BMRB Entry 25629

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for G56C_T163C mutant of Adenylate Kinase at reduced condition
Published: 2017-05-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25629

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Nicholas Rego and David Koes
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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 G56C_T163C mutant of Adenylate Kinase at reduced condition PubMed: 28559350

Deposition date: 2015-05-18 Original release date: 2017-05-19

Authors: Kovermann, Michael; Wolf-Watz, Magnus

Citation: Kovermann, Michael; Grundstrom, Christin; Sauer-Eriksson, A Elisabeth; Sauer, Uwe; Wolf-Watz, Magnus. "Structural basis for ligand binding to an enzyme by a conformational selection pathway" Proc. Natl. Acad. Sci. U.S.A. 114, 6298-6303 (2017).

Assembly members:
Adenylate_Kinase_G56C_T163C, polymer, 214 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pEAK-91 vector

Entity Sequences (FASTA):
Adenylate_Kinase_G56C_T163C: MRIILLGAPGAGKGTQAQFI MEKYGIPQISTGDMLRAAVK SGSELGKQAKDIMDACKLVT DELVIALVKERIAQEDCRNG FLLDGFPRTIPQADAMKEAG INVDYVLEFDVPDELIVDRI VGRRVHAPSGRVYHVKFNPP KVEGKDDVTGEELTTRKDDQ EECVRKRLVEYHQMTAPLIG YYSKEAEAGNTKYAKVDGTK PVAEVRADLEKILG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	410
15N chemical shifts	203
1H chemical shifts	203

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Adenylate Kinase G56C_T163C	1

Entities:

Entity 1, Adenylate Kinase G56C_T163C 214 residues - Formula weight is not available

1

MET

ARG

ILE

LEU

GLY

ALA

PRO

GLY

2

ALA

GLY

LYS

GLY

THR

GLN

ALA

GLN

PHE

ILE

3

MET

GLU

LYS

TYR

GLY

ILE

PRO

GLN

ILE

SER

4

THR

GLY

ASP

MET

LEU

ARG

ALA

VAL

LYS

5

SER

GLY

SER

GLU

LEU

GLY

LYS

GLN

ALA

LYS

6

ASP

ILE

MET

ASP

ALA

CYS

LYS

LEU

VAL

THR

7

ASP

GLU

LEU

VAL

ILE

ALA

LEU

VAL

LYS

GLU

8

ARG

ILE

ALA

GLN

GLU

ASP

CYS

ARG

ASN

GLY

9

PHE

LEU

ASP

GLY

PHE

PRO

ARG

THR

ILE

10

PRO

GLN

ALA

ASP

ALA

MET

LYS

GLU

ALA

GLY

11

ILE

ASN

VAL

ASP

TYR

VAL

LEU

GLU

PHE

ASP

12

VAL

PRO

ASP

GLU

LEU

ILE

VAL

ASP

ARG

ILE

13

VAL

GLY

ARG

VAL

HIS

ALA

PRO

SER

GLY

14

ARG

VAL

TYR

HIS

VAL

LYS

PHE

ASN

PRO

15

LYS

VAL

GLU

GLY

LYS

ASP

VAL

THR

GLY

16

GLU

LEU

THR

ARG

LYS

ASP

GLN

17

GLU

CYS

VAL

ARG

LYS

ARG

LEU

VAL

GLU

18

TYR

HIS

GLN

MET

THR

ALA

PRO

LEU

ILE

GLY

19

TYR

SER

LYS

GLU

ALA

GLU

ALA

GLY

ASN

20

THR

LYS

TYR

ALA

LYS

VAL

ASP

GLY

THR

LYS

21

PRO

VAL

ALA

GLU

VAL

ARG

ALA

ASP

LEU

GLU

22

LYS

ILE

LEU

GLY

Samples:

sample_1: Adenylate Kinase G56C_T163C, [U-100% 13C; U-100% 15N], 0.4 mM; sodium chloride 50 mM; MES 30 mM; TCEP 2 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: pH: 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - collection, data analysis, processing

NMR spectrometers:

Bruker Avance 850 MHz

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