BMRB Entry 51210

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51210

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone and sidechain 1H, 15N and 13C resonance assignments of the RNA bound tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii PubMed: 35279790

Deposition date: 2021-12-02 Original release date: 2022-12-02

Authors: Hicks, Stephanie; Venters, Ronald; Blackshear, Perry

Citation: Hicks, Stephanie; Venters, Ronald; Blackshear, Perry. "Backbone and sidechain 1H, 15N and 13C resonance assignments of the free and RNA-bound tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii" Biomol. NMR Assign. 16, 153-158 (2022).

Assembly members:
entity_1, polymer, 69 residues, 7784.89 Da.
entity_ZN, non-polymer, 65.409 Da.
entity_3, polymer, 9 residues, 2739.6 Da.

Natural source: Common Name: Selaginella moellendorffii Taxonomy ID: 88036 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Selaginella moellendorffii

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28/30

Entity Sequences (FASTA):
entity_1: NALYKTELCRSWEETGSCRY GNKCQFAHGKEDLRPVNRHP KYKTEVCRTFSAAGTCPYGK RCRFIHATP
entity_3: UUAUUUAUU

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	287
15N chemical shifts	62
1H chemical shifts	422

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tandem Zinc Finger	1
2	Zn1	2
3	Zn2	2
4	9mer RNA	3

Entities:

Entity 1, Tandem Zinc Finger 69 residues - 7784.89 Da.

This tandem zinc finger domain represents residues 10-76 from the full length protein; The first two residues in the assigned chemical shifts list (ASN and ALA) are not part of the S. moellendorfii TTP TZF sequence but are there because of the TEV cleavage site.

1

ASN

ALA

LEU

TYR

LYS

THR

GLU

LEU

CYS

ARG

2

SER

TRP

GLU

THR

GLY

SER

CYS

ARG

TYR

3

GLY

ASN

LYS

CYS

GLN

PHE

ALA

HIS

GLY

LYS

4

GLU

ASP

LEU

ARG

PRO

VAL

ASN

ARG

HIS

PRO

5

LYS

TYR

LYS

THR

GLU

VAL

CYS

ARG

THR

PHE

6

SER

ALA

GLY

THR

CYS

PRO

TYR

GLY

LYS

7

ARG

CYS

ARG

PHE

ILE

HIS

ALA

THR

PRO

Entity 2, Zn1 - Zn - 65.409 Da.

1

ZN

Entity 3, 9mer RNA 9 residues - 2739.6 Da.

1

U

A

U

A

U

Samples:

sample_1: Selaginella moellendorffii TTP TZF domain single polypeptide chain/9mer RNA complex, [U-98% 13C; U-98% 15N], 0.4 mM; D2O, [U-99% 2H], 5%; sodium phosphate 20 mM; potassium chloride 100 mM; ZnSO4 25 uM; beta-mercaptoethanol 2 mM; glycerol 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N 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 HN(CA)CB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HA(CA)NH	sample_1	isotropic	sample_conditions_1
3D HA(CACO)NH	sample_1	isotropic	sample_conditions_1
4D HC(CCO)NH	sample_1	isotropic	sample_conditions_1
4D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2 - collection

NMRPipe - processing

NMRViewJ v8.0 - data analysis

PINE - chemical shift assignment

AutoAssign - chemical shift assignment

TALOS+ - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts