BMRB Entry 25060

Name: Backbone assignment for cold shock domain 1 of Drosophila Upstream of N-ras bound with RNA
Published: 2014-11-07

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25060

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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 for cold shock domain 1 of Drosophila Upstream of N-ras bound with RNA

Deposition date:

2014-07-01

Original release date:

2014-11-07

Authors:

Wang, Iren; Hennig, Janosch; Sattler, Michael

Citation:

Citation: Hennig, Janosch; Militti, Cristina; Popowicz, Grzegorz; Wang, Iren; Sonntag, Miriam; Geerlof, Arie; Gabel, Frank; Gebauer, Fatima; Sattler, Michael. "Structural basis for the assembly of the Sxl-Unr translation regulatory complex" Nature 515, 287-290 (2014).
PubMed: 25209665

Assembly members:

Assembly members:
cold_shock_domain_1_of_upstream_of_N-ras, polymer, 72 residues, Formula weight is not available
RNA-11mer, polymer, 11 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETtrx-1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cold_shock_domain_1_of_upstream_of_N-ras: GAMATRETGIIEKLLHSYGF IQCCERQARLFFHFSQFSGN IDHLKIGDPVEFEMTYDRRT GKPIASQVSKIA
RNA-11mer: GAGCACGUGAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	207
13C chemical shifts	179
15N chemical shifts	70

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cold shock domain 1 of drosophila UNR	1
2	RNA	2

Entities:

Entity 1, cold shock domain 1 of drosophila UNR 72 residues - Formula weight is not available

Residues 1-4 represent a residual non-native tag

1

GLY

ALA

MET

ALA

THR

ARG

GLU

THR

GLY

ILE

2

ILE

GLU

LYS

LEU

HIS

SER

TYR

GLY

PHE

3

ILE

GLN

CYS

GLU

ARG

GLN

ALA

ARG

LEU

4

PHE

HIS

PHE

SER

GLN

PHE

SER

GLY

ASN

5

ILE

ASP

HIS

LEU

LYS

ILE

GLY

ASP

PRO

VAL

6

GLU

PHE

GLU

MET

THR

TYR

ASP

ARG

THR

7

GLY

LYS

PRO

ILE

ALA

SER

GLN

VAL

SER

LYS

8

ILE

ALA

Entity 2, RNA 11 residues - Formula weight is not available

1

G

A

G

C

A

C

G

U

G

A

2

A

Samples:

sample_1: dCSD1, [U-99% 13C; U-99% 15N], 0.5 mM; RNA-11mer 0.6 mM; sodium phosphate 10 mM; sodium chloride 50 mM; DTT 10 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: temperature: 298 K; pH: 6; pressure: 1 atm; ionic strength: 0.05 M

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	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

Software:

TOPSPIN, Bruker Biospin - collection

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

SPARKY, Goddard - peak picking, data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz

GB	AAF50415.2
BMRB	25059 25078
PDB	4QQB