BMRB Entry 16032

Name: Nav1.2 C-terminal EF-Hand Domain
Published: 2009-01-20

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PDB ID: 2kav
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16032
MolProbity Validation Chart

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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:

Nav1.2 C-terminal EF-Hand Domain

Deposition date:

2008-11-15

Original release date:

2009-01-20

Authors:

Miloushev, Vesselin; Levine, Joshua; Arbing, Mark; Hunt, John; Pitt, Geoff; Palmer, Arthur

Citation:

Citation: Miloushev, Vesselin; Levine, Joshua; Arbing, Mark; Hunt, John; Pitt, Geoff; Palmer, Arthur. "Solution structure of the NaV1.2 C-terminal EF-hand domain." J. Biol. Chem. 284, 6446-6454 (2009).
PubMed: 19129176

Assembly members:

Assembly members:
NaV1.2 C-terminal EF-hand domain, polymer, 129 residues, 12130.777 Da.

Natural source:

Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NaV1.2 C-terminal EF-hand domain: MGSSHHHHHHSSGLVPRGSH MASENFSVATEESAEPLSED DFEMFYEVWEKFDPDATQFI EFAKLSDFADALDPPLLIAK PNKVQLIAMDLPMVSGDRIH CLDILFAFTKRVLGESGEMD ALRIQMEER

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
conformer_family_coord_set

Data type	Count
13C chemical shifts	344
15N chemical shifts	101
1H chemical shifts	751

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NaV1.2 C-terminal EF-hand domain	1

Entities:

Entity 1, NaV1.2 C-terminal EF-hand domain 129 residues - 12130.777 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

SER

GLU

ASN

PHE

SER

VAL

ALA

THR

4

GLU

SER

ALA

GLU

PRO

LEU

SER

GLU

ASP

5

ASP

PHE

GLU

MET

PHE

TYR

GLU

VAL

TRP

GLU

6

LYS

PHE

ASP

PRO

ASP

ALA

THR

GLN

PHE

ILE

7

GLU

PHE

ALA

LYS

LEU

SER

ASP

PHE

ALA

ASP

8

ALA

LEU

ASP

PRO

LEU

ILE

ALA

LYS

9

PRO

ASN

LYS

VAL

GLN

LEU

ILE

ALA

MET

ASP

10

LEU

PRO

MET

VAL

SER

GLY

ASP

ARG

ILE

HIS

11

CYS

LEU

ASP

ILE

LEU

PHE

ALA

PHE

THR

LYS

12

ARG

VAL

LEU

GLY

GLU

SER

GLY

GLU

MET

ASP

13

ALA

LEU

ARG

ILE

GLN

MET

GLU

ARG

Samples:

13C-15N: entity, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; glycine, [D5-98%], 100 ± 10 mM; TRIS, [D11-98 %], 20 ± 2 mM; EDTA, [D16-98%], 0.1 ± 0.01 mM; D2O, [U-99% 2H], 10 ± 1 %; DTT, [D10-98%], 1 ± 0.1 mM; NaN3 0.02 ± 0.002 %

10%13-C: entity, [U-10% 13C; U-99% 15N], 0.5 ± 0.05 mM; glycine, [D5-98%], 100 ± 10 mM; TRIS, [D11-98 %], 20 ± 2 mM; EDTA, [D16-98%], 0.1 ± 0.01 mM; D2O, [U-99% 2H], 10 ± 1 %; DTT, [D10-98%], 1 ± 0.1 mM; NaN3 0.02 ± 0.002 %

phage: entity, [U-99% 13C; U-99% 15N], 0.5 ± 0.05 mM; glycine, [D5-98%], 100 ± 10 mM; TRIS, [D11-98 %], 20 ± 2 mM; EDTA, [D16-98%], 0.1 ± 0.01 mM; D2O, [U-99% 2H], 10 ± 1 %; DTT, [D10-98%], 1 ± 0.1 mM; NaN3 0.02 ± 0.002 %; pF1 phage 15 ± 1 mg

sample_conditions: ionic strength: 0.1 M; pH: 7.4; pressure: 1.0 atm; temperature: 290.5 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	13C-15N	isotropic	sample_conditions
3D HNCA	13C-15N	isotropic	sample_conditions
3D HN(CO)CA	13C-15N	isotropic	sample_conditions
3D HN(CA)CO	13C-15N	isotropic	sample_conditions
3D HNCACB	13C-15N	isotropic	sample_conditions
3D CBCA(CO)NH	13C-15N	isotropic	sample_conditions
3D HCCH-TOCSY	13C-15N	isotropic	sample_conditions
3D HBHA(CO)NH	13C-15N	isotropic	sample_conditions
3D 1H-15N NOESY	13C-15N	isotropic	sample_conditions
3D 1H-13C NOESY	13C-15N	isotropic	sample_conditions
2D 1H-13C HSQC	10%13-C	isotropic	sample_conditions
3D HCACO	phage	anisotropic	sample_conditions
2D IPAP HSQC	phage	anisotropic	sample_conditions
3D quant HNCO	phage	anisotropic	sample_conditions
3D CCa HNCO	phage	anisotropic	sample_conditions

Software:

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

ARIA v2.2, Linge, O'Donoghue and Nilges - initial structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - initial structure solution

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 700 MHz

PDB	2KAV 4JPZ
DBJ	BAA92594 BAC27748 BAC30078 BAG63295 BAK62861
EMBL	CAA27287 CAA46438 CAA68735 CAB85895
GB	AAA18895 AAA67695 AAB22226 AAG53412 AAG53413
PIR	S29185
PRF	1204264B
REF	NP_001035232 NP_001035233 NP_001075145 NP_001075146 NP_001092768
SP	P04775 P08104 Q99250 Q9NY46
TPG	DAA32692 DAA32708 DAA32709 DAA32710 DAA32711
AlphaFold	P04775 P08104 Q99250 Q9NY46