BMRB Entry 30888

Name: NMR Structure of GCAP5
Published: 2021-10-13

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PDB ID: 7m2m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30888
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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:

NMR Structure of GCAP5

Deposition date:

2021-03-17

Original release date:

2021-10-13

Authors:

Ames, J.; Cudia, D.

Citation:

Citation: Cudia, Diana; Roseman, Graham; Assafa, Tufa; Shahu, Manisha Kumari; Scholten, Alexander; Menke-Sell, Sarah-Karina; Yamada, Hiroaki; Koch, Karl-W; Milhauser, Glenn; Ames, James. "NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors" Biochemistry 60, 3058-3070 (2021).
PubMed: 34609135

Assembly members:

Assembly members:
entity_1, polymer, 198 residues, 22489.383 Da.
entity_MG, non-polymer, 24.305 Da.

Natural source:

Natural source: Common Name: Zebrafish, Brachydanio rerio Taxonomy ID: 7955 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Danio rerio

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XGDSSSMSATELSACKCHQW YRKFMTECPSGQLTFYEFKK FFGLKNLSEKSNAYVNTMFK TFDIDDDGCIDFMEYVAALS LVLKGGVQQKLRWYFKLFDM DGSGCIDKDELLLIFKAVQA INGAEPEISAEDLADIVFNK IDVNGDGELSLEEFMEGISA DEKISEMLTQSLDLTRIVSN IYNDSYIEQEAEIIEDQA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	579
15N chemical shifts	160
1H chemical shifts	812

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 198 residues - 22489.383 Da.

1

MYR

GLY

ASP

SER

MET

SER

ALA

THR

2

GLU

LEU

SER

ALA

CYS

LYS

CYS

HIS

GLN

TRP

3

TYR

ARG

LYS

PHE

MET

THR

GLU

CYS

PRO

SER

4

GLY

GLN

LEU

THR

PHE

TYR

GLU

PHE

LYS

5

PHE

GLY

LEU

LYS

ASN

LEU

SER

GLU

LYS

6

SER

ASN

ALA

TYR

VAL

ASN

THR

MET

PHE

LYS

7

THR

PHE

ASP

ILE

ASP

GLY

CYS

ILE

8

ASP

PHE

MET

GLU

TYR

VAL

ALA

LEU

SER

9

LEU

VAL

LEU

LYS

GLY

VAL

GLN

LYS

10

LEU

ARG

TRP

TYR

PHE

LYS

LEU

PHE

ASP

MET

11

ASP

GLY

SER

GLY

CYS

ILE

ASP

LYS

ASP

GLU

12

LEU

ILE

PHE

LYS

ALA

VAL

GLN

ALA

13

ILE

ASN

GLY

ALA

GLU

PRO

GLU

ILE

SER

ALA

14

GLU

ASP

LEU

ALA

ASP

ILE

VAL

PHE

ASN

LYS

15

ILE

ASP

VAL

ASN

GLY

ASP

GLY

GLU

LEU

SER

16

LEU

GLU

PHE

MET

GLU

GLY

ILE

SER

ALA

17

ASP

GLU

LYS

ILE

SER

GLU

MET

LEU

THR

GLN

18

SER

LEU

ASP

LEU

THR

ARG

ILE

VAL

SER

ASN

19

ILE

TYR

ASN

ASP

SER

TYR

ILE

GLU

GLN

GLU

20

ALA

GLU

ILE

GLU

ASP

GLN

ALA

Entity 2, unit_2 - Mg - 24.305 Da.

1

MG

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_2

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

BMRB Entry 30888

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: