BMRB Entry 52077

Name: TRBP2_dsRBD2 chemical shift assignment and dynamics data.
Published: 2023-09-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52077

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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:

TRBP2_dsRBD2 chemical shift assignment and dynamics data.

Deposition date:

2023-08-12

Original release date:

2023-09-08

Authors:

Parvez, Firdousi

Citation:

Citation: Parvez, Firdousi. "Differential conformational dynamics in two type-A RNA-binding domains drive the double-stranded RNA recognition and binding" .

Assembly members:

Assembly members:
entity_1, polymer, 84 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: pHMGWA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNAQQSECNPVGALQELVVQ KGWRLPEYTVTQESGPAHRK EFTMTCRVERFIEIGSGTSK KLAKRNAAAKMLLRVHTVPL DARD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
- heteronucl_NOEs_2
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
- heteronucl_T1_relaxation_2
heteronucl_T1rho_relaxation
- heteronucl_T1rho_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1
- heteronucl_T2_relaxation_2

Data type	Count
13C chemical shifts	183
15N chemical shifts	73
1H chemical shifts	379
T1 relaxation values	100
T2 relaxation values	98
heteronuclear NOE values	95

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRBP2-dsRBD2	1

Entities:

Entity 1, TRBP2-dsRBD2 84 residues - Formula weight is not available

1

SER

ASN

ALA

GLN

SER

GLU

CYS

ASN

PRO

2

VAL

GLY

ALA

LEU

GLN

GLU

LEU

VAL

GLN

3

LYS

GLY

TRP

ARG

LEU

PRO

GLU

TYR

THR

VAL

4

THR

GLN

GLU

SER

GLY

PRO

ALA

HIS

ARG

LYS

5

GLU

PHE

THR

MET

THR

CYS

ARG

VAL

GLU

ARG

6

PHE

ILE

GLU

ILE

GLY

SER

GLY

THR

SER

LYS

7

LYS

LEU

ALA

LYS

ARG

ASN

ALA

LYS

8

MET

LEU

ARG

VAL

HIS

THR

VAL

PRO

LEU

9

ASP

ALA

ARG

ASP

Samples:

sample_1: TRBP2-dsRBD2 (TAR RNA binding protein isoform 1, second dsRNA binding domain), [U-13C; U-15N], 1.25 mM; TRBP2-dsRBD2 (TAR RNA binding protein isoform 1, second dsRNA binding domain), [U-15N], 1.25 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
T1rho/R1rho relaxation	sample_1	isotropic	sample_conditions_1
T2rho/R2rho relaxation	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

SPARKY - peak picking

Mathematica - data analysis

NMRPipe - processing

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