BMRB Entry 51716

Name: Partial Backbone Assignment of The Q163C/Q309C Mutant of aMI-domain in the Co2+-Bound Form
Published: 2023-04-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51716

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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:

Partial Backbone Assignment of The Q163C/Q309C Mutant of aMI-domain in the Co2+-Bound Form

Deposition date:

2022-11-30

Original release date:

2023-04-04

Authors:

Nguyen, Hoa; Wang, Xu

Citation:

Citation: Nguyen, Hoa; Jing, Tianwei; Wang, Xu. "The Q163C/Q309C mutant of alphaMI-domain is an active variant suitable for NMR characterization" PLoS One 18, e0280778-e0280778 (2023).
PubMed: 36696377

Assembly members:

Assembly members:
entity_1, polymer, 194 residues, Formula weight is not available
entity_GLU, non-polymer, 147.129 Da.
entity_CO, non-polymer, 58.933 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: EDSDIAFLIDGSGSIIPHDF RRMKEFVSTVMECLKKSKTL FSLMQYSEEFRIHFTFKEFQ NNPNPRSLVKPITQLLGRTH TATGIRKVVRELFNITNGAR KNAFKILVVITDGEKFGDPL GYEDVIPEADREGVIRYVIG VGDAFRSEKSRQELNTIASK PPRDHVFQVNNFEALKTICN QLREKIFAIEGTQT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	72
15N chemical shifts	38
1H chemical shifts	38

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Q163C	1
2	Glu	2
3	Co	3

Entities:

Entity 1, Q163C 194 residues - Formula weight is not available

Contains the mutations Q163C and Q309C to create the disulfide bond needed to

1

GLU

ASP

SER

ASP

ILE

ALA

PHE

LEU

ILE

ASP

2

GLY

SER

GLY

SER

ILE

PRO

HIS

ASP

PHE

3

ARG

MET

LYS

GLU

PHE

VAL

SER

THR

VAL

4

MET

GLU

CYS

LEU

LYS

SER

LYS

THR

LEU

5

PHE

SER

LEU

MET

GLN

TYR

SER

GLU

PHE

6

ARG

ILE

HIS

PHE

THR

PHE

LYS

GLU

PHE

GLN

7

ASN

PRO

ASN

PRO

ARG

SER

LEU

VAL

LYS

8

PRO

ILE

THR

GLN

LEU

GLY

ARG

THR

HIS

9

THR

ALA

THR

GLY

ILE

ARG

LYS

VAL

ARG

10

GLU

LEU

PHE

ASN

ILE

THR

ASN

GLY

ALA

ARG

11

LYS

ASN

ALA

PHE

LYS

ILE

LEU

VAL

ILE

12

THR

ASP

GLY

GLU

LYS

PHE

GLY

ASP

PRO

LEU

13

GLY

TYR

GLU

ASP

VAL

ILE

PRO

GLU

ALA

ASP

14

ARG

GLU

GLY

VAL

ILE

ARG

TYR

VAL

ILE

GLY

15

VAL

GLY

ASP

ALA

PHE

ARG

SER

GLU

LYS

SER

16

ARG

GLN

GLU

LEU

ASN

THR

ILE

ALA

SER

LYS

17

PRO

ARG

ASP

HIS

VAL

PHE

GLN

VAL

ASN

18

ASN

PHE

GLU

ALA

LEU

LYS

THR

ILE

CYS

ASN

19

GLN

LEU

ARG

GLU

LYS

ILE

PHE

ALA

ILE

GLU

20

GLY

THR

GLN

THR

Entity 2, Glu - C5 H9 N O4 - 147.129 Da.

1

GLU

Entity 3, Co - Co - 58.933 Da.

1

CO

Samples:

sample_1: alphaM-I-domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.25 mM; sodium glutamate 10 mM; Cobalt Chloride 1 mM; HEPES 20 mM; sodium chloride 0.1 M

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRViewJ - data analysis

I-PINE - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 850 MHz