BMRB Entry 11572

Name: Chemical shift assignments of the human Smoothelin CH domain
Published: 2018-12-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11572

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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:

Chemical shift assignments of the human Smoothelin CH domain

Deposition date:

2014-07-31

Original release date:

2018-12-11

Authors:

Kasai, Takuma; Koshiba, Seizo; Yokoyama, Jun; Kigawa, Takanori

Citation:

Citation: Kasai, Takuma; Koshiba, Seizo; Yokoyama, Jun; Kigawa, Takanori. "Stable isotope labeling strategy based on coding theory." J. Biomol. NMR 63, 213-221 (2015).
PubMed: 26293126

Assembly members:

Assembly members:
Smoothelin_CH_domain, polymer, 116 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free Vector: P120404-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Smoothelin_CH_domain: GIKQMLLDWCRAKTRGYEHV DIQNFSSSWSDGMAFCALVH NFFPEAFDYGQLSPQNRRQN FEVAFSSAETHADCPQLLDT EDMVRLREPDWKCVYTYIQE FYRCLVQKGLVKTKKS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	352
15N chemical shifts	125
1H chemical shifts	74

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Smoothelin CH domain	1

Entities:

Entity 1, Smoothelin CH domain 116 residues - Formula weight is not available

Residue 1 represents a non-native cloning artifact. This is the CH domain of human Smoothelin protein.

1

GLY

ILE

LYS

GLN

MET

LEU

ASP

TRP

CYS

2

ARG

ALA

LYS

THR

ARG

GLY

TYR

GLU

HIS

VAL

3

ASP

ILE

GLN

ASN

PHE

SER

TRP

SER

4

ASP

GLY

MET

ALA

PHE

CYS

ALA

LEU

VAL

HIS

5

ASN

PHE

PRO

GLU

ALA

PHE

ASP

TYR

GLY

6

GLN

LEU

SER

PRO

GLN

ASN

ARG

GLN

ASN

7

PHE

GLU

VAL

ALA

PHE

SER

ALA

GLU

THR

8

HIS

ALA

ASP

CYS

PRO

GLN

LEU

ASP

THR

9

GLU

ASP

MET

VAL

ARG

LEU

ARG

GLU

PRO

ASP

10

TRP

LYS

CYS

VAL

TYR

THR

TYR

ILE

GLN

GLU

11

PHE

TYR

ARG

CYS

LEU

VAL

GLN

LYS

GLY

LEU

12

VAL

LYS

THR

LYS

SER

Samples:

sample_1: Smoothelin CH domain, [U-13C; U-15N], 0.9 mM; Tris-Cl, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02 % (w/v); H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY aromatic	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

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe v20130801, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis

Kujira v0.9843, Naohiro Kobayashi - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 700 MHz

UNP	P53814-5
AlphaFold	Q9UIT2