BMRB Entry 18905

Name: NMR structure of the RRM2 domain of the protein RBM10 from homo sapiens
Published: 2013-02-01

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PDB ID: 2m2b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18905
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of the RRM2 domain of the protein RBM10 from homo sapiens

Deposition date: 2012-12-17 Original release date: 2013-02-01

Authors: Serrano, Pedro; Geralt, Michael; Dutta, Samit; Wuthrich, Kurt; Wrobel, Russell; Makino, Shi-Ichi; Misenhiemer, Tina; Markley, John; Fox, Brian

Citation: Serrano, Pedro; Wuthrich, Kurt. "NMR structure of the RRM2 domain of the protein RBM10 from homo sapiens" Not known ., .-..

Assembly members:
entity, polymer, 131 residues, 13784.618 Da.

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

Experimental source: Production method: obtained from a collaborator Host organism: wheat germ - cell free

Entity Sequences (FASTA):
entity: QAQGVLASQALSQGSEPSSE NANDTIILRNLNPHSTMDSI LGALAPYAVLSSSNVRVIKD KQTQLNRGFAFIQLSTIEAA QLLQILQALHPPLTIDGKTI NVEFAKGSKRDMASNEGSRI SAASVASTAIA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	124
1H chemical shifts	766

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM2 domain of the protein RBM10 from homo sapiens	1

Entities:

Entity 1, RRM2 domain of the protein RBM10 from homo sapiens 131 residues - 13784.618 Da.

1

GLN

ALA

GLN

GLY

VAL

LEU

ALA

SER

GLN

ALA

2

LEU

SER

GLN

GLY

SER

GLU

PRO

SER

GLU

3

ASN

ALA

ASN

ASP

THR

ILE

LEU

ARG

ASN

4

LEU

ASN

PRO

HIS

SER

THR

MET

ASP

SER

ILE

5

LEU

GLY

ALA

LEU

ALA

PRO

TYR

ALA

VAL

LEU

6

SER

ASN

VAL

ARG

VAL

ILE

LYS

ASP

7

LYS

GLN

THR

GLN

LEU

ASN

ARG

GLY

PHE

ALA

8

PHE

ILE

GLN

LEU

SER

THR

ILE

GLU

ALA

9

GLN

LEU

GLN

ILE

LEU

GLN

ALA

LEU

HIS

10

PRO

LEU

THR

ILE

ASP

GLY

LYS

THR

ILE

11

ASN

VAL

GLU

PHE

ALA

LYS

GLY

SER

LYS

ARG

12

ASP

MET

ALA

SER

ASN

GLU

GLY

SER

ARG

ILE

13

SER

ALA

SER

VAL

ALA

SER

THR

ALA

ILE

14

ALA

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 0.6 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 10 mM; sodium azide 5 mM; DTT 2 mM; H2O 95%; D20 5%

sample_conditions_1: ionic strength: 0.220 M; pH: 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-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
4D APSY HACANH	sample_1	isotropic	sample_conditions_1
5D APSY CBCACONH	sample_1	isotropic	sample_conditions_1
5D APSY HACACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2M2B
DBJ	BAA12144 BAC31087 BAC40753 BAE39715 BAF85447
GB	AAH03089 AAH93519 AIC55382 EAW59284 EAW59287
REF	NP_001161248 NP_001191395 NP_690595 NP_690600 XP_003135120
SP	P70501
TPG	DAA12903

Biological Magnetic Resonance Data Bank