BMRB Entry 34498

Name: solution structure of cold-shock domain 9 of drosophila Upstream of N-Ras (Unr)
Published: 2020-07-14

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PDB ID: 6y96
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34498
MolProbity Validation Chart

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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 cold-shock domain 9 of drosophila Upstream of N-Ras (Unr)

Deposition date:

2020-03-06

Original release date:

2020-07-14

Authors:

Sweetapple, L.; Hollmann, N.; Simon, B.; Hennig, J.

Citation:

Citation: Hollmann, N.; Jagtap, P.; Masiewicz, P.; Guitart, T.; Simon, B.; Provaznik, J.; Stein, F.; Haberkant, P.; Sweetapple, L.; Villacorte, L.; Mooijman, D.; Benes, V.; Savitski, M.; Gebauer, F.; Hennig, J.. "Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras" Cell Rep. 32, 107930-107930 (2020).
PubMed: 32697992

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, 10246.532 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAKGDLVSFRIDESGRAACV NAVRQKKRATVDSIKGQFGF LNFEVEDGKKLFFHMSEVQG NTVALHPGDTVEFSVVTNQR NGKSSACNVLKIND

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	360
15N chemical shifts	91
1H chemical shifts	562

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 94 residues - 10246.532 Da.

1

GLY

ALA

LYS

GLY

ASP

LEU

VAL

SER

PHE

ARG

2

ILE

ASP

GLU

SER

GLY

ARG

ALA

CYS

VAL

3

ASN

ALA

VAL

ARG

GLN

LYS

ARG

ALA

THR

4

VAL

ASP

SER

ILE

LYS

GLY

GLN

PHE

GLY

PHE

5

LEU

ASN

PHE

GLU

VAL

GLU

ASP

GLY

LYS

6

LEU

PHE

HIS

MET

SER

GLU

VAL

GLN

GLY

7

ASN

THR

VAL

ALA

LEU

HIS

PRO

GLY

ASP

THR

8

VAL

GLU

PHE

SER

VAL

THR

ASN

GLN

ARG

9

ASN

GLY

LYS

SER

ALA

CYS

ASN

VAL

LEU

10

LYS

ILE

ASN

ASP

Samples:

sample_1: protein, [U-99% 13C; U-99% 15N], 0.24 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM

sample_2: protein, [U-99% 13C; U-99% 15N], 0.24 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 800 MHz

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