BMRB Entry 27111

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Musashi2 RRM1
Published: 2017-12-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27111

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for Musashi2 RRM1

Deposition date:

2017-05-23

Original release date:

2017-12-12

Authors:

Lan, Lan; Xing, Minli; Douglas, Justin; Gao, Philip; Hanzlik, Robert; Xu, Liang

Citation:

Citation: Lan, Lan; Xing, Minli; Kashipathy, Maithri; Douglas, Justin; Gao, Philip; Battaile, Kevin; Hanzlik, Robert; Lovell, Scott; Xu, Liang. "Crystal and solution structures of human oncoprotein Musashi-2 N-terminal RNA recognition motif 1" Proteins 88, 573-583 (2020).
PubMed: 31603583

Assembly members:

Assembly members:
MSI2_RRM1, polymer, 115 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: pTBSG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MSI2_RRM1: MHHHHHHSTSVDLGTENLYF QSNAGKMFIGGLSWQTSPDS LRDYFSKFGEIRECMVMRDP TTKRSRGFGFVTFADPASVD KVLGQPHHELDSKTIDPKVA FPRRAQPKMVTRTKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	216
15N chemical shifts	99
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MSI2 RRM1	1

Entities:

Entity 1, MSI2 RRM1 115 residues - Formula weight is not available

1

MET

HIS

SER

THR

SER

2

VAL

ASP

LEU

GLY

THR

GLU

ASN

LEU

TYR

PHE

3

GLN

SER

ASN

ALA

GLY

LYS

MET

PHE

ILE

GLY

4

GLY

LEU

SER

TRP

GLN

THR

SER

PRO

ASP

SER

5

LEU

ARG

ASP

TYR

PHE

SER

LYS

PHE

GLY

GLU

6

ILE

ARG

GLU

CYS

MET

VAL

MET

ARG

ASP

PRO

7

THR

LYS

ARG

SER

ARG

GLY

PHE

GLY

PHE

8

VAL

THR

PHE

ALA

ASP

PRO

ALA

SER

VAL

ASP

9

LYS

VAL

LEU

GLY

GLN

PRO

HIS

GLU

LEU

10

ASP

SER

LYS

THR

ILE

ASP

PRO

LYS

VAL

ALA

11

PHE

PRO

ARG

ALA

GLN

PRO

LYS

MET

VAL

12

THR

ARG

THR

LYS

Samples:

sample_2: MSI2 RRM1, [U-90% 15N], 0.5 mM; NaCl 150 mM

sample_1: MSI2 RRM1, [U-95% 13C; U-90% 15N], 0.7 mM; MSI2 RRM1, [U-95% 13C; U-90% 15N], 0.6 mM; MSI2 RRM1, [U-95% 13C; U-90% 15N], 0.8 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CCPN, CCPN - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DRX 600 MHz

UNP	Q96DH6-1
AlphaFold	Q8N9T4