BMRB Entry 50234

Name: 15N-spin relaxation data for TRBP2-dsRBD1 dynamics in presence of D10-RNA
Published: 2022-02-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50234

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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: 15N-spin relaxation data for TRBP2-dsRBD1 dynamics in presence of D10-RNA PubMed: 35134335

Deposition date: 2020-04-14 Original release date: 2022-02-16

Authors: Paithankar, Harshad; Chugh, Jeetender

Citation: Paithankar, Harshad; Tarang, Guneet Singh; Parvez, Firdousi; Marathe, Aniket; Joshi, Manali; Chugh, Jeetender. "Relay of intrinsic microsecond timescale conformational dynamics observed in an RNA-binding domain of TRBP upon enthalpy-driven binding of dsRNA" Biophys. J. ., .-. (2022).

Assembly members:
entity_1, polymer, 108 residues, Formula weight is not available
entity_2, polymer, 10 residues, Formula weight is not available
entity_3, polymer, 10 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSV272

Entity Sequences (FASTA):
entity_1: GGAMSEEEQGSGTTTGCGLP SIEQMLAANPGKTPISLLQE YGTRIGKTPVYDLLKAEGQA HQPNFTFRVTVGDTSCTGQG PSKKAAKHKAAEVALKHLKG GSMLEPAL
entity_2: UUAUAAAUGC
entity_3: GCAUUUAUGA

Data sets:

heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
T1 relaxation values	58
T2 relaxation values	58
heteronuclear NOE values	58

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRBP2-dsRBD1	1
2	D10-RNA, chain 1	2
3	D10-RNA, chain 2	3

Entities:

Entity 1, TRBP2-dsRBD1 108 residues - Formula weight is not available

N-terminal residues GGA are non-native to the protein and are left after the cleavage of the fusion tag using protease.

1

GLY

ALA

MET

SER

GLU

GLN

GLY

2

SER

GLY

THR

GLY

CYS

GLY

LEU

PRO

3

SER

ILE

GLU

GLN

MET

LEU

ALA

ASN

PRO

4

GLY

LYS

THR

PRO

ILE

SER

LEU

GLN

GLU

5

TYR

GLY

THR

ARG

ILE

GLY

LYS

THR

PRO

VAL

6

TYR

ASP

LEU

LYS

ALA

GLU

GLY

GLN

ALA

7

HIS

GLN

PRO

ASN

PHE

THR

PHE

ARG

VAL

THR

8

VAL

GLY

ASP

THR

SER

CYS

THR

GLY

GLN

GLY

9

PRO

SER

LYS

ALA

LYS

HIS

LYS

ALA

10

ALA

GLU

VAL

ALA

LEU

LYS

HIS

LEU

LYS

GLY

11

GLY

SER

MET

LEU

GLU

PRO

ALA

LEU

Entity 2, D10-RNA, chain 1 10 residues - Formula weight is not available

5'-UUAUAAAUGC-3'

1

U

A

U

A

U

G

C

Entity 3, D10-RNA, chain 2 10 residues - Formula weight is not available

5'-GCAUUUAUGA-3'

1

G

C

A

U

A

U

G

A

Samples:

sample_1: TRBP2-dsRBD1, [U-100% 15N], 200 uM; D10-RNA, chain 1 100 uM; D10-RNA, chain 2 100 uM; D2O, [U-2H], 10%; sodium phosphate 10 mM; sodium chloride 10 mM; EDTA 1 mM; DTT 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5 - collection

NMRPipe - processing

NMRFAM-SPARKY - peak picking

NMR spectrometers:

Bruker Avance 600 MHz