Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53391

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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:

MTTsa

Deposition date:

2025-10-15

Original release date:

2026-08-03

Authors:

Tao, Tiange; Jennings, Patricia

Citation:

Citation: Tao, Tiange; Capraro, Dominique; Jennings, Patricia. "1H, 13C, 15N backbone assignment of the minimally tied trefoil knot, MTTSA, a 23s rRNA SPOUT methyltransferase " Biomol. NMR Assign. 20, 16-16 (2026).
PubMed: 41963736

Assembly members:

Assembly members:
entity_1, polymer, 171 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: purified from the natural source

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSLKITILAVGKLKEKYWKQ AIAEYEKRLGPYTKIDIIEV PDEKAPENMSDKEIEQVKEK EGQRILAKIKPQSTVITLEI QGKMLSSEGLAQELNQRMTQ GQSDFVFVIGGSNGLHKDVL QRSNYALSFSKMTFPHQMMR VVLIEQVYRAFKIMRGEAYH KEGGSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	961
15N chemical shifts	318
1H chemical shifts	629

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MTT_SA, Chain A	1
2	MTT_SA, Chain B	1

Entities:

Entity 1, MTT_SA, Chain A 171 residues - Formula weight is not available

1

MET

SER

LEU

LYS

ILE

THR

ILE

LEU

ALA

VAL

2

GLY

LYS

LEU

LYS

GLU

LYS

TYR

TRP

LYS

GLN

3

ALA

ILE

ALA

GLU

TYR

GLU

LYS

ARG

LEU

GLY

4

PRO

TYR

THR

LYS

ILE

ASP

ILE

GLU

VAL

5

PRO

ASP

GLU

LYS

ALA

PRO

GLU

ASN

MET

SER

6

ASP

LYS

GLU

ILE

GLU

GLN

VAL

LYS

GLU

LYS

7

GLU

GLY

GLN

ARG

ILE

LEU

ALA

LYS

ILE

LYS

8

PRO

GLN

SER

THR

VAL

ILE

THR

LEU

GLU

ILE

9

GLN

GLY

LYS

MET

LEU

SER

GLU

GLY

LEU

10

ALA

GLN

GLU

LEU

ASN

GLN

ARG

MET

THR

GLN

11

GLY

GLN

SER

ASP

PHE

VAL

PHE

VAL

ILE

GLY

12

GLY

SER

ASN

GLY

LEU

HIS

LYS

ASP

VAL

LEU

13

GLN

ARG

SER

ASN

TYR

ALA

LEU

SER

PHE

SER

14

LYS

MET

THR

PHE

PRO

HIS

GLN

MET

ARG

15

VAL

LEU

ILE

GLU

GLN

VAL

TYR

ARG

ALA

16

PHE

LYS

ILE

MET

ARG

GLY

GLU

ALA

TYR

HIS

17

LYS

GLU

GLY

SER

HIS

18

HIS

Samples:

sample_1: MTT_SA, [U-13C; U-15N; U-2H], 500 uM; NaOAc-d3, [U-2H], 75 mM; glycerol 1%

sample_2: MTT_SA, [U-13C; U-15N], 1000 uM; NaOAc-d3, [U-2H], 75 mM; glycerol 1%

sample_conditions_1: ionic strength: 0.075 M; pH: 5.6; pressure: 1 atm; temperature: 305 K

sample_conditions_2: ionic strength: 0.075 M; pH: 5.6; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 HBHA(CO)NH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRFx - processing

SPARKY - chemical shift assignment

TALOS-N - data analysis

NMR spectrometers:

Bruker Avance 800 MHz
Bruker AVANCE NEO 600 MHz

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

BMRB Entry 53391