BMRB Entry 51489

Name: NMR assignment of the mCherry protein
Published: 2023-07-28

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51489

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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 assignment of the mCherry protein

Deposition date:

2022-06-14

Original release date:

2023-07-28

Authors:

Sette, Marco; Johnson, Laura Anne; Friis, Pia; Pardi, Arthur; Jimenez, Ralph; Mulder, Frans

Citation:

Citation: Sette, Marco; Johnson, Laura Anne; Jimenez, Ralph; Mulder, Frans. "Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry" Biomol. NMR Assign. 17, 243-247 (2023).
PubMed: 37684490

Assembly members:

Assembly members:
entity_1, polymer, 242 residues, Formula weight is not available

Natural source:

Natural source: Common Name: coral anemones Taxonomy ID: 86600 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Discosoma Discosoma sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHHHHHHGVSKGEEDNMAI IKEFMRFKVHMEGSVNGHEF EIEGEGEGRPYEGTQTAKLK VTKGGPLPFAWDILSPQFMY GSKAYVKHPADIPDYLKLSF PEGFKWERVMNFEDGGVVTV TQDSSLQDGEFIYKVKLRGT NFPSDGPVMQKKTMGWEASS ERMYPEDGALKGEIKQRLKL KDGGHYDAEVKTTYKAKKPV QLPGAYNVNIKLDITSHNED YTIVEQYERAEGRHSTGGMD ELYK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	608
15N chemical shifts	199
1H chemical shifts	199

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mCherry	1

Entities:

Entity 1, mCherry 242 residues - Formula weight is not available

1

MET

GLY

HIS

GLY

VAL

2

SER

LYS

GLY

GLU

ASP

ASN

MET

ALA

ILE

3

ILE

LYS

GLU

PHE

MET

ARG

PHE

LYS

VAL

HIS

4

MET

GLU

GLY

SER

VAL

ASN

GLY

HIS

GLU

PHE

5

GLU

ILE

GLU

GLY

GLU

GLY

GLU

GLY

ARG

PRO

6

TYR

GLU

GLY

THR

GLN

THR

ALA

LYS

LEU

LYS

7

VAL

THR

LYS

GLY

PRO

LEU

PRO

PHE

ALA

8

TRP

ASP

ILE

LEU

SER

PRO

GLN

PHE

MET

TYR

9

GLY

SER

LYS

ALA

TYR

VAL

LYS

HIS

PRO

ALA

10

ASP

ILE

PRO

ASP

TYR

LEU

LYS

LEU

SER

PHE

11

PRO

GLU

GLY

PHE

LYS

TRP

GLU

ARG

VAL

MET

12

ASN

PHE

GLU

ASP

GLY

VAL

THR

VAL

13

THR

GLN

ASP

SER

LEU

GLN

ASP

GLY

GLU

14

PHE

ILE

TYR

LYS

VAL

LYS

LEU

ARG

GLY

THR

15

ASN

PHE

PRO

SER

ASP

GLY

PRO

VAL

MET

GLN

16

LYS

THR

MET

GLY

TRP

GLU

ALA

SER

17

GLU

ARG

MET

TYR

PRO

GLU

ASP

GLY

ALA

LEU

18

LYS

GLY

GLU

ILE

LYS

GLN

ARG

LEU

LYS

LEU

19

LYS

ASP

GLY

HIS

TYR

ASP

ALA

GLU

VAL

20

LYS

THR

TYR

LYS

ALA

LYS

PRO

VAL

21

GLN

LEU

PRO

GLY

ALA

TYR

ASN

VAL

ASN

ILE

22

LYS

LEU

ASP

ILE

THR

SER

HIS

ASN

GLU

ASP

23

TYR

THR

ILE

VAL

GLU

GLN

TYR

GLU

ARG

ALA

24

GLU

GLY

ARG

HIS

SER

THR

GLY

MET

ASP

25

GLU

LEU

TYR

LYS

Samples:

sample_1: mCherry, [U-95% 13C; U-95% 15N], 0.7 mM; Tris 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCOCANH	sample_1	isotropic	sample_conditions_1
3D IHNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz