BMRB Entry 26700

Name: Backbone assignment of Sam68 STAR domain
Published: 2016-01-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26700

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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:

Backbone assignment of Sam68 STAR domain

Deposition date:

2015-11-04

Original release date:

2016-01-06

Authors:

Foot, Jaelle; Dominguez, Cyril

Citation:

Citation: Feracci, Mikael; Foot, Jaelle; Grellscheid, Sushma; Danilenko, Marina; Stehle, Ralf; Gonchar, Oksana; Kang, Hyun-Seo; Dalgliesh, Caroline; Meyer, Helge; Liu, Yilei; Lahat, Albert; Sattler, Michael; Eperon, Ian; Elliott, David; Dominguez, Cyril. "Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68" Nat. Commun. 7, 10355-10355 (2016).
PubMed: 26758068

Assembly members:

Assembly members:
Sam68, polymer, 189 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: recombinant technology Host organism: Escherichia coli Vector: pLEICS-01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sam68: GAMEPENKYLPELMAEKDSL DPSFTHAMQLLTAEIEKIQK GDSKKDDEENYLDLFSHKNM KLKERVLIPVKQYPKFNFVG KILGPQGNTIKRLQEETGAK ISVLGKGSMRDKAKEEELRK GGDPKYAHLNMDLHVFIEVF GPPCEAYALMAHAMEEVKKF LVPDMMDDICQEQFLELSYL NGVPEPSRG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	144
1H chemical shifts	144

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sam68	1

Entities:

Entity 1, Sam68 189 residues - Formula weight is not available

residues 1 and 2 are non-native amino acids from the tag after Tev cleavage

1

GLY

ALA

MET

GLU

PRO

GLU

ASN

LYS

TYR

LEU

2

PRO

GLU

LEU

MET

ALA

GLU

LYS

ASP

SER

LEU

3

ASP

PRO

SER

PHE

THR

HIS

ALA

MET

GLN

LEU

4

LEU

THR

ALA

GLU

ILE

GLU

LYS

ILE

GLN

LYS

5

GLY

ASP

SER

LYS

ASP

GLU

ASN

6

TYR

LEU

ASP

LEU

PHE

SER

HIS

LYS

ASN

MET

7

LYS

LEU

LYS

GLU

ARG

VAL

LEU

ILE

PRO

VAL

8

LYS

GLN

TYR

PRO

LYS

PHE

ASN

PHE

VAL

GLY

9

LYS

ILE

LEU

GLY

PRO

GLN

GLY

ASN

THR

ILE

10

LYS

ARG

LEU

GLN

GLU

THR

GLY

ALA

LYS

11

ILE

SER

VAL

LEU

GLY

LYS

GLY

SER

MET

ARG

12

ASP

LYS

ALA

LYS

GLU

LEU

ARG

LYS

13

GLY

ASP

PRO

LYS

TYR

ALA

HIS

LEU

ASN

14

MET

ASP

LEU

HIS

VAL

PHE

ILE

GLU

VAL

PHE

15

GLY

PRO

CYS

GLU

ALA

TYR

ALA

LEU

MET

16

ALA

HIS

ALA

MET

GLU

VAL

LYS

PHE

17

LEU

VAL

PRO

ASP

MET

ASP

ILE

CYS

18

GLN

GLU

GLN

PHE

LEU

GLU

LEU

SER

TYR

LEU

19

ASN

GLY

VAL

PRO

GLU

PRO

SER

ARG

GLY

Samples:

sample_1: Sam68, [U-15N], 0.5 ± 0.1 mM; Sam68, [U-13C; U-15N], 1 ± 0.1 mM; H2O 93%; D2O 7%; Tris 10 mM; NaCl 100 mM; beta-mercapto-ethanol 0.1%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.110, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DRX 800 MHz

UNP	Q07666
AlphaFold	Q99760