BMRB Entry 34586

Name: NMR structure of an optimized version of the first TPR domain of the human SPAG1 protein
Published: 2021-03-26

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PDB ID: 7bev
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34586
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of an optimized version of the first TPR domain of the human SPAG1 protein PubMed: 33739091

Deposition date: 2020-12-29 Original release date: 2021-03-26

Authors: Dermouche, S.; Chagot, M.; Quinternet, M.

Citation: Dermouche, S.; Chagot, M.; Manival, X.; Quinternet, M.. "Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties" Biochemistry 60, 2349-2363 (2021).

Assembly members:
entity_1, polymer, 126 residues, 14527.270 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: GPHMDYLATREKEKGNEAFN SGDYEEAVMYYTRSISALPT VVAYNNRAQAYIKLQNWNSA EQDCEKVLELEPGNVKALLR RATAYKHQNKLREAREDLKK VLKVEPDNDLAKKTLSEVER DLKNSE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	551
15N chemical shifts	142
1H chemical shifts	915

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 126 residues - 14527.270 Da.

1

GLY

PRO

HIS

MET

ASP

TYR

LEU

ALA

THR

ARG

2

GLU

LYS

GLU

LYS

GLY

ASN

GLU

ALA

PHE

ASN

3

SER

GLY

ASP

TYR

GLU

ALA

VAL

MET

TYR

4

TYR

THR

ARG

SER

ILE

SER

ALA

LEU

PRO

THR

5

VAL

ALA

TYR

ASN

ARG

ALA

GLN

ALA

6

TYR

ILE

LYS

LEU

GLN

ASN

TRP

ASN

SER

ALA

7

GLU

GLN

ASP

CYS

GLU

LYS

VAL

LEU

GLU

LEU

8

GLU

PRO

GLY

ASN

VAL

LYS

ALA

LEU

ARG

9

ARG

ALA

THR

ALA

TYR

LYS

HIS

GLN

ASN

LYS

10

LEU

ARG

GLU

ALA

ARG

GLU

ASP

LEU

LYS

11

VAL

LEU

LYS

VAL

GLU

PRO

ASP

ASN

ASP

LEU

12

ALA

LYS

THR

LEU

SER

GLU

VAL

GLU

ARG

13

ASP

LEU

LYS

ASN

SER

GLU

Samples:

sample_1: SPAG1-TPR1, [U-13C; U-15N], 1 ± 0.1 mM; NaPi 10 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.4; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

CARA, Keller and Wuthrich - chemical shift assignment

TopSpin, Bruker Biospin - collection, processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker AVANCE III 600 MHz

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