BMRB Entry 16045

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PDB ID: 2kbi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16045
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments for the C-terminal EF-Hand domain of human cardiac sodium channel NaV1.5

Deposition date:

2008-11-28

Original release date:

2009-02-09

Authors:

Chagot, Benjamin; Potet, Franck; Balser, Jeffrey; Chazin, Walter

Citation:

Citation: Chagot, Benjamin; Potet, Franck; Balser, Jeffrey; Chazin, Walter. "Solution NMR structure of the C-terminal EF-Hand domain of human cardiac sodium channel NaV1.5" J. Biol. Chem. 284, 6436-6445 (2009).
PubMed: 19074138

Assembly members:

Assembly members:
hH1, polymer, 97 residues, 10994.295 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: pBG100

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hH1: GPGSENFSVATEESTEPLSE DDFDMFYEIWEKFDPEATQF IEYSVLSDFADALSEPLRIA KPNQISLINMDLPMVSGDRI HCMDILFAFTKRVLGES

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	381
15N chemical shifts	96
1H chemical shifts	673

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hH1	1

Entities:

Entity 1, hH1 97 residues - 10994.295 Da.

Residues 1-4 represent a non-native affinity tag

1

GLY

PRO

GLY

SER

GLU

ASN

PHE

SER

VAL

ALA

2

THR

GLU

SER

THR

GLU

PRO

LEU

SER

GLU

3

ASP

PHE

ASP

MET

PHE

TYR

GLU

ILE

TRP

4

GLU

LYS

PHE

ASP

PRO

GLU

ALA

THR

GLN

PHE

5

ILE

GLU

TYR

SER

VAL

LEU

SER

ASP

PHE

ALA

6

ASP

ALA

LEU

SER

GLU

PRO

LEU

ARG

ILE

ALA

7

LYS

PRO

ASN

GLN

ILE

SER

LEU

ILE

ASN

MET

8

ASP

LEU

PRO

MET

VAL

SER

GLY

ASP

ARG

ILE

9

HIS

CYS

MET

ASP

ILE

LEU

PHE

ALA

PHE

THR

10

LYS

ARG

VAL

LEU

GLY

GLU

SER

Samples:

sample_1: hH1, [U-100% 13C; U-100% 15N], 1.2 mM; H2O 100%; phosphate 100 mM; NaCl 200 mM; beta-mercaptoethanol 5 mM; NaN3 0.01%

sample_2: hH1 1.2 mM; H2O 100%; phosphate 100 mM; NaCl 200 mM; beta-mercaptoethanol 5 mM; NaN3 0.01%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	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
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection, processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker AMX 600 MHz

BMRB	16031
PDB	2KBI 4DCK 4JQ0
DBJ	BAD12084 BAD12085 BAD92103 BAE27800 BAE27966
EMBL	CAB70096 CAD88248
GB	AAA42114 AAA58644 AAI40814 AAI44622 AAI72643
REF	NP_000326 NP_001002994 NP_001092874 NP_001092875 NP_001153632
SP	P15389 Q14524 Q9JJV9
TPG	DAA34921
AlphaFold	P15389 Q14524 Q9JJV9