BMRB Entry 19163

Name: The solution structure of the J-domain of human DnaJA1
Published: 2013-06-24

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PDB ID: 2m6y
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19163
MolProbity Validation Chart

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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:

The solution structure of the J-domain of human DnaJA1

Deposition date:

2013-04-14

Original release date:

2013-06-24

Authors:

Stark, Jaime; Mehla, Kamiya; Chaika, Nina; Acton, Thomas; Xiao, Rong; Singh, Pankaj; Montelione, Gaetano; Powers, Robert

Citation:

Citation: Stark, Jaime; Mehla, Kamiya; Chaika, Nina; Acton, Thomas; Xiao, Rong; Singh, Pankaj; Montelione, Gaetano; Powers, Robert. "Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer." Biochemistry 53, 1360-1372 (2014).
PubMed: 24512202

Assembly members:

Assembly members:
J-domain_of_DnaJA1, polymer, 77 residues, 9095.388 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: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
J-domain_of_DnaJA1: MGHHHHHHSHMVKETTYYDV LGVKPNATQEELKKAYRKLA LKYHPDKNPNEGEKFKQISQ AYEVLSDAKKRELYDKG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	277
15N chemical shifts	63
1H chemical shifts	430

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	J-domain of human DnaJA1	1

Entities:

Entity 1, J-domain of human DnaJA1 77 residues - 9095.388 Da.

Residues 1-10 represent a non-native affinity tag

1

MET

GLY

HIS

SER

HIS

2

MET

VAL

LYS

GLU

THR

TYR

ASP

VAL

3

LEU

GLY

VAL

LYS

PRO

ASN

ALA

THR

GLN

GLU

4

GLU

LEU

LYS

ALA

TYR

ARG

LYS

LEU

ALA

5

LEU

LYS

TYR

HIS

PRO

ASP

LYS

ASN

PRO

ASN

6

GLU

GLY

GLU

LYS

PHE

LYS

GLN

ILE

SER

GLN

7

ALA

TYR

GLU

VAL

LEU

SER

ASP

ALA

LYS

8

ARG

GLU

LEU

TYR

ASP

LYS

GLY

Samples:

HR3099K.006: J-domain of DnaJA1, [U-13C; U-15N], 1.03 mM; MES 20 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; DSS 50 uM

sample_conditions_1: ionic strength: 125 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	HR3099K.006	isotropic	sample_conditions_1
2D 1H-13C HSQC	HR3099K.006	isotropic	sample_conditions_1
3D HNCO	HR3099K.006	isotropic	sample_conditions_1
3D HN(CA)CO	HR3099K.006	isotropic	sample_conditions_1
3D HNCA	HR3099K.006	isotropic	sample_conditions_1
3D HN(CO)CA	HR3099K.006	isotropic	sample_conditions_1
3D CBCA(CO)NH	HR3099K.006	isotropic	sample_conditions_1
3D CBCANH	HR3099K.006	isotropic	sample_conditions_1
3D HNHA	HR3099K.006	isotropic	sample_conditions_1
3D HBHA(CO)NH	HR3099K.006	isotropic	sample_conditions_1
3D CC(CO)NH	HR3099K.006	isotropic	sample_conditions_1
3D HCC(CO)NH	HR3099K.006	isotropic	sample_conditions_1
3D HCCH-TOCSY	HR3099K.006	isotropic	sample_conditions_1
3D HCCH-COSY	HR3099K.006	isotropic	sample_conditions_1
3D 1H-15N NOESY	HR3099K.006	isotropic	sample_conditions_1
3D 1H-13C NOESY	HR3099K.006	isotropic	sample_conditions_1

Software:

ANALYSIS v2.2.2, CCPN - chemical shift assignment, data analysis, peak picking

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

PSVS, Bhattacharya and Montelione - structure validation

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz

BMRB	18190
PDB	2LO1 2M6Y
DBJ	BAA02656 BAC38744 BAC82111 BAD82815 BAE26788
EMBL	CAI29674
GB	AAA98855 AAC37517 AAC78597 AAH08182 AAH57876
PIR	S34632
REF	NP_001015637 NP_001127102 NP_001158143 NP_001158144 NP_001231092
SP	P31689 P63036 P63037 Q5E954 Q5NVI9
TPG	DAA12974 DAA26671
AlphaFold	P31689 P63036 P63037 Q5E954 Q5NVI9