BMRB Entry 19642

Name: NMR structure of the first RRM domain of the protein RBM39 from homo sapiens
Published: 2013-12-20

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PDB ID: 2mhn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19642
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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 first RRM domain of the protein RBM39 from homo sapiens

Deposition date:

2013-12-02

Original release date:

2013-12-20

Authors:

Serrano, Pedro; Geralt, Michael; Dutta, Samit; 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, 152 residues, 10574.261 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: GHMNLTPEERDARTVFCMQL AARIRPRDLEEFFSTVGKVR DVRMISDRNSRRSKGIAYVE FVDVSSVPLAIGLTGQRVLG VPIIVQASQAEKNRRRSKGI AYVEFVDVSSVPLAIGLTGQ RVLGVPIIVQASQAEKNRVP IIVQASQAEKNR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	95
1H chemical shifts	643

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 152 residues - 10574.261 Da.

1

GLY

HIS

MET

ASN

LEU

THR

PRO

GLU

ARG

2

ASP

ALA

ARG

THR

VAL

PHE

CYS

MET

GLN

LEU

3

ALA

ARG

ILE

ARG

PRO

ARG

ASP

LEU

GLU

4

GLU

PHE

SER

THR

VAL

GLY

LYS

VAL

ARG

5

ASP

VAL

ARG

MET

ILE

SER

ASP

ARG

ASN

SER

6

ARG

SER

LYS

GLY

ILE

ALA

TYR

VAL

GLU

7

PHE

VAL

ASP

VAL

SER

VAL

PRO

LEU

ALA

8

ILE

GLY

LEU

THR

GLY

GLN

ARG

VAL

LEU

GLY

9

VAL

PRO

ILE

VAL

GLN

ALA

SER

GLN

ALA

10

GLU

LYS

ASN

ARG

SER

LYS

GLY

ILE

11

ALA

TYR

VAL

GLU

PHE

VAL

ASP

VAL

SER

12

VAL

PRO

LEU

ALA

ILE

GLY

LEU

THR

GLY

GLN

13

ARG

VAL

LEU

GLY

VAL

PRO

ILE

VAL

GLN

14

ALA

SER

GLN

ALA

GLU

LYS

ASN

ARG

VAL

PRO

15

ILE

VAL

GLN

ALA

SER

GLN

ALA

GLU

LYS

16

ASN

ARG

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%; D2O 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

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, data analysis, processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MHN 4YUD
DBJ	BAE22477 BAE27657 BAE32977 BAG54289 BAG59582
EMBL	CAD97833 CAE45833 CAE45890 CAH18281 CAH90627
GB	AAA16346 AAA16347 AAH04000 AAH30493 AAH82607
REF	NP_001013225 NP_001125339 NP_001162566 NP_001164806 NP_001193433
SP	Q14498 Q5RC80 Q8VH51
TPG	DAA23046
AlphaFold	Q14498 Q5RC80 Q8VH51