BMRB Entry 27055

Name: NMR structure of the RNA recognition motif 2 (RRM2) of the splicing factor RBM10
Published: 2017-04-25

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27055

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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:

NMR structure of the RNA recognition motif 2 (RRM2) of the splicing factor RBM10

Deposition date:

2017-03-23

Original release date:

2017-04-25

Authors:

Qin, Haina; Serrano, Pedro; Wuthrich, Kurt

Citation:

Citation: Serrano, Pedro; Hammond, John; Geralt, Michael; Wuthrich, Kurt. "Splicing Site Recognition by Synergy of Three Domains in Splicing Factor RBM10" Biochemistry 57, 1563-1567 (2018).
PubMed: 29450990

Assembly members:

Assembly members:
RBM_10RRM2, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RBM_10RRM2: GHMDTIILRNLNPHSTMDSI LGALAPYAVLSSSNVRVIKD KQTQLNRGFAFIQLSTIVEA AQLLQILQALHPPLTIDGKT INVEFAKGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	291
15N chemical shifts	91
1H chemical shifts	606

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RBM10RRM2	1

Entities:

Entity 1, RBM10RRM2 89 residues - Formula weight is not available

1

GLY

HIS

MET

ASP

THR

ILE

LEU

ARG

ASN

2

LEU

ASN

PRO

HIS

SER

THR

MET

ASP

SER

ILE

3

LEU

GLY

ALA

LEU

ALA

PRO

TYR

ALA

VAL

LEU

4

SER

ASN

VAL

ARG

VAL

ILE

LYS

ASP

5

LYS

GLN

THR

GLN

LEU

ASN

ARG

GLY

PHE

ALA

6

PHE

ILE

GLN

LEU

SER

THR

ILE

VAL

GLU

ALA

7

ALA

GLN

LEU

GLN

ILE

LEU

GLN

ALA

LEU

8

HIS

PRO

LEU

THR

ILE

ASP

GLY

LYS

THR

9

ILE

ASN

VAL

GLU

PHE

ALA

LYS

GLY

SER

Samples:

sample_1: RBM 10RRM2, [U-100% 13C], 1.1 mM; sodium azide 5 uM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
APSY 4D ZANH	sample_1	isotropic	sample_conditions_1
APSY 4D ZAONH	sample_1	isotropic	sample_conditions_1
APSY 4D BAONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Braun and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

UNIO, Herrmann - chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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