BMRB Entry 28036

Name: Shaker-VSD(S2bot_mutant)
Published: 2020-01-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28036

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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:

Shaker-VSD(S2bot_mutant)

Deposition date:

2019-11-04

Original release date:

2020-01-10

Authors:

Chen, Hongbo; Chanda, Baron; Henzler-Wildman, Katherine

Citation:

Citation: Chen, Hongbo; Deng, Jiahua; Cui, Qiang; Chanda, Baron; Henzler-Wildman, Katherine. "Mapping temperature-dependent conformational change in the voltage-sensing domain of an engineered heat-activated K + channel" Proc. Natl. Acad. Sci. U. S. A. 118, e2017280118-e2017280118 (2021).
PubMed: 33782120

Assembly members:

Assembly members:
Shaker-VSD(S2bot_mutant), polymer, 185 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-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Shaker-VSD(S2bot_mutant): GGGGFEYPESSQAARVVAII SVFVILLSIVIFCLETLPEF KHYKVFNTTTNGTKIEEDEV PDITDPFFLIETLCIIWFTF ELTVRFLACPNKLNFCRDVM NVIDIIAIIPYFITLATVVA EEEDTLNLPKAPVSPQDKSS NQAMSLAILRVIRLVRSSRI FKLSRHSKGLQILGRTLKAS MRELG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	510
15N chemical shifts	155
1H chemical shifts	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Shaker-VSD(S2bot_mutant)	1

Entities:

Entity 1, Shaker-VSD(S2bot_mutant) 185 residues - Formula weight is not available

1

GLY

PHE

GLU

TYR

PRO

GLU

SER

2

SER

GLN

ALA

ARG

VAL

ALA

ILE

3

SER

VAL

PHE

VAL

ILE

LEU

SER

ILE

VAL

4

ILE

PHE

CYS

LEU

GLU

THR

LEU

PRO

GLU

PHE

5

LYS

HIS

TYR

LYS

VAL

PHE

ASN

THR

6

ASN

GLY

THR

LYS

ILE

GLU

ASP

GLU

VAL

7

PRO

ASP

ILE

THR

ASP

PRO

PHE

LEU

ILE

8

GLU

THR

LEU

CYS

ILE

TRP

PHE

THR

PHE

9

GLU

LEU

THR

VAL

ARG

PHE

LEU

ALA

CYS

PRO

10

ASN

LYS

LEU

ASN

PHE

CYS

ARG

ASP

VAL

MET

11

ASN

VAL

ILE

ASP

ILE

ALA

ILE

PRO

12

TYR

PHE

ILE

THR

LEU

ALA

THR

VAL

ALA

13

GLU

ASP

THR

LEU

ASN

LEU

PRO

LYS

14

ALA

PRO

VAL

SER

PRO

GLN

ASP

LYS

SER

15

ASN

GLN

ALA

MET

SER

LEU

ALA

ILE

LEU

ARG

16

VAL

ILE

ARG

LEU

VAL

ARG

SER

ARG

ILE

17

PHE

LYS

LEU

SER

ARG

HIS

SER

LYS

GLY

LEU

18

GLN

ILE

LEU

GLY

ARG

THR

LEU

LYS

ALA

SER

19

MET

ARG

GLU

LEU

GLY

Samples:

15N-13C-D_S2bot: H2O 90%; D2O 10%; Shaker-VSD(S2bot_mutant), [U-13C; U-15N; U-2H], 0.35 mM; potassium chloride 50 mM; MOPS 100 mM; LPPG 40 mM; TCEP 4 mM

sample_conditions_1: pH: 6.7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-13C-D_S2bot	isotropic	sample_conditions_1
3D HNCO	15N-13C-D_S2bot	isotropic	sample_conditions_1
3D HNCA	15N-13C-D_S2bot	isotropic	sample_conditions_1
3D HNCACB	15N-13C-D_S2bot	isotropic	sample_conditions_1
3D HN(CO)CA	15N-13C-D_S2bot	isotropic	sample_conditions_1
3D HCACO	15N-13C-D_S2bot	isotropic	sample_conditions_1

Software:

CCPNmr_Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 750 MHz

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