BMRB Entry 26688

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments of Guanylyl Cyclase Activator Protein 1 (GCAP1) mutant V77E in a Ca2+-free/Mg2+-bound Activator State
Published: 2015-12-28

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PDB ID: 2na0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26688
MolProbity Validation Chart

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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 of Guanylyl Cyclase Activator Protein 1 (GCAP1) mutant V77E in a Ca2+-free/Mg2+-bound Activator State

Deposition date:

2015-10-08

Original release date:

2015-12-28

Authors:

Lim, Sunghyuk; Ames, James

Citation:

Citation: Lim, Sunghyuk; Peshenko, Igor; Olshevskaya, Elena; Dizhoor, Alexander; Ames, James. "Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State" J. Biol. Chem. 291, 4429-4441 (2016).
PubMed: 26703466

Assembly members:

Assembly members:
GCAP1_(V77E)_mutant, polymer, 204 residues, Formula weight is not available
entity_MYR, non-polymer, 228.371 Da.
entity_MG, non-polymer, 24.305 Da.

Natural source:

Natural source: Common Name: cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GCAP1_(V77E)_mutant: GNIMDGKSVEELSSTECHQW YKKFMTECPSGQLTLYEFRQ FFGLKNLSPWASQYVEQMFE TFDFNKDGYIDFMEYEAALS LVLKGKVEQKLRWYFKLYDV DGNGCIDRDELLTIIRAIRA INPCSDSTMTAEEFTDTVFS KIDVNGDGELSLEEFMEGVQ KDQMLLDTLTRSLDLTRIVR RLQNGEQDEEGASGRETEAA EADG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	283
15N chemical shifts	113
1H chemical shifts	188

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GCAP1 (V77E) mutant	1
2	myristic acid	2
3	Mg2+ ion	3

Entities:

Entity 1, GCAP1 (V77E) mutant 204 residues - Formula weight is not available

A myristoyl group is attached to the N-terminal of the first residue glycine.

1

GLY

ASN

ILE

MET

ASP

GLY

LYS

SER

VAL

GLU

2

GLU

LEU

SER

THR

GLU

CYS

HIS

GLN

TRP

3

TYR

LYS

PHE

MET

THR

GLU

CYS

PRO

SER

4

GLY

GLN

LEU

THR

LEU

TYR

GLU

PHE

ARG

GLN

5

PHE

GLY

LEU

LYS

ASN

LEU

SER

PRO

TRP

6

ALA

SER

GLN

TYR

VAL

GLU

GLN

MET

PHE

GLU

7

THR

PHE

ASP

PHE

ASN

LYS

ASP

GLY

TYR

ILE

8

ASP

PHE

MET

GLU

TYR

GLU

ALA

LEU

SER

9

LEU

VAL

LEU

LYS

GLY

LYS

VAL

GLU

GLN

LYS

10

LEU

ARG

TRP

TYR

PHE

LYS

LEU

TYR

ASP

VAL

11

ASP

GLY

ASN

GLY

CYS

ILE

ASP

ARG

ASP

GLU

12

LEU

THR

ILE

ARG

ALA

ILE

ARG

ALA

13

ILE

ASN

PRO

CYS

SER

ASP

SER

THR

MET

THR

14

ALA

GLU

PHE

THR

ASP

THR

VAL

PHE

SER

15

LYS

ILE

ASP

VAL

ASN

GLY

ASP

GLY

GLU

LEU

16

SER

LEU

GLU

PHE

MET

GLU

GLY

VAL

GLN

17

LYS

ASP

GLN

MET

LEU

ASP

THR

LEU

THR

18

ARG

SER

LEU

ASP

LEU

THR

ARG

ILE

VAL

ARG

19

ARG

LEU

GLN

ASN

GLY

GLU

GLN

ASP

GLU

20

GLY

ALA

SER

GLY

ARG

GLU

THR

GLU

ALA

21

GLU

ALA

ASP

GLY

Entity 2, myristic acid - C14 H28 O2 - 228.371 Da.

1

MYR

Entity 3, Mg2+ ion - Mg - 24.305 Da.

1

MG

Samples:

sample_1: TRIS, [U-100% 2H], 5 mM; DTT, [U-100% 2H], 5 mM; GCAP1 (V77E) mutant, [U-100% 15N], 0.5 mM; MgCl2 5 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_2: TRIS, [U-100% 2H], 5 mM; DTT, [U-100% 2H], 5 mM; GCAP1 (V77E) mutant, [U-100% 13C; U-100% 15N], 0.5 mM; MgCl2 5 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_3: TRIS, [U-100% 2H], 5 mM; DTT, [U-100% 2H], 5 mM; GCAP1 (V77E) mutant, [U-13C; U-15N; U-2H], 0.5 mM; MgCl2 5 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 320 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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