BMRB Entry 25779

Name: Partial 1H, 13C and 15N backbone resonance assignments for the carboxy-terminal RNA recognition motif of Plasmodium falciparum Ser/Arg-rich protein 1
Published: 2018-12-21

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25779

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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:

Partial 1H, 13C and 15N backbone resonance assignments for the carboxy-terminal RNA recognition motif of Plasmodium falciparum Ser/Arg-rich protein 1

Deposition date:

2015-08-28

Original release date:

2018-12-21

Authors:

Ganguly, Akshay; Verma, Garima; Bhavesh, Neel Sarovar

Citation:

Citation: Ganguly, Akshay; Verma, Garima; Bhavesh, Neel Sarovar. "The N-terminal RNA Recognition Motif of PfSR1 Confers Semi-specificity for Pyrimidines during RNA Recognition" J. Mol. Biol. ., .-. (2018).
PubMed: 30500338

Assembly members:

Assembly members:
RRM2, polymer, 84 residues, 9467.6 Da.

Natural source:

Natural source: Common Name: malaria parasite Taxonomy ID: 5833 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM2: GSHMRRGRYVVEVTGLPISG SWQDLKDHLREAGECGHADV FKDGTGEVSFFNKDDMLEAI DKFNGSIFRSHEGEKSKISI RQKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	131
15N chemical shifts	71
1H chemical shifts	71

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM2	1

Entities:

Entity 1, RRM2 84 residues - 9467.6 Da.

Residues G1 to M4 are from the pET28a vector.R107 to K186 are native amino acids of PfSR1-RRM2

1

GLY

SER

HIS

MET

ARG

GLY

ARG

TYR

VAL

2

VAL

GLU

VAL

THR

GLY

LEU

PRO

ILE

SER

GLY

3

SER

TRP

GLN

ASP

LEU

LYS

ASP

HIS

LEU

ARG

4

GLU

ALA

GLY

GLU

CYS

GLY

HIS

ALA

ASP

VAL

5

PHE

LYS

ASP

GLY

THR

GLY

GLU

VAL

SER

PHE

6

PHE

ASN

LYS

ASP

MET

LEU

GLU

ALA

ILE

7

ASP

LYS

PHE

ASN

GLY

SER

ILE

PHE

ARG

SER

8

HIS

GLU

GLY

GLU

LYS

SER

LYS

ILE

SER

ILE

9

ARG

GLN

LYS

Samples:

PfSR1-RRM2: RRM2, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; TCEP 3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 125 mM; pH: 5.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	PfSR1-RRM2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	PfSR1-RRM2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	PfSR1-RRM2	isotropic	sample_conditions_1
3D HNCACB	PfSR1-RRM2	isotropic	sample_conditions_1
3D CBCA(CO)NH	PfSR1-RRM2	isotropic	sample_conditions_1
3D C(CO)NH	PfSR1-RRM2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance III 500 MHz
Bruker Avance III 700 MHz