BMRB Entry 27307

Name: NMR resonance assignments of RNase P protein from Thermotoga maritima
Published: 2018-03-08

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27307

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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 RNase P protein from Thermotoga maritima

Deposition date:

2017-11-08

Original release date:

2018-03-08

Authors:

Zeng, Danyun; Reiter, Nicholas

Citation:

Citation: Zeng, Danyun; Brown, Ben; Voehler, Markus; Cai, Sheng; Reiter, Nicholas. "NMR resonance assignments of RNase P protein from Thermotoga maritima" Biomol. NMR Assign. 12, 183-187 (2018).
PubMed: 29450823

Assembly members:

Assembly members:
RNase_P_protein_from_Thermotoga_maritima, 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):
RNase_P_protein_from_Thermotoga_maritima: GSTESFTRRERLRLRRDFLL IFKEGKSLQNEYFVVLFRKN GLDYSRLGIVVKRKFGKATR RNKLKRWVREIFRRNKGVIP KGFDIVVIPRKKLSEEFERV DFWTVREKLLNLLKRIEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	547
15N chemical shifts	115
1H chemical shifts	871

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RNase P protein monomer	1

Entities:

Entity 1, RNase P protein monomer 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], 400 uM; sodium phosphate 20 mM; sodium chloride 80 mM; DSS 50 uM; D2O, [U-99% 2H], 5 % v/v

sample_2: RNase P protein from Thermotoga maritima, [U-100% 13C; U-100% 15N], 400 uM; sodium phosphate 20 mM; sodium chloride 80 mM; DSS 50 uM; D2O 100 % v/v

sample_conditions_1: ionic strength: 20 mM; 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
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCO	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
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1

Software:

CARA v1.9.1.4, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz
Bruker Avance 900 MHz
Varian INOVA 600 MHz

UNP	Q9X1H4
AlphaFold	Q9X1H4