BMRB Entry 25515

Name: Solution Structure of the non-phosphorylated J-domain of Human Cysteine String Protein (CSP)
Published: 2016-07-11

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PDB ID: 2n05
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25515
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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:

Solution Structure of the non-phosphorylated J-domain of Human Cysteine String Protein (CSP)

Deposition date:

2015-03-04

Original release date:

2016-07-11

Authors:

Patel, Pryank; Lian, Lu-Yun; Morgan, Alan; Burgoyne, Robert

Citation:

Citation: Patel, Pryank; Prescott, Gerald; Burgoyne, Robert; Lian, Lu-Yun; Morgan, Alan. "Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch" Structure 24, 1380-1386 (2016).
PubMed: 27452402

Assembly members:

Assembly members:
DnaJ_domain_of_cysteine-string_protein, polymer, 105 residues, 11904.328 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: pE-Sumo Pro Kan

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DnaJ_domain_of_cysteine-string_protein: MRSPGMADQRQRSLSTSGES LYHVLGLDKNATSDDIKKSY RKLALKYHPDKNPDNPEAAD KFKEINNAHAILTDATKRNI YDKYGSLGLYVAEQFGEENV NTYFV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	410
15N chemical shifts	104
1H chemical shifts	647

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 105 residues - 11904.328 Da.

1

MET

ARG

SER

PRO

GLY

MET

ALA

ASP

GLN

ARG

2

GLN

ARG

SER

LEU

SER

THR

SER

GLY

GLU

SER

3

LEU

TYR

HIS

VAL

LEU

GLY

LEU

ASP

LYS

ASN

4

ALA

THR

SER

ASP

ILE

LYS

SER

TYR

5

ARG

LYS

LEU

ALA

LEU

LYS

TYR

HIS

PRO

ASP

6

LYS

ASN

PRO

ASP

ASN

PRO

GLU

ALA

ASP

7

LYS

PHE

LYS

GLU

ILE

ASN

ALA

HIS

ALA

8

ILE

LEU

THR

ASP

ALA

THR

LYS

ARG

ASN

ILE

9

TYR

ASP

LYS

TYR

GLY

SER

LEU

GLY

LEU

TYR

10

VAL

ALA

GLU

GLN

PHE

GLY

GLU

ASN

VAL

11

ASN

THR

TYR

PHE

VAL

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
3D HBHANH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	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
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

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BMRB Entry 25515

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: