BMRB Entry 19792

Name: NMR structure of the RRM domain of RBMX from homo sapiens
Published: 2014-03-10

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PDB ID: 2mks
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19792
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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 RRM domain of RBMX from homo sapiens

Deposition date:

2014-02-14

Original release date:

2014-03-10

Authors:

Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Serrano, Pedro; Wuthrich, Kurt; Geralt, Michael; Dutta, Samit. "NMR structure of the first RRM domain of the protein RBM39 from homo sapiens" .

Assembly members:

Assembly members:
entity, polymer, 92 residues, 10093.535 Da.

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: pSpeedET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GHMVEADRPGKLFIGGLNTE TNEKALEAVFGKYGRIVEVL LMKDRETNKSRGFAFVTFES PADAKDAARDMNGKSLDGKA IKVEQATKPSFE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	366
15N chemical shifts	92
1H chemical shifts	581

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RBMX	1

Entities:

Entity 1, RBMX 92 residues - 10093.535 Da.

1

GLY

HIS

MET

VAL

GLU

ALA

ASP

ARG

PRO

GLY

2

LYS

LEU

PHE

ILE

GLY

LEU

ASN

THR

GLU

3

THR

ASN

GLU

LYS

ALA

LEU

GLU

ALA

VAL

PHE

4

GLY

LYS

TYR

GLY

ARG

ILE

VAL

GLU

VAL

LEU

5

LEU

MET

LYS

ASP

ARG

GLU

THR

ASN

LYS

SER

6

ARG

GLY

PHE

ALA

PHE

VAL

THR

PHE

GLU

SER

7

PRO

ALA

ASP

ALA

LYS

ASP

ALA

ARG

ASP

8

MET

ASN

GLY

LYS

SER

LEU

ASP

GLY

LYS

ALA

9

ILE

LYS

VAL

GLU

GLN

ALA

THR

LYS

PRO

SER

10

PHE

GLU

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 10 mM; sodium azide 5 mM; DTT 2 mM

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, Guntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

CAra, Keller and Wuthrich - chemical shift assignment, data analysis

UNIO, UNIO Herrmann and Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

BMRB	19382
PDB	2MB0 2MKS
DBJ	BAC31099 BAE00972 BAE22448 BAE37998 BAF62396
EMBL	CAA80599 CAB51361 CAB51362 CAG31684 CAI46148
GB	AAH03710 AAH06550 AAH07435 AAH11441 AAH12942
PIR	S41766
REF	NP_001020834 NP_001073196 NP_001100890 NP_001128678 NP_001156008
SP	A5A6M3 D4AE41 P38159 P84586 Q4R7F0
TPG	DAA13328 DAA13329
AlphaFold	A5A6M3 D4AE41 P38159 P84586 Q4R7F0