BMRB Entry 50233

Name: Model-free analysis of 15N spin-relaxation data for TRBP2-dsRBD1
Published: 2022-02-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50233

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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:

Model-free analysis of 15N spin-relaxation data for TRBP2-dsRBD1

Deposition date:

2020-04-14

Original release date:

2022-02-16

Authors:

Paithankar, Harshad; Chugh, Jeetender

Citation:

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).
PubMed: 35134335

Assembly members:

Assembly members:
entity_1, polymer, 108 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: pSV272

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GGAMSEEEQGSGTTTGCGLP SIEQMLAANPGKTPISLLQE YGTRIGKTPVYDLLKAEGQA HQPNFTFRVTVGDTSCTGQG PSKKAAKHKAAEVALKHLKG GSMLEPAL

Data sets:

heteronucl_NOEs
- heteronucl_NOEs_1
- heteronucl_NOEs_2
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
- heteronucl_T1_relaxation_2
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1
- heteronucl_T2_relaxation_2

Data type	Count
T1 relaxation values	138
T2 relaxation values	138
heteronuclear NOE values	138

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TRBP2-dsRBD1	1

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

Samples:

sample_1: TRBP2-dsRBD1, [U-100% 15N], 1.8 mM; D2O, [U-2H], 10%; DTT 1 mM; sodium phosphate 10 mM; sodium chloride 100 mM; EDTA 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
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

Relax v4.0.3 - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 750 MHz