BMRB Entry 34329

Name: NMR structure of the third TPR domain of the human SPAG1 protein
Published: 2019-05-31

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PDB ID: 6i57
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34329
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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 the third TPR domain of the human SPAG1 protein

Deposition date:

2018-11-13

Original release date:

2019-05-31

Authors:

Chagot, M.; Quinternet, M.

Citation:

Citation: Chagot, M.; Dos Santos Morais, R.; Dermouche, S.; Lefebvre, D.; Manival, X.; Chipot, C.; Dehez, F.; Quinternet, M.. "Binding properties of the quaternary assembly protein SPAG1." Biochem. J. 476, 1679-1694 (2019).
PubMed: 31118266

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14381.639 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPHMTFKALKEEGNQCVNDK NYKDALSKYSECLKINNKEC AIYTNRALCYLKLCQFEEAK QDCDQALQLADGNVKAFYRR ALAHKGLKNYQKSLIDLNKV ILLDPSIIEAKMELEEVTRL LNLKD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	555
15N chemical shifts	143
1H chemical shifts	940

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 125 residues - 14381.639 Da.

1

GLY

PRO

HIS

MET

THR

PHE

LYS

ALA

LEU

LYS

2

GLU

GLY

ASN

GLN

CYS

VAL

ASN

ASP

LYS

3

ASN

TYR

LYS

ASP

ALA

LEU

SER

LYS

TYR

SER

4

GLU

CYS

LEU

LYS

ILE

ASN

LYS

GLU

CYS

5

ALA

ILE

TYR

THR

ASN

ARG

ALA

LEU

CYS

TYR

6

LEU

LYS

LEU

CYS

GLN

PHE

GLU

ALA

LYS

7

GLN

ASP

CYS

ASP

GLN

ALA

LEU

GLN

LEU

ALA

8

ASP

GLY

ASN

VAL

LYS

ALA

PHE

TYR

ARG

9

ALA

LEU

ALA

HIS

LYS

GLY

LEU

LYS

ASN

TYR

10

GLN

LYS

SER

LEU

ILE

ASP

LEU

ASN

LYS

VAL

11

ILE

LEU

ASP

PRO

SER

ILE

GLU

ALA

12

LYS

MET

GLU

LEU

GLU

VAL

THR

ARG

LEU

13

LEU

ASN

LEU

LYS

ASP

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 34329

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: