BMRB Entry 19248

Name: Structure of SRSF1 RRM2 in complex with the RNA 5'-UGAAGGAC-3'
Published: 2013-07-08

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PDB ID: 2m8d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19248
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of SRSF1 RRM2 in complex with the RNA 5'-UGAAGGAC-3' PubMed: 23836656

Deposition date: 2013-05-17 Original release date: 2013-07-08

Authors: Clery, Antoine; Sinha, Rahul; Anczukow, Olga; Corrionero, Anna; Moursy, Ahmed; Daubner, Gerrit; Valcarcel, Juan; Krainer, Adrian; Allain, Frederic

Citation: Clery, Antoine; Sinha, Rahul; Anczukow, Olga; Corrionero, Anna; Moursy, Ahmed; Daubner, Gerrit; Valcarcel, Juan; Krainer, Adrian; Allain, Frederic H-T. "Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition." Proc. Natl. Acad. Sci. U.S.A. 110, E2802-E2811 (2013).

Assembly members:
RNA_5'-UGAAGGAC-3, polymer, 8 residues, 2589.643 Da.
SRSF1_RRM2, polymer, 91 residues, 10338.676 Da.

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
RNA_5'-UGAAGGAC-3: UGAAGGAC
SRSF1_RRM2: MAPRGRYGPPSRRSENRVVV SGLPPSGSWQDLKDHMREAG DVCYADVYRDGTGVVEFVRK EDMTYAVRKLDNTKFRSHEG ETAYIRVKVDG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	271
15N chemical shifts	89
1H chemical shifts	638

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNA_5'-UGAAGGAC-3	1
2	SRSF1_RRM2	2

Entities:

Entity 1, RNA_5'-UGAAGGAC-3 8 residues - 2589.643 Da.

1

U

G

A

G

A

C

Entity 2, SRSF1_RRM2 91 residues - 10338.676 Da.

1

MET

ALA

PRO

ARG

GLY

ARG

TYR

GLY

PRO

2

SER

ARG

SER

GLU

ASN

ARG

VAL

3

SER

GLY

LEU

PRO

SER

GLY

SER

TRP

GLN

4

ASP

LEU

LYS

ASP

HIS

MET

ARG

GLU

ALA

GLY

5

ASP

VAL

CYS

TYR

ALA

ASP

VAL

TYR

ARG

ASP

6

GLY

THR

GLY

VAL

GLU

PHE

VAL

ARG

LYS

7

GLU

ASP

MET

THR

TYR

ALA

VAL

ARG

LYS

LEU

8

ASP

ASN

THR

LYS

PHE

ARG

SER

HIS

GLU

GLY

9

GLU

THR

ALA

TYR

ILE

ARG

VAL

LYS

VAL

ASP

10

GLY

Samples:

sample_1: SRSF1_RRM2, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: SRSF1_RRM2, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 5.5; pressure: 1 atm; temperature: 273 K

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
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 700 MHz

BMRB	19203
PDB	1X4C 2M7S 2M8D 2O3D 3BEG 4C0O
DBJ	BAB93456 BAC37367 BAE29641 BAE88160 BAF82622
EMBL	CAH92288
GB	AAA03476 AAA35564 AAA35565 AAH10264 AAH42354
REF	NP_001006919 NP_001033096 NP_001069862 NP_001071635 NP_001103022
SP	Q07955 Q0VCY7 Q3YLA6 Q5R7H2 Q6DII2
TPG	DAA19172

Biological Magnetic Resonance Data Bank