BMRB Entry 36078

Name: Solution structure for human HSP70 substrate binding domain L542Y mutant
Published: 2018-05-14

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PDB ID: 5xir
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36078
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure for human HSP70 substrate binding domain L542Y mutant PubMed: 29495458

Deposition date: 2017-04-27 Original release date: 2018-05-14

Authors: Hoshikawa, M.; Tochio, N.; Tate, S.

Citation: Umehara, Kohei; Hoshikawa, Miho; Tochio, Naoya; Tate, Shin-Ichi. "Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication" Molecules 23, E528-E528 (2018).

Assembly members:
Heat shock 70 kDa protein 1A, polymer, 185 residues, 20373.900 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

Entity Sequences (FASTA):
Heat shock 70 kDa protein 1A: HMGDKSENVQDLLLLDVAPL SLGLETAGGVMTALIKRNST IPTKQTQIFTTYSDNQPGVL IQVYEGERAMTKDNNLLGRF ELSGIPPAPRGVPQIEVTFD IDANGILNVTATDKSTGKAN KITITNDKGRLSKEEIERMV QEAEKYKAEDEVQRERVSAK NAYESYAFNMKSAVEDEGLK GKISE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	765
15N chemical shifts	187
1H chemical shifts	1074

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_1 185 residues - 20373.900 Da.

1

HIS

MET

GLY

ASP

LYS

SER

GLU

ASN

VAL

GLN

2

ASP

LEU

ASP

VAL

ALA

PRO

LEU

3

SER

LEU

GLY

LEU

GLU

THR

ALA

GLY

VAL

4

MET

THR

ALA

LEU

ILE

LYS

ARG

ASN

SER

THR

5

ILE

PRO

THR

LYS

GLN

THR

GLN

ILE

PHE

THR

6

THR

TYR

SER

ASP

ASN

GLN

PRO

GLY

VAL

LEU

7

ILE

GLN

VAL

TYR

GLU

GLY

GLU

ARG

ALA

MET

8

THR

LYS

ASP

ASN

LEU

GLY

ARG

PHE

9

GLU

LEU

SER

GLY

ILE

PRO

ALA

PRO

ARG

10

GLY

VAL

PRO

GLN

ILE

GLU

VAL

THR

PHE

ASP

11

ILE

ASP

ALA

ASN

GLY

ILE

LEU

ASN

VAL

THR

12

ALA

THR

ASP

LYS

SER

THR

GLY

LYS

ALA

ASN

13

LYS

ILE

THR

ILE

THR

ASN

ASP

LYS

GLY

ARG

14

LEU

SER

LYS

GLU

ILE

GLU

ARG

MET

VAL

15

GLN

GLU

ALA

GLU

LYS

TYR

LYS

ALA

GLU

ASP

16

GLU

VAL

GLN

ARG

GLU

ARG

VAL

SER

ALA

LYS

17

ASN

ALA

TYR

GLU

SER

TYR

ALA

PHE

ASN

MET

18

LYS

SER

ALA

VAL

GLU

ASP

GLU

GLY

LEU

LYS

19

GLY

LYS

ILE

SER

GLU

Samples:

sample_1: human HSP70 substrate binding domain L542Y mutant mM; DTT 10 mM; potassium chloride 50 mM; potassium phosphate 50 mM

sample_conditions_1: ionic strength: 100 M; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	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
1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

MAGRO, Kobayashi, N. - data analysis

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

NMRView, Johnson, One Moon Scientific - data analysis

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker AvanceII 700 MHz

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