BMRB Entry 51201

Name: 1H-15N HSQC spectrum of cGMP-bound human PKG CBD-B
Published: 2022-03-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51201

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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:

1H-15N HSQC spectrum of cGMP-bound human PKG CBD-B

Deposition date:

2021-11-30

Original release date:

2022-03-04

Authors:

Byun, Jung; VanSchouwen, Bryan; Huang, Jinfeng; Baryar, Ubaidullah; Melacini, Giuseppe

Citation:

Citation: Byun, Jung; VanSchouwen, Bryan; Huang, Jinfeng; Baryar, Ubaidullah; Melacini, Giuseppe. "Divergent allostery reveals critical differences between structurally homologous regulatory domains of Plasmodium falciparum and human protein kinase G" J. Biol. Chem. 298, 101691-101691 (2022).
PubMed: 35143840

Assembly members:

Assembly members:
entity_1, polymer, 153 residues, Formula weight is not available
entity_PCG, non-polymer, 345.205 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: pQTEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSTGLIKHTEYMEFLKSVPT FQSLPEEILSKLADVLEETH YENGEYIIRQGARGDTFFII SKGTVNVTREDSPSEDPVFL RTLGKGDWFGEKALQGEDVR TANVIAAEAVTCLVIDRDSF KHLIGGLDDVSNKAYEDAEA KAKYEAEAAFFAN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	125
1H chemical shifts	125

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Human protein kinase G isoform Ib CBD-B domain	1
2	Cyclic guanosine monophosphate	2

Entities:

Entity 1, Human protein kinase G isoform Ib CBD-B domain 153 residues - Formula weight is not available

Residues 1 and 2 represent part of a non-native N-terminal affinity tag. The remaining residues represent residues 219-369 of the CBD-B domain of human protein kinase G isoform Ib.

1

GLY

SER

THR

GLY

LEU

ILE

LYS

HIS

THR

GLU

2

TYR

MET

GLU

PHE

LEU

LYS

SER

VAL

PRO

THR

3

PHE

GLN

SER

LEU

PRO

GLU

ILE

LEU

SER

4

LYS

LEU

ALA

ASP

VAL

LEU

GLU

THR

HIS

5

TYR

GLU

ASN

GLY

GLU

TYR

ILE

ARG

GLN

6

GLY

ALA

ARG

GLY

ASP

THR

PHE

ILE

7

SER

LYS

GLY

THR

VAL

ASN

VAL

THR

ARG

GLU

8

ASP

SER

PRO

SER

GLU

ASP

PRO

VAL

PHE

LEU

9

ARG

THR

LEU

GLY

LYS

GLY

ASP

TRP

PHE

GLY

10

GLU

LYS

ALA

LEU

GLN

GLY

GLU

ASP

VAL

ARG

11

THR

ALA

ASN

VAL

ILE

ALA

GLU

ALA

VAL

12

THR

CYS

LEU

VAL

ILE

ASP

ARG

ASP

SER

PHE

13

LYS

HIS

LEU

ILE

GLY

LEU

ASP

VAL

14

SER

ASN

LYS

ALA

TYR

GLU

ASP

ALA

GLU

ALA

15

LYS

ALA

LYS

TYR

GLU

ALA

GLU

ALA

PHE

16

PHE

ALA

ASN

Entity 2, Cyclic guanosine monophosphate - C10 H12 N5 O7 P - 345.205 Da.

1

PCG

Samples:

sample_1: Human protein kinase G isoform Ib CBD-B domain, [U-98% 15N], 20 uM; CYCLIC GUANOSINE MONOPHOSPHATE 2 mM; N-acetylglycine, [U-98% 15N], 80 uM; TRIS 50 mM; NaCl 100 mM; DTT 1 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 306 K

Experiments:

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

Software:

TOPSPIN - collection

NMRPipe - processing

SPARKY - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

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