TYR

GLU

15

PHE

VAL

GLN

MET

THR

ALA

LYS

Entity 2, IQ_motif 31 residues - 3529.137 Da.

first 4 are cloning artefacts

1

GLY

PRO

GLY

SER

GLU

VAL

SER

ALA

MET

2

VAL

ILE

GLN

ARG

ALA

PHE

ARG

HIS

LEU

3

LEU

GLN

ARG

SER

LEU

LYS

HIS

ALA

SER

PHE

4

LEU

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Related Database Links:

BMRB	15184 15185 15186 15187 15188 15191 15470 15624 15650 15852 1634 16418 16465 1648 16764 17360 17771 17807 18027 18028 18556 19036 19238 19586 19604 25253 25257 26503 26626 26627 4056 4270 4284 4310
PDB	1A29 1CFC 1CFD 1CFF 1CKK 1CLL 1CM1 1CM4 1CTR 1DMO 1G4Y 1IQ5 1IWQ 1K90 1K93 1L7Z 1LIN 1LVC 1MUX 1MXE 1NWD 1OOJ 1PRW 1QIV 1QIW 1QX5 1S26 1SK6 1SY9 1UP5 1WRZ 1X02 1XA5 1XFU 1XFV 1XFW 1XFY 1XFZ 1Y0V 1YR5 2BBM 2BBN 2BCX 2BKH 2BKI 2DFS 2F2O 2F2P 2F3Y 2F3Z 2FOT 2HQW 2JZI 2K0E 2K0F 2K0J 2K61 2KDU 2KNE 2L53 2L7L 2LGF 2LL6 2LL7 2LV6 2M0J 2M0K 2M55 2MG5 2MGU 2O5G 2O60 2R28 2V01 2V02 2VAS 2VAY 2VB6 2W73 2WEL 2X0G 2X51 2Y4V 2YGG 3BXK 3BXL 3BYA 3CLN 3DVE 3DVJ 3DVK 3DVM 3EK4 3EK7 3EK8 3EKH 3EVU 3EVV 3EWT 3EWV 3G43 3GN4 3GOF 3HR4 3IF7 3J41 3L9I 3O77 3O78 3OXQ 3SG2 3SG3 3SG4 3SG5 3SG6 3SG7 3SJQ 3SUI 3U0K 3WFN 4ANJ 4BW7 4BW8 4BYF 4CLN 4DBP 4DBQ 4DCK 4DJC 4E50 4EHQ 4G27 4G28 4HEX 4IK1 4IK3 4IK4 4IK5 4IK8 4IK9 4J9Y 4J9Z 4JPZ 4JQ0 4L79 4LZX 4M1L 4PJJ 4Q5U 4QNH 4R8G 4UMO 4UPU 4V0C 2L53 4DCK 4JQ0
DBJ	BAA08302 BAA11896 BAA19786 BAA19787 BAA19788 BAD12084 BAD12085 BAD92103
EMBL	CAA10601 CAA32050 CAA32062 CAA32119 CAA32120
GB	AAA35635 AAA35641 AAA37365 AAA40862 AAA40863 AAA58644 AAI40814 AAI44622 AAK74065 AAN61120
PIR	JC1305 MCON
PRF	0409298A 0608335A
REF	NP_001008160 NP_001009759 NP_001027633 NP_001039714 NP_001040234 NP_000326 NP_001092874 NP_001092875 NP_001153632 NP_001153633
SP	O02367 O16305 O96081 P02594 P05932 Q14524
TPG	DAA13808 DAA18029 DAA19590 DAA24777 DAA24988
AlphaFold	O02367 O16305 O96081 P02594 P05932 Q14524

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

BMRB Entry 17264

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: