BMRB Entry 26999

Name: Adenylate kinase in Apo form
Published: 2019-07-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26999

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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 in Apo form

Deposition date:

2017-01-19

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:
Wild_type, polymer, 214 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: pEAK91

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- AdK_Apo

Data type	Count
15N chemical shifts	190
1H chemical shifts	190

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AdK	1

Entities:

Entity 1, AdK 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

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

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

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

Samples:

ApoWT_sample: Wild type, [U-15N], 200 uM; MOPS 30 mM; NaCl 50 mM; TMSP 100 uM

sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v3.2, Bruker Biospin - collection

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

ANSIG, Kraulis - chemical shift assignment, peak picking

NMR spectrometers:

Bruker AvanceIIIHD 850 MHz

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