BMRB Entry 26025

Name: 1H, 13C, and 15N Chemical Shift Assignments for Q4DY78
Published: 2016-07-12

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PDB ID: 5kgq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26025
MolProbity Validation Chart

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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, 13C, and 15N Chemical Shift Assignments for Q4DY78

Deposition date:

2016-04-03

Original release date:

2016-07-12

Authors:

D'Andrea, Everton; Diehl, Anne; Schmieder, Peter; Oschkinat, Hartmut; Pires, Jose

Citation:

Citation: D'Andrea, Everton; Diehl, Anne; Schmieder, Peter; Oschkinat, Hartmut; Pires, Jose. "Chemical shift assignments and secondary structure prediction for Q4DY78, a conserved kinetoplastid-specific protein from Trypanosoma cruzi" Biomol. NMR Assign. 10, 325-328 (2016).
PubMed: 27356988

Assembly members:

Assembly members:
Q4DY78, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Trypanosoma cruzi Taxonomy ID: 5693 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma cruzi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Q4DY78: GSAMGHMVKISHEDTQRIKT AFLSYAQGQDKVTEAMIDQL ICGAFPGLSWEQLQEKKKGR AAANGYDRSAFFSLVASDEQ YVRFIAQHFPCAPEEEKPPE IDALELKTQKGF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	451
15N chemical shifts	106
1H chemical shifts	718

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Q4DY78 monomer	1

Entities:

Entity 1, Q4DY78 monomer 112 residues - Formula weight is not available

1

GLY

SER

ALA

MET

GLY

HIS

MET

VAL

LYS

ILE

2

SER

HIS

GLU

ASP

THR

GLN

ARG

ILE

LYS

THR

3

ALA

PHE

LEU

SER

TYR

ALA

GLN

GLY

GLN

ASP

4

LYS

VAL

THR

GLU

ALA

MET

ILE

ASP

GLN

LEU

5

ILE

CYS

GLY

ALA

PHE

PRO

GLY

LEU

SER

TRP

6

GLU

GLN

LEU

GLN

GLU

LYS

GLY

ARG

7

ALA

ASN

GLY

TYR

ASP

ARG

SER

ALA

8

PHE

SER

LEU

VAL

ALA

SER

ASP

GLU

GLN

9

TYR

VAL

ARG

PHE

ILE

ALA

GLN

HIS

PHE

PRO

10

CYS

ALA

PRO

GLU

LYS

PRO

GLU

11

ILE

ASP

ALA

LEU

GLU

LEU

LYS

THR

GLN

LYS

12

GLY

PHE

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_2_conditions
2D 1H-13C HSQC	sample_3	isotropic	sample_3_conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_1_conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_1_conditions
3D CBCA(CO)NH	sample_3	isotropic	sample_3_conditions
3D HNCACB	sample_3	isotropic	sample_3_conditions
3D HBHA(CO)NH	sample_2	isotropic	sample_2_conditions
3D 1H-15N TOCSY	sample_2	isotropic	sample_2_conditions
3D HCCH-COSY	sample_3	isotropic	sample_3_conditions
3D HCCH-TOCSY	sample_3	isotropic	sample_3_conditions
3D HNCO	sample_3	isotropic	sample_3_conditions
3D 1H-15N NOESY	sample_2	isotropic	sample_2_conditions
3D 1H-13C NOESY	sample_3	isotropic	sample_3_conditions

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SPARKY: Backbone or all simulated peaks

BMRB Entry 26025

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: