BMRB Entry 27831

Name: Backbone chemical shiftsof human Mtr4 KOW
Published: 2019-06-17

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27831

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone chemical shiftsof human Mtr4 KOW

Deposition date:

2019-03-07

Original release date:

2019-06-17

Authors:

Schlundt, Andreas; Sattler, Michael

Citation:

Citation: Lingaraju, Mahesh; Johnsen, Dennis; Schlundt, Andreas; Langer, Lukas; Basquin, Jerome; Sattler, Michael; Heick Jensen, Torben; Falk, Sebastian; Conti, Elena. "The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs" Nat. Commun. 10, 3393-3393 (2019).
PubMed: 31358741

Assembly members:

Assembly members:
hMTR4-KOW, polymer, 148 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM33

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hMTR4-KOW: GPDSMHKPKYCLPFLQPGRL VKVKNEGDDFGWGVVVNFSK KSNVKPNSGELDPLYVVEVL LRCSKESLKNSATEAAKPAK PDEKGEMQVVPVLVHLLSAI SSVRLYIPKDLRPVDNRQSV LKSIQEVQKRFPDGIPLLDP IDDMGIQD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	277
15N chemical shifts	124
1H chemical shifts	124

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Mtr4 KOW domain	1

Entities:

Entity 1, Mtr4 KOW domain 148 residues - Formula weight is not available

GPDSM is cloning artefact

1

GLY

PRO

ASP

SER

MET

HIS

LYS

PRO

LYS

TYR

2

CYS

LEU

PRO

PHE

LEU

GLN

PRO

GLY

ARG

LEU

3

VAL

LYS

VAL

LYS

ASN

GLU

GLY

ASP

PHE

4

GLY

TRP

GLY

VAL

ASN

PHE

SER

LYS

5

LYS

SER

ASN

VAL

LYS

PRO

ASN

SER

GLY

GLU

6

LEU

ASP

PRO

LEU

TYR

VAL

GLU

VAL

LEU

7

LEU

ARG

CYS

SER

LYS

GLU

SER

LEU

LYS

ASN

8

SER

ALA

THR

GLU

ALA

LYS

PRO

ALA

LYS

9

PRO

ASP

GLU

LYS

GLY

GLU

MET

GLN

VAL

10

PRO

VAL

LEU

VAL

HIS

LEU

SER

ALA

ILE

11

SER

VAL

ARG

LEU

TYR

ILE

PRO

LYS

ASP

12

LEU

ARG

PRO

VAL

ASP

ASN

ARG

GLN

SER

VAL

13

LEU

LYS

SER

ILE

GLN

GLU

VAL

GLN

LYS

ARG

14

PHE

PRO

ASP

GLY

ILE

PRO

LEU

ASP

PRO

15

ILE

ASP

MET

GLY

ILE

GLN

ASP

Samples:

sample_1: hMTR4-KOW, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; Phosphate 10 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 298 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 HN(CO)CA	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 HCACO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker - collection, processing

CCPNMR_Analysis, CCPN - chemical shift assignment, chemical shift calculation, data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 900 MHz
Bruker Avance 950 MHz

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