BMRB Entry 27090

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Elongation factor P
Published: 2017-10-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27090

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 1H, 13C, and 15N Chemical Shift Assignments for Elongation factor P

Deposition date:

2017-05-02

Original release date:

2017-10-03

Authors:

Macosek, Jakub; Hennig, Janosch

Citation:

Citation: Krafczyk, Ralph; Macosek, Jakub; Jagtap, Pravin Kumar Ankush; Gast, Daniel; Wunder, Swetlana; Mitra, Prithiba; Jha, Amit Kumar; Rohr, Jurgen; Hoffmann-Roder, Anja; Jung, Kirsten; Hennig, Janosch; Lassak, Jurgen. "Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P" MBio 8, e01412-e01417 (2017).
PubMed: 28951478

Assembly members:

Assembly members:
EF-P, polymer, 189 residues, 21303.1 Da.

Natural source:

Natural source: Common Name: Pseudomonas putida Taxonomy ID: 303 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas putida

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EF-P: MKTGKELKPGTVLRIDNDPW LVQKAEFTKSGRNSAIMKTK LKNLLTGYKTETVYGADDKL DDVILDRKEATLSFINGDEY TFMDTTDYTMYELNAEDIEA VLPYIEEGMEDVCEAVFFEG RLVSVELPTTISRKVVYTEN AARGDTSGKVMKPAKLANGT EISVADFIQIDEWIDIDTRD NSFKGRSKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	516
15N chemical shifts	178
1H chemical shifts	178

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Elongation factor P	1

Entities:

Entity 1, Elongation factor P 189 residues - 21303.1 Da.

1

MET

LYS

THR

GLY

LYS

GLU

LEU

LYS

PRO

GLY

2

THR

VAL

LEU

ARG

ILE

ASP

ASN

ASP

PRO

TRP

3

LEU

VAL

GLN

LYS

ALA

GLU

PHE

THR

LYS

SER

4

GLY

ARG

ASN

SER

ALA

ILE

MET

LYS

THR

LYS

5

LEU

LYS

ASN

LEU

THR

GLY

TYR

LYS

THR

6

GLU

THR

VAL

TYR

GLY

ALA

ASP

LYS

LEU

7

ASP

VAL

ILE

LEU

ASP

ARG

LYS

GLU

ALA

8

THR

LEU

SER

PHE

ILE

ASN

GLY

ASP

GLU

TYR

9

THR

PHE

MET

ASP

THR

ASP

TYR

THR

MET

10

TYR

GLU

LEU

ASN

ALA

GLU

ASP

ILE

GLU

ALA

11

VAL

LEU

PRO

TYR

ILE

GLU

GLY

MET

GLU

12

ASP

VAL

CYS

GLU

ALA

VAL

PHE

GLU

GLY

13

ARG

LEU

VAL

SER

VAL

GLU

LEU

PRO

THR

14

ILE

SER

ARG

LYS

VAL

TYR

THR

GLU

ASN

15

ALA

ARG

GLY

ASP

THR

SER

GLY

LYS

VAL

16

MET

LYS

PRO

ALA

LYS

LEU

ALA

ASN

GLY

THR

17

GLU

ILE

SER

VAL

ALA

ASP

PHE

ILE

GLN

ILE

18

ASP

GLU

TRP

ILE

ASP

ILE

ASP

THR

ARG

ASP

19

ASN

SER

PHE

LYS

GLY

ARG

SER

LYS

Samples:

sample_1: EF-P, [U-100% 13C; U-100% 15N], 0.45 mM; sodium phosphate 100 mM; sodium chloride 50 mM; DTT 5 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

CcpNMR, CCPN - chemical shift assignment

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 700 MHz
Bruker Avance 800 MHz

UNP	A0A059UQW3
AlphaFold	A0A1L5PKK0