BMRB Entry 27811

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Elongation factor P from E.coli
Published: 2019-06-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27811

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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 Elongation factor P from E.coli

Deposition date:

2019-02-28

Original release date:

2019-06-26

Authors:

Jagtap, Pravin Kumar Ankush; Macosek, Jakub; Hennig, Janosch

Citation:

Citation: Volkwein, Wolfram; Krafczyk, Ralph; Jagtap, Pravin Kumar Ankush; Parr, Marina; Mankina, Elena; Macosek, Jakub; Guo, Zhenghuan; Furst, Maximilian Josef; Pfab, Miriam; Frishman, Dmitrij; Hennig, Janosch; Jung, Kirsten; Lassak, Jurgen. "Switching the Post-translational Modification of Translation Elongation Factor EF-P." Front. Microbiol. 10, 1148-1148 (2019).
PubMed: 31178848

Assembly members:

Assembly members:
EFP, polymer, 188 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EFP: MATYYSNDFRAGLKIMLDGE PYAVEASEFVKPGKGQAFAR VKLRRLLTGTRVEKTFKSTD SAEGADVVDMNLTYLYNDGE FWHFMNNETFEQLSADAKAI GDNAKWLLDQAECIVTLWNG QPISVTPPNFVELEIVDTDP GLKGDTAGTGGKPATLSTGA VVKVPLFVQIGEVIKVDTRS GEYVSRVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	168
1H chemical shifts	168

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EFP	1

Entities:

Entity 1, EFP 188 residues - Formula weight is not available

1

MET

ALA

THR

TYR

SER

ASN

ASP

PHE

ARG

2

ALA

GLY

LEU

LYS

ILE

MET

LEU

ASP

GLY

GLU

3

PRO

TYR

ALA

VAL

GLU

ALA

SER

GLU

PHE

VAL

4

LYS

PRO

GLY

LYS

GLY

GLN

ALA

PHE

ALA

ARG

5

VAL

LYS

LEU

ARG

LEU

THR

GLY

THR

6

ARG

VAL

GLU

LYS

THR

PHE

LYS

SER

THR

ASP

7

SER

ALA

GLU

GLY

ALA

ASP

VAL

ASP

MET

8

ASN

LEU

THR

TYR

LEU

TYR

ASN

ASP

GLY

GLU

9

PHE

TRP

HIS

PHE

MET

ASN

GLU

THR

PHE

10

GLU

GLN

LEU

SER

ALA

ASP

ALA

LYS

ALA

ILE

11

GLY

ASP

ASN

ALA

LYS

TRP

LEU

ASP

GLN

12

ALA

GLU

CYS

ILE

VAL

THR

LEU

TRP

ASN

GLY

13

GLN

PRO

ILE

SER

VAL

THR

PRO

ASN

PHE

14

VAL

GLU

LEU

GLU

ILE

VAL

ASP

THR

ASP

PRO

15

GLY

LEU

LYS

GLY

ASP

THR

ALA

GLY

THR

GLY

16

GLY

LYS

PRO

ALA

THR

LEU

SER

THR

GLY

ALA

17

VAL

LYS

VAL

PRO

LEU

PHE

VAL

GLN

ILE

18

GLY

GLU

VAL

ILE

LYS

VAL

ASP

THR

ARG

SER

19

GLY

GLU

TYR

VAL

SER

ARG

VAL

LYS

Samples:

sample_1: EFP, [U-100% 13C; U-100% 15N], 0.8 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

Cara, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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