BMRB Entry 31097

Name: Solution NMR structure of a RiPP proteusin precursor protein
Published: 2024-02-08

Click here to enlarge.

PDB ID: 8tb1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31097
MolProbity Validation Chart

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:

Solution NMR structure of a RiPP proteusin precursor protein

Deposition date:

2023-06-28

Original release date:

2024-02-08

Authors:

McShan, A.; Vinayak, A.; Nguyen, N.

Citation:

Citation: McShan, A.; Vinayak, A.; Nguyen, N.. "Solution NMR structure of a RiPP proteusin precursor protein" .

Assembly members:

Assembly members:
entity_1, polymer, 91 residues, 9677.898 Da.

Natural source:

Natural source: Common Name: Methylovulum psychrotolerans Taxonomy ID: 1704499 Superkingdom: Bacteria Kingdom: not available Genus/species: Methylovulum psychrotolerans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMMNEEQTQQYSQIVAKC WADAEFKAKLIADPKATLAA ESIAVPDGIELRVLENTATV VNLVLPPPPAEGELSDEDLG AVTGGLTVLPW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	173
15N chemical shifts	60
1H chemical shifts	60

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 91 residues - 9677.898 Da.

1

GLY

SER

HIS

MET

ASN

GLU

GLN

THR

2

GLN

TYR

SER

GLN

ILE

VAL

ALA

LYS

CYS

3

TRP

ALA

ASP

ALA

GLU

PHE

LYS

ALA

LYS

LEU

4

ILE

ALA

ASP

PRO

LYS

ALA

THR

LEU

ALA

5

GLU

SER

ILE

ALA

VAL

PRO

ASP

GLY

ILE

GLU

6

LEU

ARG

VAL

LEU

GLU

ASN

THR

ALA

THR

VAL

7

VAL

ASN

LEU

VAL

LEU

PRO

ALA

8

GLU

GLY

GLU

LEU

SER

ASP

GLU

ASP

LEU

GLY

9

ALA

VAL

THR

GLY

LEU

THR

VAL

LEU

PRO

10

TRP

Samples:

sample_1: MprE7-TH1, [U-100% 13C; U-100% 15N], 0.4 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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

Software:

Sparky, Goddard - chemical shift assignment

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Bruker AVIIIHD-800 800 MHz

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