BMRB Entry 19163

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):

Data sets:
Data typeCount
13C chemical shifts277
15N chemical shifts63
1H chemical shifts430

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1J-domain of human DnaJA11

Entities:

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

Residues 1-10 represent a non-native affinity tag

1   METGLYHISHISHISHISHISHISSERHIS
2   METVALLYSGLUTHRTHRTYRTYRASPVAL
3   LEUGLYVALLYSPROASNALATHRGLNGLU
4   GLULEULYSLYSALATYRARGLYSLEUALA
5   LEULYSTYRHISPROASPLYSASNPROASN
6   GLUGLYGLULYSPHELYSGLNILESERGLN
7   ALATYRGLUVALLEUSERASPALALYSLYS
8   ARGGLULEUTYRASPLYSGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR3099K.006isotropicsample_conditions_1
2D 1H-13C HSQCHR3099K.006isotropicsample_conditions_1
3D HNCOHR3099K.006isotropicsample_conditions_1
3D HN(CA)COHR3099K.006isotropicsample_conditions_1
3D HNCAHR3099K.006isotropicsample_conditions_1
3D HN(CO)CAHR3099K.006isotropicsample_conditions_1
3D CBCA(CO)NHHR3099K.006isotropicsample_conditions_1
3D CBCANHHR3099K.006isotropicsample_conditions_1
3D HNHAHR3099K.006isotropicsample_conditions_1
3D HBHA(CO)NHHR3099K.006isotropicsample_conditions_1
3D CC(CO)NHHR3099K.006isotropicsample_conditions_1
3D HCC(CO)NHHR3099K.006isotropicsample_conditions_1
3D HCCH-TOCSYHR3099K.006isotropicsample_conditions_1
3D HCCH-COSYHR3099K.006isotropicsample_conditions_1
3D 1H-15N NOESYHR3099K.006isotropicsample_conditions_1
3D 1H-13C NOESYHR3099K.006isotropicsample_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

Related Database Links:

BMRB 18190
PDB
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

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