BMRB Entry 52588

Name: NMR resonance assignments of FtsY at 298 K
Published: 2024-08-26

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52588

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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:

NMR resonance assignments of FtsY at 298 K

Deposition date:

2024-08-20

Original release date:

2024-08-26

Authors:

Mohanty, Biswaranjan

Citation:

Citation: Zhong, Yichen; Wilkinson-White, Lorna; Zhang, Esther; Mohanty, Biswaranjan; Zhang, Belinda; McRae, Madeline; Luo, Rachel; Allport, Thomas; Duff, Anthony; Zhao, Jennifer; El-Kamand, Serene; Du Plessis, Mar-Dean; Cubeddu, Liza; Gamsjaeger, Roland; Ataide, Sandro; Kwan, Ann. "Peptide nucleic acids can form hairpins and bind RNA-binding proteins" PLoS One 19, e0310565-e0310565 (2024).
PubMed: 39283902

Assembly members:

Assembly members:
entity_1, polymer, 303 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GFARLKRSLLKTKENLGSGF ISLFRGKKIDDDLFEELEEQ LLIADVGVETTRKIITNLTE GASRKQLRDAEALYGLLKEE MGEILAKVDEPLNVEGKAPF VILMVGVNGVGKTTTIGKLA RQFEQQGKSVMLAAGDTFRA AAVEQLQVWGQRNNIPVIAQ HTGADSASVIFDAIQAAKAR NIDVLIADTAGRLQNKSHLM EELKKIVRVMKKLDVEAPHE VMLTIDASTGQNAVSQAKLF HEAVGLTGITLTKLDGTAKG GVIFSVADQFGIPIRYIGVG ERIEDLRPFKADDFIEALFA RED

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	338
15N chemical shifts	161
1H chemical shifts	161

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FtsY	1

Entities:

Entity 1, FtsY 303 residues - Formula weight is not available

1

GLY

PHE

ALA

ARG

LEU

LYS

ARG

SER

LEU

2

LYS

THR

LYS

GLU

ASN

LEU

GLY

SER

GLY

PHE

3

ILE

SER

LEU

PHE

ARG

GLY

LYS

ILE

ASP

4

ASP

LEU

PHE

GLU

LEU

GLU

GLN

5

LEU

ILE

ALA

ASP

VAL

GLY

VAL

GLU

THR

6

THR

ARG

LYS

ILE

THR

ASN

LEU

THR

GLU

7

GLY

ALA

SER

ARG

LYS

GLN

LEU

ARG

ASP

ALA

8

GLU

ALA

LEU

TYR

GLY

LEU

LYS

GLU

9

MET

GLY

GLU

ILE

LEU

ALA

LYS

VAL

ASP

GLU

10

PRO

LEU

ASN

VAL

GLU

GLY

LYS

ALA

PRO

PHE

11

VAL

ILE

LEU

MET

VAL

GLY

VAL

ASN

GLY

VAL

12

GLY

LYS

THR

ILE

GLY

LYS

LEU

ALA

13

ARG

GLN

PHE

GLU

GLN

GLY

LYS

SER

VAL

14

MET

LEU

ALA

GLY

ASP

THR

PHE

ARG

ALA

15

ALA

VAL

GLU

GLN

LEU

GLN

VAL

TRP

GLY

16

GLN

ARG

ASN

ILE

PRO

VAL

ILE

ALA

GLN

17

HIS

THR

GLY

ALA

ASP

SER

ALA

SER

VAL

ILE

18

PHE

ASP

ALA

ILE

GLN

ALA

LYS

ALA

ARG

19

ASN

ILE

ASP

VAL

LEU

ILE

ALA

ASP

THR

ALA

20

GLY

ARG

LEU

GLN

ASN

LYS

SER

HIS

LEU

MET

21

GLU

LEU

LYS

ILE

VAL

ARG

VAL

MET

22

LYS

LEU

ASP

VAL

GLU

ALA

PRO

HIS

GLU

23

VAL

MET

LEU

THR

ILE

ASP

ALA

SER

THR

GLY

24

GLN

ASN

ALA

VAL

SER

GLN

ALA

LYS

LEU

PHE

25

HIS

GLU

ALA

VAL

GLY

LEU

THR

GLY

ILE

THR

26

LEU

THR

LYS

LEU

ASP

GLY

THR

ALA

LYS

GLY

27

GLY

VAL

ILE

PHE

SER

VAL

ALA

ASP

GLN

PHE

28

GLY

ILE

PRO

ILE

ARG

TYR

ILE

GLY

VAL

GLY

29

GLU

ARG

ILE

GLU

ASP

LEU

ARG

PRO

PHE

LYS

30

ALA

ASP

PHE

ILE

GLU

ALA

LEU

PHE

ALA

31

ARG

GLU

ASP

Samples:

sample_1: FtsY, [U-100% 13C; U-100% 15N] with fractional deuteration, 225 uM; sodium phosphate 25 mM; NaCl 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D TROSY HNCA	sample_1	isotropic	sample_conditions_1
2D 15N-1H TROSY-HSQC	sample_1	isotropic	sample_conditions_1
3D TRSOY HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D TROSY HNCACB	sample_1	isotropic	sample_conditions_1
3D TROSY HNCB	sample_1	isotropic	sample_conditions_1
3D TROSY HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - data collection and processing

NMRbox - data processing

CARA - Resonance assignments

NMR spectrometers:

Bruker AVANCE III 800 MHz

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