BMRB Entry 27489

Name: 1H, 15N, 13C Assignment of rS1-D5
Published: 2018-08-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27489

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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:

1H, 15N, 13C Assignment of rS1-D5

Deposition date:

2018-05-23

Original release date:

2018-08-13

Authors:

Qureshi, Nusrat; Bains, Jasleen; Sreeramulu, Sridhar; Schwalbe, Harald; Fuertig, Boris

Citation:

Citation: Qureshi, Nusrat; Bains, Jasleen; Sreeramulu, Sridhar; Schwalbe, Harald; Fuertig, Boris. "Conformational switch in the ribosomal protein S1 guides unfolding of structured RNAs for translation initiation" Nucleic Acids Res. 46, 10917-10929 (2018).
PubMed: 30124944

Assembly members:

Assembly members:
rS1-D5, polymer, 94 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Vibrio vulnificus Taxonomy ID: 672 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio vulnificus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rS1-D5: GAMAEAQAKGDKVTGKIKSI TDFGIFIGLDGGIDGLVHLS DISWNVAGEETVREFKKGDE ISAVVLAVDAERERISLGIK QMENDPFNAYVADN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	220
15N chemical shifts	91
1H chemical shifts	91

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	rS1-D5	1

Entities:

Entity 1, rS1-D5 94 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

GLU

ALA

GLN

ALA

LYS

GLY

2

ASP

LYS

VAL

THR

GLY

LYS

ILE

LYS

SER

ILE

3

THR

ASP

PHE

GLY

ILE

PHE

ILE

GLY

LEU

ASP

4

GLY

ILE

ASP

GLY

LEU

VAL

HIS

LEU

SER

5

ASP

ILE

SER

TRP

ASN

VAL

ALA

GLY

GLU

6

THR

VAL

ARG

GLU

PHE

LYS

GLY

ASP

GLU

7

ILE

SER

ALA

VAL

LEU

ALA

VAL

ASP

ALA

8

GLU

ARG

GLU

ARG

ILE

SER

LEU

GLY

ILE

LYS

9

GLN

MET

GLU

ASN

ASP

PRO

PHE

ASN

ALA

TYR

10

VAL

ALA

ASP

ASN

Samples:

sample_1: rS1-D5, [U-98% 13C; U-98% 15N], 0.35 mM; potassium phosphate 25 mM; KCl 150 mM; DTT 5 mM

sample_2: rS1-D5, [U-98% 15N], 0.1 mM; potassium phosphate 25 mM; KCl 150 mM; DTT 5 mM

sample_conditions_1: ionic strength: 206 mM; pH: 7.2; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

SPARKY v3.114, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 600 MHz
Bruker Avance 950 MHz

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