BMRB Entry 51021

Name: NMR resonance assignments of the monomer of RNase P protein from Thermotoga maritima
Published: 2021-11-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51021

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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:

NMR resonance assignments of the monomer of RNase P protein from Thermotoga maritima

Deposition date:

2021-07-19

Original release date:

2021-11-03

Authors:

Zeng, Danyun; Reiter, Nicholas

Citation:

Citation: Zeng, Danyun; Abzhanova, Ainur; Brown, Benjamin; Reiter, Nicholas. "Dissecting Monomer-Dimer Equilibrium of an RNase P Protein Provides Insight Into the Synergistic Flexibility of 5' Leader Pre-tRNA Recognition" Front. Mol. Biosci 8, 730274-730274 (2021).
PubMed: 34540901

Assembly members:

Assembly members:
entity_1, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX4Ta

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSTESFTRRERLRLRRDFLL IFKEGKSLQNEYFVVLFRKN GLDYSRLGIVVKRKFGKATR RNKLKRWVREIFRRNKGVIP KGFDIVVIPRKKLSEEFERV DFWTVREKLLNLLKRIEG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	287
15N chemical shifts	105
1H chemical shifts	105

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNase P protein from Thermotoga maritima	1

Entities:

Entity 1, RNase P protein from Thermotoga maritima 118 residues - Formula weight is not available

1

GLY

SER

THR

GLU

SER

PHE

THR

ARG

GLU

2

ARG

LEU

ARG

LEU

ARG

ASP

PHE

LEU

3

ILE

PHE

LYS

GLU

GLY

LYS

SER

LEU

GLN

ASN

4

GLU

TYR

PHE

VAL

LEU

PHE

ARG

LYS

ASN

5

GLY

LEU

ASP

TYR

SER

ARG

LEU

GLY

ILE

VAL

6

VAL

LYS

ARG

LYS

PHE

GLY

LYS

ALA

THR

ARG

7

ARG

ASN

LYS

LEU

LYS

ARG

TRP

VAL

ARG

GLU

8

ILE

PHE

ARG

ASN

LYS

GLY

VAL

ILE

PRO

9

LYS

GLY

PHE

ASP

ILE

VAL

ILE

PRO

ARG

10

LYS

LEU

SER

GLU

PHE

GLU

ARG

VAL

11

ASP

PHE

TRP

THR

VAL

ARG

GLU

LYS

LEU

12

ASN

LEU

LYS

ARG

ILE

GLU

GLY

Samples:

sample_1: RNase P protein from Thermotoga maritima, [U-100% 13C; U-100% 15N], 153 uM; sodium phosphate 20 mM; sodium chloride 80 mM; DSS 50 uM; D2O, [U-100% 2H], 10%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 318 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5.7 - collection, processing

NMRPipe - processing

CARA - chemical shift assignment

NMRViewJ - data analysis

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 900 MHz
Varian VNMRS 600 MHz

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