BMRB Entry 17293

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17293

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Title:
Solution structure of human J-protein co-chaperone Dph4
Deposition date:
2010-11-11
Original release date:
2012-01-09
Authors:
Thakur, Anushikha; Chitoor, Balasubramanyam; Atreya, Hanudatta; Silva, Patrick
Citation:

Citation: Thakur, Anushikha; Chitoor, Balasubramanyam; Goswami, Arvind; Pareek, Gautam; Atreya, Hanudatta. "Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4."  J. Biol. Chem. 287, 13194-13205 (2012).
PubMed: 22367199

Assembly members:

Assembly members:
Dph4, polymer, 155 residues, Formula weight is not available
ZN, non-polymer, 65.409 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: pET3A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dph4: MMAVEQMPKKDWYSILGADP SANISDLKQKYQKLILMYHP DKQSTDVPAGTVEECVQKFI EIDQAWKILGNEETKREYDL QRCEDDLRNVGPVDAQVYLE EMSWNEGDHSFYLSCRCGGK YSVSKDEAEEVSLISCDTCS LIIELLHYNHHHHHH

Data sets:
Data typeCount
13C chemical shifts524
15N chemical shifts135
1H chemical shifts932

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Dph41
2Zn2

Entities:

Entity 1, Dph4 155 residues - Formula weight is not available

1   METMETALAVALGLUGLNMETPROLYSLYS
2   ASPTRPTYRSERILELEUGLYALAASPPRO
3   SERALAASNILESERASPLEULYSGLNLYS
4   TYRGLNLYSLEUILELEUMETTYRHISPRO
5   ASPLYSGLNSERTHRASPVALPROALAGLY
6   THRVALGLUGLUCYSVALGLNLYSPHEILE
7   GLUILEASPGLNALATRPLYSILELEUGLY
8   ASNGLUGLUTHRLYSARGGLUTYRASPLEU
9   GLNARGCYSGLUASPASPLEUARGASNVAL
10   GLYPROVALASPALAGLNVALTYRLEUGLU
11   GLUMETSERTRPASNGLUGLYASPHISSER
12   PHETYRLEUSERCYSARGCYSGLYGLYLYS
13   TYRSERVALSERLYSASPGLUALAGLUGLU
14   VALSERLEUILESERCYSASPTHRCYSSER
15   LEUILEILEGLULEULEUHISTYRASNHIS
16   HISHISHISHISHIS

Entity 2, Zn - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Dph4 polypeptide, [U-13C; U-15N], 1 mM; Zn 1 mM; sodium chloride 80 mM; TRIS 20 mM; H2O 90%; D2O 10%

sample_2: Dph4 polypeptide 1 mM; Zn 1 mM; sodium chloride 80 mM; TRIS 20 mM; D2O 100%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D H(CCO)NH-TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D (H)C(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_1isotropicsample_conditions_1
GFT (3,2)D HA(CA)CO(N)Hsample_1isotropicsample_conditions_1
GFT (4,3)D NOESY-HCCHsample_2isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, peak picking

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

xwinnmr, Bruker Biospin - collection

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAF82354
GB AAH36571 AAH63804 AIC62319 EAW68242 EAW68243
REF NP_859057 XP_001141859 XP_003254415 XP_003830465 XP_009244778
SP Q6P3W2
AlphaFold Q6P3W2

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