BMRB Entry 27954

Name: Adenylate kinase mutant R119K bound to ATP
Published: 2019-07-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27954

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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:

Adenylate kinase mutant R119K bound to ATP

Deposition date:

2019-06-24

Original release date:

2019-07-30

Authors:

Rogne, Per; Wolf-Watz, Magnus

Citation:

Citation: Rogne, Per; Andersson, David; Grundstrom, Christin; Sauer-Eriksson, Elisabeth; Linusson, Anna; Wolf-Watz, Magnus. "Nucleation of an Activating Conformational Change by a Cation-pi Interaction" Biochemistry 58, 3408-3412 (2019).
PubMed: 31339702

Assembly members:

Assembly members:
Adenylate_kinase, polymer, 214 residues, 23557 Da.
entity_ATP, non-polymer, 507.181 Da.

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: pEAK91

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Adenylate_kinase: MRIILLGAPGAGKGTQAQFI MEKYGIPQISTGDMLRAAVK SGSELGKQAKDIMDAGKLVT DELVIALVKERIAQEDCRNG FLLDGFPRTIPQADAMKEAG INVDYVLEFDVPDELIVDKI VGRRVHAPSGRVYHVKFNPP KVEGKDDVTGEELTTRKDDQ EETVRKRLVEYHQMTAPLIG YYSKEAEAGNTKYAKVDGTK PVAEVRADLEKILG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	158
1H chemical shifts	158

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Protein	1
2	ATP	2

Entities:

Entity 1, Protein 214 residues - 23557 Da.

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

GLY

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

LYS

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

THR

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

Entity 2, ATP - C10 H16 N5 O13 P3 - 507.181 Da.

1

ATP

Samples:

sample_1: Adenylate kinase, [U-100% 15N], 200 uM; ADENOSINE-5'-TRIPHOSPHATE 10 mM; MOPS 30 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 7 % v/v

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANSIG, Kraulis - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 850 MHz

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