BMRB Entry 17727

Name: 3D ssNMR structure of membrane embedded KcsA-Kv1.3 channel (Closed state)
Published: 2012-06-21

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PDB ID: 2les
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17727
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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:

3D ssNMR structure of membrane embedded KcsA-Kv1.3 channel (Closed state)

Deposition date:

2011-08-11

Original release date:

2012-06-21

Authors:

Nand, D.; Ader, C.; Prokofyev, A.; Hornig, S.; A Bonvin, M.; Killian, A.; Becker, S.; Pongs, O.; Baldus, M.

Citation:

Citation: van der Cruijsen, Elwin; Nand, Deepak; Weingarth, Markus; Prokofyev, Alexander; Hornig, Sonke; Cukkemane, Abhishek Arun; Bonvin, Alexandre M J J; Becker, Stefan; Hulse, Raymond; Perozo, Eduardo; Pongs, Olaf; Baldus, Marc. "Importance of lipid-pore loop interface for potassium channel structure and function." Proc. Natl. Acad. Sci. U.S.A. 110, 13008-13013 (2013).
PubMed: 23882077

Assembly members:

Assembly members:
KcsA-Kv1.3_(Closed_state), polymer, 94 residues, 9775.335 Da.

Natural source:

Natural source: Common Name: Streptomyces lividans Taxonomy ID: 1916 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces lividans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE32

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KcsA-Kv1.3_(Closed_state): SALHWRAAGAATVLLVIVLL AGSYLAVLAEADDPTSGFSS IPDALWWSVETATTVGYGDL YPVTLWGRCVAVVVMVAGIT SFGLVTAALATWFV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	270
15N chemical shifts	41

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KcsA-Kv1.3 (Closed state)_1	1
2	KcsA-Kv1.3 (Closed state)_2	1
3	KcsA-Kv1.3 (Closed state)_3	1
4	KcsA-Kv1.3 (Closed state)_4	1

Entities:

Entity 1, KcsA-Kv1.3 (Closed state)_1 94 residues - 9775.335 Da.

1

SER

ALA

LEU

HIS

TRP

ARG

ALA

GLY

ALA

2

ALA

THR

VAL

LEU

VAL

ILE

VAL

LEU

3

ALA

GLY

SER

TYR

LEU

ALA

VAL

LEU

ALA

GLU

4

ALA

ASP

PRO

THR

SER

GLY

PHE

SER

5

ILE

PRO

ASP

ALA

LEU

TRP

SER

VAL

GLU

6

THR

ALA

THR

VAL

GLY

TYR

GLY

ASP

LEU

7

TYR

PRO

VAL

THR

LEU

TRP

GLY

ARG

CYS

VAL

8

ALA

VAL

MET

VAL

ALA

GLY

ILE

THR

9

SER

PHE

GLY

LEU

VAL

THR

ALA

LEU

ALA

10

THR

TRP

PHE

VAL

Samples:

sample_1: KcsA-Kv1.3 (Closed state), [U-100% 13C; U-100% 15N], 50 mM; potassium ions 50 mM; H2O 100%

sample_2: KcsA-Kv1.3 (Closed state), [U-100% 13C; U-100% 15N; U-80% 2H], 5 mM; H2O 100%

sample_conditions_1: pH: 7.4; temperature: 243 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D_13C-13C_CHHC	sample_1	solid	sample_conditions_1
2D_13C-13C_Proton driven spin difussion	sample_2	solid	sample_conditions_1

Software:

CNS_HADDOCK, Brunger, Adams, Clore, Gros, Nilges and Read, (HADDOCK) - structure solution(Monomer)

NMR spectrometers:

Bruker Avance 600, 800 MHz
Bruker AvanceIII 700 MHz