BMRB Entry 26932

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for MTTTm
Published: 2017-03-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26932

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for MTTTm

Deposition date:

2016-11-03

Original release date:

2017-03-27

Authors:

Burban, David; Jennings, Patricia

Citation:

Citation: Burban, David; Jennings, Patricia. "Backbone assignments for the SPOUT methyltransferase MTT Tm , a knotted protein from Thermotoga maritima" Biomol. NMR Assign. 11, 151-154 (2017).
PubMed: 28284017

Assembly members:

Assembly members:
MTTTm, polymer, 162 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: pet28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MTTTm: SLRVRIAVIGKLDGFIKEGI KHYEKFLRRFCKPEVLEIKR VHRGSIEEIVRKETEDLTNR ILPGSFVMVMDKRGEEVSSE EFADFLKDLEMKGKDITILI GGPYGLNEEIFAKAHRVFSL SKMTFTHGMTVLIVLEQIFR AFKIIHGENYHYEGGSHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	438
15N chemical shifts	145
1H chemical shifts	145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MTTTm monomer	1

Entities:

Entity 1, MTTTm monomer 162 residues - Formula weight is not available

1

SER

LEU

ARG

VAL

ARG

ILE

ALA

VAL

ILE

GLY

2

LYS

LEU

ASP

GLY

PHE

ILE

LYS

GLU

GLY

ILE

3

LYS

HIS

TYR

GLU

LYS

PHE

LEU

ARG

PHE

4

CYS

LYS

PRO

GLU

VAL

LEU

GLU

ILE

LYS

ARG

5

VAL

HIS

ARG

GLY

SER

ILE

GLU

ILE

VAL

6

ARG

LYS

GLU

THR

GLU

ASP

LEU

THR

ASN

ARG

7

ILE

LEU

PRO

GLY

SER

PHE

VAL

MET

VAL

MET

8

ASP

LYS

ARG

GLY

GLU

VAL

SER

GLU

9

GLU

PHE

ALA

ASP

PHE

LEU

LYS

ASP

LEU

GLU

10

MET

LYS

GLY

LYS

ASP

ILE

THR

ILE

LEU

ILE

11

GLY

PRO

TYR

GLY

LEU

ASN

GLU

ILE

12

PHE

ALA

LYS

ALA

HIS

ARG

VAL

PHE

SER

LEU

13

SER

LYS

MET

THR

PHE

THR

HIS

GLY

MET

THR

14

VAL

LEU

ILE

VAL

LEU

GLU

GLN

ILE

PHE

ARG

15

ALA

PHE

LYS

ILE

HIS

GLY

GLU

ASN

TYR

16

HIS

TYR

GLU

GLY

SER

HIS

17

HIS

Samples:

sample_1: MTTTm, [U-100% 13C; U-100% 15N], 350 uM; sodium acetate buffer 75 mM

sample_conditions_1: ionic strength: 75 mM; pH: 5.6; pressure: 1 atm; temperature: 323 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian Avance 800 MHz

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