BMRB Entry 17825

Name: Solution Structure of the J Domain of HSJ1a
Published: 2012-01-09

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PDB ID: 2lgw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17825
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the J Domain of HSJ1a

Deposition date:

2011-08-02

Original release date:

2012-01-09

Authors:

Zhou, Chenjie; Gao, Xuechao; Cao, Chunyang; Hu, Hongyu

Citation:

Citation: Gao, Xue-Chao; Zhou, Chen-Jie; Zhou, Zi-Ren; Wu, Meng; Cao, Chun-Yang; Hu, Hong-Yu. "The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation." J. Biol. Chem. 287, 6044-6052 (2012).
PubMed: 22219199

Assembly members:

Assembly members:
entity, polymer, 99 residues, 8556.679 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 Vector: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MASYYEILDVPRSASADDIK KAYRRKALQWHPDKNPDNKE FAEKKFKEVAEAYEVLSDKH KREIYDRYGREPLTGTGTGP SRAEAGSGGPGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	185
15N chemical shifts	66
1H chemical shifts	367

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HSJ1a	1

Entities:

Entity 1, HSJ1a 99 residues - 8556.679 Da.

1

MET

ALA

SER

TYR

GLU

ILE

LEU

ASP

VAL

2

PRO

ARG

SER

ALA

SER

ALA

ASP

ILE

LYS

3

LYS

ALA

TYR

ARG

LYS

ALA

LEU

GLN

TRP

4

HIS

PRO

ASP

LYS

ASN

PRO

ASP

ASN

LYS

GLU

5

PHE

ALA

GLU

LYS

PHE

LYS

GLU

VAL

ALA

6

GLU

ALA

TYR

GLU

VAL

LEU

SER

ASP

LYS

HIS

7

LYS

ARG

GLU

ILE

TYR

ASP

ARG

TYR

GLY

ARG

8

GLU

PRO

LEU

THR

GLY

THR

GLY

THR

GLY

PRO

9

SER

ARG

ALA

GLU

ALA

GLY

SER

GLY

PRO

10

GLY

LEU

GLU

HIS

Samples:

sample_1: HSJ1a, [U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: HSJ1a, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - peak picking

ARIA, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2LGW
DBJ	BAE87866 BAE88406 BAF82315 BAF85450 BAG35597
EMBL	CAA44968 CAA44969
GB	AAA09034 AAA09035 AAH11609 AAH47056 AAP35751
REF	NP_001034639 NP_001162567 NP_001253510 NP_001267342 NP_001271020
SP	P25686
AlphaFold	P25686