BMRB Entry 19354

Name: Solution structure of Smoothened
Published: 2014-02-13

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PDB ID: 2mah
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19354
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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:

Solution structure of Smoothened

Deposition date:

2013-07-09

Original release date:

2014-02-13

Authors:

Rana, Rajashree; Lee, Ho-Jin; Zheng, Jie

Citation:

Citation: Rana, Rajashree; Carroll, Candace; Lee, Ho-Jin; Bao, Ju; Marada, Suresh; Grace, Christy; Guibao, Cristina; Ogden, Stacey; Zheng, Jie. "Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling." Nat. Commun. 4, 2965-2965 (2013).
PubMed: 24351982

Assembly members:

Assembly members:
entity, polymer, 128 residues, 15224.935 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SGLVPRGSHMVRRARCYPTS NATNTCFGSKLPYELSSLDL TDFHTEKELNDKLNDYYALK HVPKCWAAIQPFLCAVFKPK CEKINGEDMVYLPSYEMCRI TMEPCRILYNTTFFPKFLRC NETLFPTK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	556
15N chemical shifts	125
1H chemical shifts	926

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Smoothened	1

Entities:

Entity 1, Smoothened 128 residues - 15224.935 Da.

1

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

MET

2

VAL

ARG

ALA

ARG

CYS

TYR

PRO

THR

SER

3

ASN

ALA

THR

ASN

THR

CYS

PHE

GLY

SER

LYS

4

LEU

PRO

TYR

GLU

LEU

SER

LEU

ASP

LEU

5

THR

ASP

PHE

HIS

THR

GLU

LYS

GLU

LEU

ASN

6

ASP

LYS

LEU

ASN

ASP

TYR

ALA

LEU

LYS

7

HIS

VAL

PRO

LYS

CYS

TRP

ALA

ILE

GLN

8

PRO

PHE

LEU

CYS

ALA

VAL

PHE

LYS

PRO

LYS

9

CYS

GLU

LYS

ILE

ASN

GLY

GLU

ASP

MET

VAL

10

TYR

LEU

PRO

SER

TYR

GLU

MET

CYS

ARG

ILE

11

THR

MET

GLU

PRO

CYS

ARG

ILE

LEU

TYR

ASN

12

THR

PHE

PRO

LYS

PHE

LEU

ARG

CYS

13

ASN

GLU

THR

LEU

PHE

PRO

THR

LYS

Samples:

sample_1: entity 200 mM; acetic acid, [U-2H], 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz